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You searched for subject:(substrate specificity). Showing records 1 – 30 of 63 total matches.

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Cornell University

1. Samuel Yesudasan, Teddy. WHAT MAKES A RED POTATO RED: IDENTIFYING AMINO ACIDS THAT INFLUENCE SUBSTRATE SPECIFICITY OF POTATO DFR .

Degree: 2019, Cornell University

 Pigmented potatoes (Solanum tuberosum L.) are a rich source of anthocyanin pigments. Dihydroflavonol 4-reductase (DFR) is a rate limiting enzyme in the flavonoid pathway that… (more)

Subjects/Keywords: Anthocyanins; DFR; Red potatoes; Substrate Specificity; Biology; Agriculture; Plant sciences

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Samuel Yesudasan, T. (2019). WHAT MAKES A RED POTATO RED: IDENTIFYING AMINO ACIDS THAT INFLUENCE SUBSTRATE SPECIFICITY OF POTATO DFR . (Thesis). Cornell University. Retrieved from http://hdl.handle.net/1813/67318

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Samuel Yesudasan, Teddy. “WHAT MAKES A RED POTATO RED: IDENTIFYING AMINO ACIDS THAT INFLUENCE SUBSTRATE SPECIFICITY OF POTATO DFR .” 2019. Thesis, Cornell University. Accessed January 24, 2020. http://hdl.handle.net/1813/67318.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Samuel Yesudasan, Teddy. “WHAT MAKES A RED POTATO RED: IDENTIFYING AMINO ACIDS THAT INFLUENCE SUBSTRATE SPECIFICITY OF POTATO DFR .” 2019. Web. 24 Jan 2020.

Vancouver:

Samuel Yesudasan T. WHAT MAKES A RED POTATO RED: IDENTIFYING AMINO ACIDS THAT INFLUENCE SUBSTRATE SPECIFICITY OF POTATO DFR . [Internet] [Thesis]. Cornell University; 2019. [cited 2020 Jan 24]. Available from: http://hdl.handle.net/1813/67318.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Samuel Yesudasan T. WHAT MAKES A RED POTATO RED: IDENTIFYING AMINO ACIDS THAT INFLUENCE SUBSTRATE SPECIFICITY OF POTATO DFR . [Thesis]. Cornell University; 2019. Available from: http://hdl.handle.net/1813/67318

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation


Northeastern University

2. Kenton, Nathaniel Thomas. Design and synthesis of methionine analogues for the enzymatic synthesis of S-adenosyl-methionine analogues: tools for the analysis of methyltransferase substrate specificity.

Degree: MS, Department of Chemistry and Chemical Biology, 2012, Northeastern University

 Determining enzyme-substrate specificity is tantamount to understanding biology on a molecular level. In medicinal chemistry, for example, this is often the crucial starting point from… (more)

Subjects/Keywords: chemistry; adomet; analogue; methyltransferase; specificity; substrate; Methionine; Enzymes - Synthesis; Analytical Chemistry

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APA (6th Edition):

Kenton, N. T. (2012). Design and synthesis of methionine analogues for the enzymatic synthesis of S-adenosyl-methionine analogues: tools for the analysis of methyltransferase substrate specificity. (Masters Thesis). Northeastern University. Retrieved from http://hdl.handle.net/2047/d20002527

Chicago Manual of Style (16th Edition):

Kenton, Nathaniel Thomas. “Design and synthesis of methionine analogues for the enzymatic synthesis of S-adenosyl-methionine analogues: tools for the analysis of methyltransferase substrate specificity.” 2012. Masters Thesis, Northeastern University. Accessed January 24, 2020. http://hdl.handle.net/2047/d20002527.

MLA Handbook (7th Edition):

Kenton, Nathaniel Thomas. “Design and synthesis of methionine analogues for the enzymatic synthesis of S-adenosyl-methionine analogues: tools for the analysis of methyltransferase substrate specificity.” 2012. Web. 24 Jan 2020.

Vancouver:

Kenton NT. Design and synthesis of methionine analogues for the enzymatic synthesis of S-adenosyl-methionine analogues: tools for the analysis of methyltransferase substrate specificity. [Internet] [Masters thesis]. Northeastern University; 2012. [cited 2020 Jan 24]. Available from: http://hdl.handle.net/2047/d20002527.

Council of Science Editors:

Kenton NT. Design and synthesis of methionine analogues for the enzymatic synthesis of S-adenosyl-methionine analogues: tools for the analysis of methyltransferase substrate specificity. [Masters Thesis]. Northeastern University; 2012. Available from: http://hdl.handle.net/2047/d20002527


University of Southern California

3. Mitra, Sayantan. Development, synthesis and applications of highly sensitive fluorescent probes for studying protein tyrosine phosphatases.

Degree: PhD, Chemistry, 2009, University of Southern California

 Protein tyrosine phosphatases (PTPs) constitute an important class of enzymes that are involved in various cellular processes such as mitogenesis, cell growth, signal transduction, immune… (more)

Subjects/Keywords: fluorescence; protein tyrosine phosphatases; coumarin; fluorescent amino acids; PTP substrate selectivity; substrate specificity; selective PTP inhibitors; cellular imaging

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APA (6th Edition):

Mitra, S. (2009). Development, synthesis and applications of highly sensitive fluorescent probes for studying protein tyrosine phosphatases. (Doctoral Dissertation). University of Southern California. Retrieved from http://digitallibrary.usc.edu/cdm/compoundobject/collection/p15799coll127/id/518695/rec/1969

Chicago Manual of Style (16th Edition):

Mitra, Sayantan. “Development, synthesis and applications of highly sensitive fluorescent probes for studying protein tyrosine phosphatases.” 2009. Doctoral Dissertation, University of Southern California. Accessed January 24, 2020. http://digitallibrary.usc.edu/cdm/compoundobject/collection/p15799coll127/id/518695/rec/1969.

MLA Handbook (7th Edition):

Mitra, Sayantan. “Development, synthesis and applications of highly sensitive fluorescent probes for studying protein tyrosine phosphatases.” 2009. Web. 24 Jan 2020.

Vancouver:

Mitra S. Development, synthesis and applications of highly sensitive fluorescent probes for studying protein tyrosine phosphatases. [Internet] [Doctoral dissertation]. University of Southern California; 2009. [cited 2020 Jan 24]. Available from: http://digitallibrary.usc.edu/cdm/compoundobject/collection/p15799coll127/id/518695/rec/1969.

Council of Science Editors:

Mitra S. Development, synthesis and applications of highly sensitive fluorescent probes for studying protein tyrosine phosphatases. [Doctoral Dissertation]. University of Southern California; 2009. Available from: http://digitallibrary.usc.edu/cdm/compoundobject/collection/p15799coll127/id/518695/rec/1969

4. ANUPRIYA GOPALSAMY. CHARACTERIZATION OF THE E3 UBIQUITIN LIGASE SIAH2 AS AN ANTI-CANCER TARGET.

Degree: 2013, National University of Singapore

Subjects/Keywords: Siah1; Siah2; Substrate Binding Domain; PHD3; Inhibitors; Substrate specificity

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APA (6th Edition):

GOPALSAMY, A. (2013). CHARACTERIZATION OF THE E3 UBIQUITIN LIGASE SIAH2 AS AN ANTI-CANCER TARGET. (Thesis). National University of Singapore. Retrieved from http://scholarbank.nus.edu.sg/handle/10635/53741

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

GOPALSAMY, ANUPRIYA. “CHARACTERIZATION OF THE E3 UBIQUITIN LIGASE SIAH2 AS AN ANTI-CANCER TARGET.” 2013. Thesis, National University of Singapore. Accessed January 24, 2020. http://scholarbank.nus.edu.sg/handle/10635/53741.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

GOPALSAMY, ANUPRIYA. “CHARACTERIZATION OF THE E3 UBIQUITIN LIGASE SIAH2 AS AN ANTI-CANCER TARGET.” 2013. Web. 24 Jan 2020.

Vancouver:

GOPALSAMY A. CHARACTERIZATION OF THE E3 UBIQUITIN LIGASE SIAH2 AS AN ANTI-CANCER TARGET. [Internet] [Thesis]. National University of Singapore; 2013. [cited 2020 Jan 24]. Available from: http://scholarbank.nus.edu.sg/handle/10635/53741.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

GOPALSAMY A. CHARACTERIZATION OF THE E3 UBIQUITIN LIGASE SIAH2 AS AN ANTI-CANCER TARGET. [Thesis]. National University of Singapore; 2013. Available from: http://scholarbank.nus.edu.sg/handle/10635/53741

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation


University of Oulu

5. Meriläinen, G. (Gitte). Structural and enzymological studies of the thiolase enzymes.

Degree: 2009, University of Oulu

 Abstract In the cells, the last step of the beta-oxidation cycle, aiming at the degradation of fatty acids, is catalyzed by the enzyme named thiolase.… (more)

Subjects/Keywords: Acetyl-CoA C-acetyltransferase; Coenzyme A; X-ray crystallography; acyltransferases; kinetics; substrate specificity

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APA (6th Edition):

Meriläinen, G. (. (2009). Structural and enzymological studies of the thiolase enzymes. (Doctoral Dissertation). University of Oulu. Retrieved from http://urn.fi/urn:isbn:9789514291982

Chicago Manual of Style (16th Edition):

Meriläinen, G (Gitte). “Structural and enzymological studies of the thiolase enzymes.” 2009. Doctoral Dissertation, University of Oulu. Accessed January 24, 2020. http://urn.fi/urn:isbn:9789514291982.

MLA Handbook (7th Edition):

Meriläinen, G (Gitte). “Structural and enzymological studies of the thiolase enzymes.” 2009. Web. 24 Jan 2020.

Vancouver:

Meriläinen G(. Structural and enzymological studies of the thiolase enzymes. [Internet] [Doctoral dissertation]. University of Oulu; 2009. [cited 2020 Jan 24]. Available from: http://urn.fi/urn:isbn:9789514291982.

Council of Science Editors:

Meriläinen G(. Structural and enzymological studies of the thiolase enzymes. [Doctoral Dissertation]. University of Oulu; 2009. Available from: http://urn.fi/urn:isbn:9789514291982


Duquesne University

6. Henkel, Matthew A. Evaluation of PilO Substrate Specificity Using Normally Non-Glycosylated Proteins in Pseudomonas Aeruginosa.

Degree: MS, Biological Sciences, 2009, Duquesne University

 P. aeruginosa 1244 (PA1244) possesses an O-linked glycosylation system by which the glycosyltransferase, PilO, transfers a single preassembled O-antigen repeating unit to the C-terminal serine… (more)

Subjects/Keywords: substrate specificity; PilO; peptide extension; Pseudomonas aeruginosa; O-linked glycosylation; vaccine design

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APA (6th Edition):

Henkel, M. A. (2009). Evaluation of PilO Substrate Specificity Using Normally Non-Glycosylated Proteins in Pseudomonas Aeruginosa. (Masters Thesis). Duquesne University. Retrieved from https://dsc.duq.edu/etd/646

Chicago Manual of Style (16th Edition):

Henkel, Matthew A. “Evaluation of PilO Substrate Specificity Using Normally Non-Glycosylated Proteins in Pseudomonas Aeruginosa.” 2009. Masters Thesis, Duquesne University. Accessed January 24, 2020. https://dsc.duq.edu/etd/646.

MLA Handbook (7th Edition):

Henkel, Matthew A. “Evaluation of PilO Substrate Specificity Using Normally Non-Glycosylated Proteins in Pseudomonas Aeruginosa.” 2009. Web. 24 Jan 2020.

Vancouver:

Henkel MA. Evaluation of PilO Substrate Specificity Using Normally Non-Glycosylated Proteins in Pseudomonas Aeruginosa. [Internet] [Masters thesis]. Duquesne University; 2009. [cited 2020 Jan 24]. Available from: https://dsc.duq.edu/etd/646.

Council of Science Editors:

Henkel MA. Evaluation of PilO Substrate Specificity Using Normally Non-Glycosylated Proteins in Pseudomonas Aeruginosa. [Masters Thesis]. Duquesne University; 2009. Available from: https://dsc.duq.edu/etd/646


The Ohio State University

7. Selner, Nicholas. PROFILING THE INTRINSIC SEQUENCE SPECIFICITY OF PROTEIN TYROSINE PHOSPHATASES.

Degree: PhD, Chemistry, 2013, The Ohio State University

 Many signaling pathways are mediated by protein tyrosine phosphorylation. Regulation of protein tyrosine phosphorylation is balanced between protein tyrosine kinases (PTKs) and protein tyrosine phosphatases… (more)

Subjects/Keywords: Chemistry; Biochemistry; Combinatorial library, catalytic activity, kinetics, phosphotyrosine, phosphatase, PTP, substrate specificity

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APA (6th Edition):

Selner, N. (2013). PROFILING THE INTRINSIC SEQUENCE SPECIFICITY OF PROTEIN TYROSINE PHOSPHATASES. (Doctoral Dissertation). The Ohio State University. Retrieved from http://rave.ohiolink.edu/etdc/view?acc_num=osu1384269733

Chicago Manual of Style (16th Edition):

Selner, Nicholas. “PROFILING THE INTRINSIC SEQUENCE SPECIFICITY OF PROTEIN TYROSINE PHOSPHATASES.” 2013. Doctoral Dissertation, The Ohio State University. Accessed January 24, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=osu1384269733.

MLA Handbook (7th Edition):

Selner, Nicholas. “PROFILING THE INTRINSIC SEQUENCE SPECIFICITY OF PROTEIN TYROSINE PHOSPHATASES.” 2013. Web. 24 Jan 2020.

Vancouver:

Selner N. PROFILING THE INTRINSIC SEQUENCE SPECIFICITY OF PROTEIN TYROSINE PHOSPHATASES. [Internet] [Doctoral dissertation]. The Ohio State University; 2013. [cited 2020 Jan 24]. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1384269733.

Council of Science Editors:

Selner N. PROFILING THE INTRINSIC SEQUENCE SPECIFICITY OF PROTEIN TYROSINE PHOSPHATASES. [Doctoral Dissertation]. The Ohio State University; 2013. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1384269733


University of Ottawa

8. Hari, Taylor P. A. Chemoenzymatic Synthesis of Polyketide Natural Products .

Degree: 2018, University of Ottawa

 Polyketide secondary metabolites constitute a structurally-diverse and clinically-important family of natural products. The wide range of biological activities represented by these substrates have contributed to… (more)

Subjects/Keywords: Polyketide; Natural products; Neopeltolide; Oxa-conjugate addition; Tetrahydropyran; Thioesterase; Macrocyclization; Substrate-specificity

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APA (6th Edition):

Hari, T. P. A. (2018). Chemoenzymatic Synthesis of Polyketide Natural Products . (Thesis). University of Ottawa. Retrieved from http://hdl.handle.net/10393/37220

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Hari, Taylor P A. “Chemoenzymatic Synthesis of Polyketide Natural Products .” 2018. Thesis, University of Ottawa. Accessed January 24, 2020. http://hdl.handle.net/10393/37220.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Hari, Taylor P A. “Chemoenzymatic Synthesis of Polyketide Natural Products .” 2018. Web. 24 Jan 2020.

Vancouver:

Hari TPA. Chemoenzymatic Synthesis of Polyketide Natural Products . [Internet] [Thesis]. University of Ottawa; 2018. [cited 2020 Jan 24]. Available from: http://hdl.handle.net/10393/37220.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Hari TPA. Chemoenzymatic Synthesis of Polyketide Natural Products . [Thesis]. University of Ottawa; 2018. Available from: http://hdl.handle.net/10393/37220

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation


Australian National University

9. Lim, Jo Leen. Protein Engineering of Escherichia coli β-glucuronidase .

Degree: 2017, Australian National University

 This thesis describes engineering studies with the Escherichia coli β-glucuronidase enzyme (E. coli β-GUS) that catalyzes the hydrolysis of D-glucuronic acids (glycone) that are conjugated… (more)

Subjects/Keywords: Protein Engineering; Escherichia coli β-glucuronidase; Stability; Evolvability; Substrate specificity; n-octyl β-D-thioglucopyranoside

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APA (6th Edition):

Lim, J. L. (2017). Protein Engineering of Escherichia coli β-glucuronidase . (Thesis). Australian National University. Retrieved from http://hdl.handle.net/1885/136125

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Lim, Jo Leen. “Protein Engineering of Escherichia coli β-glucuronidase .” 2017. Thesis, Australian National University. Accessed January 24, 2020. http://hdl.handle.net/1885/136125.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Lim, Jo Leen. “Protein Engineering of Escherichia coli β-glucuronidase .” 2017. Web. 24 Jan 2020.

Vancouver:

Lim JL. Protein Engineering of Escherichia coli β-glucuronidase . [Internet] [Thesis]. Australian National University; 2017. [cited 2020 Jan 24]. Available from: http://hdl.handle.net/1885/136125.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Lim JL. Protein Engineering of Escherichia coli β-glucuronidase . [Thesis]. Australian National University; 2017. Available from: http://hdl.handle.net/1885/136125

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation


Universitat Autònoma de Barcelona

10. Garcia Pardo, Javier. Structural and functional characterization of regulatory metallocarboxypeptidases: Studies on human carboxypeptidases D and Z, and the transthyretin-like domain.

Degree: Departament de Bioquímica i Biologia Molecular, 2015, Universitat Autònoma de Barcelona

 Metallocarboxypeptidases (MCPs) are zinc-dependent enzymes that cleave single amino acids from the C termini of proteins and peptides. The first MCP to be identified was… (more)

Subjects/Keywords: Carboxypeptidases; Carboxipeptidasa; Enzymology; Enzimologia; Substrate specificity; Especificitat de substrat; Especificidad de substrato; Ciències Experimentals; 577

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APA (6th Edition):

Garcia Pardo, J. (2015). Structural and functional characterization of regulatory metallocarboxypeptidases: Studies on human carboxypeptidases D and Z, and the transthyretin-like domain. (Thesis). Universitat Autònoma de Barcelona. Retrieved from http://hdl.handle.net/10803/319703

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Garcia Pardo, Javier. “Structural and functional characterization of regulatory metallocarboxypeptidases: Studies on human carboxypeptidases D and Z, and the transthyretin-like domain.” 2015. Thesis, Universitat Autònoma de Barcelona. Accessed January 24, 2020. http://hdl.handle.net/10803/319703.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Garcia Pardo, Javier. “Structural and functional characterization of regulatory metallocarboxypeptidases: Studies on human carboxypeptidases D and Z, and the transthyretin-like domain.” 2015. Web. 24 Jan 2020.

Vancouver:

Garcia Pardo J. Structural and functional characterization of regulatory metallocarboxypeptidases: Studies on human carboxypeptidases D and Z, and the transthyretin-like domain. [Internet] [Thesis]. Universitat Autònoma de Barcelona; 2015. [cited 2020 Jan 24]. Available from: http://hdl.handle.net/10803/319703.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Garcia Pardo J. Structural and functional characterization of regulatory metallocarboxypeptidases: Studies on human carboxypeptidases D and Z, and the transthyretin-like domain. [Thesis]. Universitat Autònoma de Barcelona; 2015. Available from: http://hdl.handle.net/10803/319703

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation


University of Lethbridge

11. Van Herk, Peter. Specificity of a novel myo-inositol phosphatase towards less-phosphorylated myo-inositol phosphates .

Degree: 2014, University of Lethbridge

 Protein tyrosine phosphatase-like myo-inositol phosphatases (PTPLPs) remove phosphoryl groups from phosphorylated myo-inositols (IPs) via largely ordered pathways. To understand the substrate specificity of this enzyme… (more)

Subjects/Keywords: Crystallography; Biochemistry; Enzyme; Phosphatase; Myo-Inositol; PTPLP; Fluorescence Spectroscopy; Kinetic; Substrate Specificity; Physical Biochemistry

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APA (6th Edition):

Van Herk, P. (2014). Specificity of a novel myo-inositol phosphatase towards less-phosphorylated myo-inositol phosphates . (Thesis). University of Lethbridge. Retrieved from http://hdl.handle.net/10133/3638

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Van Herk, Peter. “Specificity of a novel myo-inositol phosphatase towards less-phosphorylated myo-inositol phosphates .” 2014. Thesis, University of Lethbridge. Accessed January 24, 2020. http://hdl.handle.net/10133/3638.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Van Herk, Peter. “Specificity of a novel myo-inositol phosphatase towards less-phosphorylated myo-inositol phosphates .” 2014. Web. 24 Jan 2020.

Vancouver:

Van Herk P. Specificity of a novel myo-inositol phosphatase towards less-phosphorylated myo-inositol phosphates . [Internet] [Thesis]. University of Lethbridge; 2014. [cited 2020 Jan 24]. Available from: http://hdl.handle.net/10133/3638.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Van Herk P. Specificity of a novel myo-inositol phosphatase towards less-phosphorylated myo-inositol phosphates . [Thesis]. University of Lethbridge; 2014. Available from: http://hdl.handle.net/10133/3638

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation


University of California – Berkeley

12. Chen, Janice Sha. Mechanisms and applications of DNA-targeting CRISPR interference proteins.

Degree: Molecular & Cell Biology, 2018, University of California – Berkeley

 The ongoing battle between bacteria and phage has influenced the evolution of complex defense pathways. In bacteria and archaea, clustered regularly interspaced short palindromic repeats… (more)

Subjects/Keywords: Biochemistry; Molecular biology; CRISPR; endonucleases; enzymology; gene editing; nucleic acids; substrate specificity

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APA (6th Edition):

Chen, J. S. (2018). Mechanisms and applications of DNA-targeting CRISPR interference proteins. (Thesis). University of California – Berkeley. Retrieved from http://www.escholarship.org/uc/item/70p7b5fm

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Chen, Janice Sha. “Mechanisms and applications of DNA-targeting CRISPR interference proteins.” 2018. Thesis, University of California – Berkeley. Accessed January 24, 2020. http://www.escholarship.org/uc/item/70p7b5fm.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Chen, Janice Sha. “Mechanisms and applications of DNA-targeting CRISPR interference proteins.” 2018. Web. 24 Jan 2020.

Vancouver:

Chen JS. Mechanisms and applications of DNA-targeting CRISPR interference proteins. [Internet] [Thesis]. University of California – Berkeley; 2018. [cited 2020 Jan 24]. Available from: http://www.escholarship.org/uc/item/70p7b5fm.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Chen JS. Mechanisms and applications of DNA-targeting CRISPR interference proteins. [Thesis]. University of California – Berkeley; 2018. Available from: http://www.escholarship.org/uc/item/70p7b5fm

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation


University of Michigan

13. Tippett, Larry D. Substrate Specificity of the Widely Expressed Subtilisin-like Proprotein Convertases (SPCs): A Role for the Substrate Amino Acid Directly Downstream of the Endoproteolytic Cleavage Site.

Degree: Master's, College of Arts and Sciences: Biology, 2001, University of Michigan

Substrate specificity was investigated among four of the eukaryotic, widely expressed subtilisin-like proprotein convertases (SPCs): furin, PACE4, PC5, and PC7. Through site-directed mutagenesis, amino acid… (more)

Subjects/Keywords: furin; PACE4; PC5; PC7; substrate specificity

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APA (6th Edition):

Tippett, L. D. (2001). Substrate Specificity of the Widely Expressed Subtilisin-like Proprotein Convertases (SPCs): A Role for the Substrate Amino Acid Directly Downstream of the Endoproteolytic Cleavage Site. (Masters Thesis). University of Michigan. Retrieved from http://hdl.handle.net/2027.42/117758

Chicago Manual of Style (16th Edition):

Tippett, Larry D. “Substrate Specificity of the Widely Expressed Subtilisin-like Proprotein Convertases (SPCs): A Role for the Substrate Amino Acid Directly Downstream of the Endoproteolytic Cleavage Site.” 2001. Masters Thesis, University of Michigan. Accessed January 24, 2020. http://hdl.handle.net/2027.42/117758.

MLA Handbook (7th Edition):

Tippett, Larry D. “Substrate Specificity of the Widely Expressed Subtilisin-like Proprotein Convertases (SPCs): A Role for the Substrate Amino Acid Directly Downstream of the Endoproteolytic Cleavage Site.” 2001. Web. 24 Jan 2020.

Vancouver:

Tippett LD. Substrate Specificity of the Widely Expressed Subtilisin-like Proprotein Convertases (SPCs): A Role for the Substrate Amino Acid Directly Downstream of the Endoproteolytic Cleavage Site. [Internet] [Masters thesis]. University of Michigan; 2001. [cited 2020 Jan 24]. Available from: http://hdl.handle.net/2027.42/117758.

Council of Science Editors:

Tippett LD. Substrate Specificity of the Widely Expressed Subtilisin-like Proprotein Convertases (SPCs): A Role for the Substrate Amino Acid Directly Downstream of the Endoproteolytic Cleavage Site. [Masters Thesis]. University of Michigan; 2001. Available from: http://hdl.handle.net/2027.42/117758


Georgia State University

14. Chen, Yan. The Structure and Function Study of Three Metalloenzymes That Utilize Three Histidines as Metal Ligands.

Degree: PhD, Chemistry, 2013, Georgia State University

  The function of the metalloenzymes is mainly determined by four structural features: the metal core, the metal binding motif, the second sphere residues in… (more)

Subjects/Keywords: Cysteamine dioxygenase; Cysteine dioxygenase; ACMSD; Metal binding motif; Metal selectivity; Substrate specificity

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APA (6th Edition):

Chen, Y. (2013). The Structure and Function Study of Three Metalloenzymes That Utilize Three Histidines as Metal Ligands. (Doctoral Dissertation). Georgia State University. Retrieved from https://scholarworks.gsu.edu/chemistry_diss/86

Chicago Manual of Style (16th Edition):

Chen, Yan. “The Structure and Function Study of Three Metalloenzymes That Utilize Three Histidines as Metal Ligands.” 2013. Doctoral Dissertation, Georgia State University. Accessed January 24, 2020. https://scholarworks.gsu.edu/chemistry_diss/86.

MLA Handbook (7th Edition):

Chen, Yan. “The Structure and Function Study of Three Metalloenzymes That Utilize Three Histidines as Metal Ligands.” 2013. Web. 24 Jan 2020.

Vancouver:

Chen Y. The Structure and Function Study of Three Metalloenzymes That Utilize Three Histidines as Metal Ligands. [Internet] [Doctoral dissertation]. Georgia State University; 2013. [cited 2020 Jan 24]. Available from: https://scholarworks.gsu.edu/chemistry_diss/86.

Council of Science Editors:

Chen Y. The Structure and Function Study of Three Metalloenzymes That Utilize Three Histidines as Metal Ligands. [Doctoral Dissertation]. Georgia State University; 2013. Available from: https://scholarworks.gsu.edu/chemistry_diss/86


University of Guelph

15. Rea, Kevin. Multifaceted in vivo and in vitro Characterization of cis-Prenyltransferase 5 from Solanum lycopersicum .

Degree: 2017, University of Guelph

 The widespread occurrence of polyprenols throughout the plant kingdom is well documented. These compounds are believed to be assembled by a class of enzymes designated… (more)

Subjects/Keywords: isoprenoids; polyisoprenoids; cis-prenyltransferase; CPT; polyprenol; dolichol; solanum lycopersicum; tomato; prenyltransferase; functional complementation; serial dilution; CPT5; rer2; substrate specificity; preferred substrate; enzyme characterization; carotenoids

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APA (6th Edition):

Rea, K. (2017). Multifaceted in vivo and in vitro Characterization of cis-Prenyltransferase 5 from Solanum lycopersicum . (Thesis). University of Guelph. Retrieved from https://atrium.lib.uoguelph.ca/xmlui/handle/10214/11614

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Rea, Kevin. “Multifaceted in vivo and in vitro Characterization of cis-Prenyltransferase 5 from Solanum lycopersicum .” 2017. Thesis, University of Guelph. Accessed January 24, 2020. https://atrium.lib.uoguelph.ca/xmlui/handle/10214/11614.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Rea, Kevin. “Multifaceted in vivo and in vitro Characterization of cis-Prenyltransferase 5 from Solanum lycopersicum .” 2017. Web. 24 Jan 2020.

Vancouver:

Rea K. Multifaceted in vivo and in vitro Characterization of cis-Prenyltransferase 5 from Solanum lycopersicum . [Internet] [Thesis]. University of Guelph; 2017. [cited 2020 Jan 24]. Available from: https://atrium.lib.uoguelph.ca/xmlui/handle/10214/11614.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Rea K. Multifaceted in vivo and in vitro Characterization of cis-Prenyltransferase 5 from Solanum lycopersicum . [Thesis]. University of Guelph; 2017. Available from: https://atrium.lib.uoguelph.ca/xmlui/handle/10214/11614

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation


Lehigh University

16. MacDonald, Logan Charles. Characterization and utilization of polysaccharide lyases from Stenotrophomonas maltophilia K279a as platforms for the design of mutant lyases with specialized substrate specificity for therapeutic and industrial applications.

Degree: PhD, Bioengineering, 2016, Lehigh University

 Multidrug resistant bacterial infections are of a global concern due to the rapidly increasing incidence over the past three decades and alarmingly few new antimicrobial… (more)

Subjects/Keywords: Enzymes; Multidrug resistance; Polysaccharide lyases; Stenotrophomonas maltophilia; Substrate specificity; Uronic acid; Biomedical Engineering and Bioengineering; Engineering

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APA (6th Edition):

MacDonald, L. C. (2016). Characterization and utilization of polysaccharide lyases from Stenotrophomonas maltophilia K279a as platforms for the design of mutant lyases with specialized substrate specificity for therapeutic and industrial applications. (Doctoral Dissertation). Lehigh University. Retrieved from https://preserve.lehigh.edu/etd/2705

Chicago Manual of Style (16th Edition):

MacDonald, Logan Charles. “Characterization and utilization of polysaccharide lyases from Stenotrophomonas maltophilia K279a as platforms for the design of mutant lyases with specialized substrate specificity for therapeutic and industrial applications.” 2016. Doctoral Dissertation, Lehigh University. Accessed January 24, 2020. https://preserve.lehigh.edu/etd/2705.

MLA Handbook (7th Edition):

MacDonald, Logan Charles. “Characterization and utilization of polysaccharide lyases from Stenotrophomonas maltophilia K279a as platforms for the design of mutant lyases with specialized substrate specificity for therapeutic and industrial applications.” 2016. Web. 24 Jan 2020.

Vancouver:

MacDonald LC. Characterization and utilization of polysaccharide lyases from Stenotrophomonas maltophilia K279a as platforms for the design of mutant lyases with specialized substrate specificity for therapeutic and industrial applications. [Internet] [Doctoral dissertation]. Lehigh University; 2016. [cited 2020 Jan 24]. Available from: https://preserve.lehigh.edu/etd/2705.

Council of Science Editors:

MacDonald LC. Characterization and utilization of polysaccharide lyases from Stenotrophomonas maltophilia K279a as platforms for the design of mutant lyases with specialized substrate specificity for therapeutic and industrial applications. [Doctoral Dissertation]. Lehigh University; 2016. Available from: https://preserve.lehigh.edu/etd/2705


University of Helsinki

17. Huang, Liyang. Biochemical characteristics of three heterologously produced ferulic acid esterases (FAEs) from Aspergillus niger.

Degree: Department of Food and Environmental Sciences; Helsingfors universitet, Agrikultur- och forstvetenskapliga fakulteten, Institutionen för livsmedels- och miljövetenskaper, 2016, University of Helsinki

 Plant biomass consists largely of polymeric compounds of which diverse polysaccharides are the main components. Ferulic acid is a ubiquitous phenolic phytochemical in plant cell… (more)

Subjects/Keywords: Aspergillus niger; ferulic acid esterase; substrate specificity; thermostability; pH optimum; solvent stability; Bioteknik (EYT); Biotechnology (EYT); Biotekniikka (EYT)

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APA (6th Edition):

Huang, L. (2016). Biochemical characteristics of three heterologously produced ferulic acid esterases (FAEs) from Aspergillus niger. (Masters Thesis). University of Helsinki. Retrieved from http://hdl.handle.net/10138/166915

Chicago Manual of Style (16th Edition):

Huang, Liyang. “Biochemical characteristics of three heterologously produced ferulic acid esterases (FAEs) from Aspergillus niger.” 2016. Masters Thesis, University of Helsinki. Accessed January 24, 2020. http://hdl.handle.net/10138/166915.

MLA Handbook (7th Edition):

Huang, Liyang. “Biochemical characteristics of three heterologously produced ferulic acid esterases (FAEs) from Aspergillus niger.” 2016. Web. 24 Jan 2020.

Vancouver:

Huang L. Biochemical characteristics of three heterologously produced ferulic acid esterases (FAEs) from Aspergillus niger. [Internet] [Masters thesis]. University of Helsinki; 2016. [cited 2020 Jan 24]. Available from: http://hdl.handle.net/10138/166915.

Council of Science Editors:

Huang L. Biochemical characteristics of three heterologously produced ferulic acid esterases (FAEs) from Aspergillus niger. [Masters Thesis]. University of Helsinki; 2016. Available from: http://hdl.handle.net/10138/166915


Kansas State University

18. Bansal, Sunil. Defining the substrate specificity of an unusual acyltransferase: a step towards the production of an advanced biofuel.

Degree: PhD, Biochemistry and Molecular Biophysics Interdepartmental Program, 2016, Kansas State University

 The direct use of vegetable oils as a biofuel suffers from problems such as high viscosity, low volatility and poor cold temperature properties. 3-acetyl-1,2-diacyl-sn-glycerols (acetyl-TAGs)… (more)

Subjects/Keywords: Acetyl-TAGs; Substrate specificity; Metabolic engineering; Low viscosity biofuel; Acyltransferase; Camelina; Alternative Energy (0363); Biochemistry (0487); Plant Sciences (0479)

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APA (6th Edition):

Bansal, S. (2016). Defining the substrate specificity of an unusual acyltransferase: a step towards the production of an advanced biofuel. (Doctoral Dissertation). Kansas State University. Retrieved from http://hdl.handle.net/2097/27647

Chicago Manual of Style (16th Edition):

Bansal, Sunil. “Defining the substrate specificity of an unusual acyltransferase: a step towards the production of an advanced biofuel.” 2016. Doctoral Dissertation, Kansas State University. Accessed January 24, 2020. http://hdl.handle.net/2097/27647.

MLA Handbook (7th Edition):

Bansal, Sunil. “Defining the substrate specificity of an unusual acyltransferase: a step towards the production of an advanced biofuel.” 2016. Web. 24 Jan 2020.

Vancouver:

Bansal S. Defining the substrate specificity of an unusual acyltransferase: a step towards the production of an advanced biofuel. [Internet] [Doctoral dissertation]. Kansas State University; 2016. [cited 2020 Jan 24]. Available from: http://hdl.handle.net/2097/27647.

Council of Science Editors:

Bansal S. Defining the substrate specificity of an unusual acyltransferase: a step towards the production of an advanced biofuel. [Doctoral Dissertation]. Kansas State University; 2016. Available from: http://hdl.handle.net/2097/27647


Wesleyan University

19. Nemmara, Venkatesh V. Substrate Specificity of Bacterial DD-Peptidases.

Degree: Chemistry, 2014, Wesleyan University

  The bacterial DD-peptidases or penicillin-binding proteins (PBPs) catalyze the formation and regulation of cross-links in peptidoglycan biosynthesis. β-Lactam antibiotics, which have been studied for… (more)

Subjects/Keywords: DD-Peptidases; Peptidoglycan; Penicillin Binding Proteins; Bacteria; Cell wall; Enzyme; Catalysis; Kinetics; Enzymology; Substrate specificity; Inhibitors

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APA (6th Edition):

Nemmara, V. V. (2014). Substrate Specificity of Bacterial DD-Peptidases. (Doctoral Dissertation). Wesleyan University. Retrieved from https://wesscholar.wesleyan.edu/etd_diss/33

Chicago Manual of Style (16th Edition):

Nemmara, Venkatesh V. “Substrate Specificity of Bacterial DD-Peptidases.” 2014. Doctoral Dissertation, Wesleyan University. Accessed January 24, 2020. https://wesscholar.wesleyan.edu/etd_diss/33.

MLA Handbook (7th Edition):

Nemmara, Venkatesh V. “Substrate Specificity of Bacterial DD-Peptidases.” 2014. Web. 24 Jan 2020.

Vancouver:

Nemmara VV. Substrate Specificity of Bacterial DD-Peptidases. [Internet] [Doctoral dissertation]. Wesleyan University; 2014. [cited 2020 Jan 24]. Available from: https://wesscholar.wesleyan.edu/etd_diss/33.

Council of Science Editors:

Nemmara VV. Substrate Specificity of Bacterial DD-Peptidases. [Doctoral Dissertation]. Wesleyan University; 2014. Available from: https://wesscholar.wesleyan.edu/etd_diss/33


Utah State University

20. Suh-Lailam, Brenda Bienka. Development of Novel Methods and their Utilization in the Analysis of the Effect of the N-terminus of Human Protein Arginine Methyltransferase 1 Variant 1 on Enzymatic Activity, Protein-protein Interactions, and Substrate Specificity.

Degree: PhD, Chemistry and Biochemistry, 2010, Utah State University

  Protein arginine methyltransferases (PRMTs) are enzymes that catalyze the methylation of protein arginine residues, resulting in the formation of monomethylarginine, and/or asymmetric or symmetric… (more)

Subjects/Keywords: enzyme activity measurement; Methylation; PROTEIN ARGININE METHYLTRANSFERASEs (PRMTs); protein-protein interactions; S-adenosyl-L-methionine-dependent methyltransferase; substrate specificity; Biochemistry

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APA (6th Edition):

Suh-Lailam, B. B. (2010). Development of Novel Methods and their Utilization in the Analysis of the Effect of the N-terminus of Human Protein Arginine Methyltransferase 1 Variant 1 on Enzymatic Activity, Protein-protein Interactions, and Substrate Specificity. (Doctoral Dissertation). Utah State University. Retrieved from https://digitalcommons.usu.edu/etd/863

Chicago Manual of Style (16th Edition):

Suh-Lailam, Brenda Bienka. “Development of Novel Methods and their Utilization in the Analysis of the Effect of the N-terminus of Human Protein Arginine Methyltransferase 1 Variant 1 on Enzymatic Activity, Protein-protein Interactions, and Substrate Specificity.” 2010. Doctoral Dissertation, Utah State University. Accessed January 24, 2020. https://digitalcommons.usu.edu/etd/863.

MLA Handbook (7th Edition):

Suh-Lailam, Brenda Bienka. “Development of Novel Methods and their Utilization in the Analysis of the Effect of the N-terminus of Human Protein Arginine Methyltransferase 1 Variant 1 on Enzymatic Activity, Protein-protein Interactions, and Substrate Specificity.” 2010. Web. 24 Jan 2020.

Vancouver:

Suh-Lailam BB. Development of Novel Methods and their Utilization in the Analysis of the Effect of the N-terminus of Human Protein Arginine Methyltransferase 1 Variant 1 on Enzymatic Activity, Protein-protein Interactions, and Substrate Specificity. [Internet] [Doctoral dissertation]. Utah State University; 2010. [cited 2020 Jan 24]. Available from: https://digitalcommons.usu.edu/etd/863.

Council of Science Editors:

Suh-Lailam BB. Development of Novel Methods and their Utilization in the Analysis of the Effect of the N-terminus of Human Protein Arginine Methyltransferase 1 Variant 1 on Enzymatic Activity, Protein-protein Interactions, and Substrate Specificity. [Doctoral Dissertation]. Utah State University; 2010. Available from: https://digitalcommons.usu.edu/etd/863


Brandeis University

21. Xu, Changhan. The Mechanistic, Structural, and Evolutionary Origin of Lactate Dehydrogenase Substrate Specificity in the Apicomplexa.

Degree: 2017, Brandeis University

 Apicomplexa are unicellular eukaryotic parasites of many animals, including humans. The most notorious example is malaria, caused by the apicomplexan parasite Plasmodium falciparum. The apicomplexan… (more)

Subjects/Keywords: Lactate dehydrogenase; Apicomplexa; Enzyme substrate specificity; Protein evolution; Plasmodium falciparum; Eimeria maxima; Enzyme kinetics; X-Ray Crystallography

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APA (6th Edition):

Xu, C. (2017). The Mechanistic, Structural, and Evolutionary Origin of Lactate Dehydrogenase Substrate Specificity in the Apicomplexa. (Thesis). Brandeis University. Retrieved from http://hdl.handle.net/10192/33900

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Xu, Changhan. “The Mechanistic, Structural, and Evolutionary Origin of Lactate Dehydrogenase Substrate Specificity in the Apicomplexa.” 2017. Thesis, Brandeis University. Accessed January 24, 2020. http://hdl.handle.net/10192/33900.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Xu, Changhan. “The Mechanistic, Structural, and Evolutionary Origin of Lactate Dehydrogenase Substrate Specificity in the Apicomplexa.” 2017. Web. 24 Jan 2020.

Vancouver:

Xu C. The Mechanistic, Structural, and Evolutionary Origin of Lactate Dehydrogenase Substrate Specificity in the Apicomplexa. [Internet] [Thesis]. Brandeis University; 2017. [cited 2020 Jan 24]. Available from: http://hdl.handle.net/10192/33900.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Xu C. The Mechanistic, Structural, and Evolutionary Origin of Lactate Dehydrogenase Substrate Specificity in the Apicomplexa. [Thesis]. Brandeis University; 2017. Available from: http://hdl.handle.net/10192/33900

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation


University of Michigan

22. Li, Jingjing. Substrate Specificity and Metal Requirements of 3-Deoxy-D-manno-octulosonate 8-Phosphate Synthase (KDOPS).

Degree: PhD, Chemistry, 2008, University of Michigan

 3-Deoxy-D-manno-octulosonate 8-phosphate synthase (KDOPS) catalyzes the aldol-type condensation of D-arabinose 5-phosphate (A5P) and phosphoenolpyruvate (PEP) to form 3-deoxy-D-manno-octulosonate 8-phosphate (KDO8P) and inorganic phosphate. This reaction… (more)

Subjects/Keywords: KDOPS; Substrate Specificity; Metal Requirements; Chemistry; Science

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APA (6th Edition):

Li, J. (2008). Substrate Specificity and Metal Requirements of 3-Deoxy-D-manno-octulosonate 8-Phosphate Synthase (KDOPS). (Doctoral Dissertation). University of Michigan. Retrieved from http://hdl.handle.net/2027.42/58440

Chicago Manual of Style (16th Edition):

Li, Jingjing. “Substrate Specificity and Metal Requirements of 3-Deoxy-D-manno-octulosonate 8-Phosphate Synthase (KDOPS).” 2008. Doctoral Dissertation, University of Michigan. Accessed January 24, 2020. http://hdl.handle.net/2027.42/58440.

MLA Handbook (7th Edition):

Li, Jingjing. “Substrate Specificity and Metal Requirements of 3-Deoxy-D-manno-octulosonate 8-Phosphate Synthase (KDOPS).” 2008. Web. 24 Jan 2020.

Vancouver:

Li J. Substrate Specificity and Metal Requirements of 3-Deoxy-D-manno-octulosonate 8-Phosphate Synthase (KDOPS). [Internet] [Doctoral dissertation]. University of Michigan; 2008. [cited 2020 Jan 24]. Available from: http://hdl.handle.net/2027.42/58440.

Council of Science Editors:

Li J. Substrate Specificity and Metal Requirements of 3-Deoxy-D-manno-octulosonate 8-Phosphate Synthase (KDOPS). [Doctoral Dissertation]. University of Michigan; 2008. Available from: http://hdl.handle.net/2027.42/58440


University of Lethbridge

23. University of Lethbridge. Faculty of Arts and Science. Structure and function of PhyA from Desulfovibrio magneticus and use of its product in affinity pull-down experiments .

Degree: 2019, University of Lethbridge

 The X-ray crystallographic structure of a divergent PTPLP from Desulfovibrio magneticus has been determined in the presence and absence of InsP6 substrate in order to… (more)

Subjects/Keywords: protein complex; substrate specificity; PTP-like; affinity pull-down; Cysteine proteinases; Inositol phosphates; Phosphatases; X-ray crystallography

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APA (6th Edition):

Science, U. o. L. F. o. A. a. (2019). Structure and function of PhyA from Desulfovibrio magneticus and use of its product in affinity pull-down experiments . (Thesis). University of Lethbridge. Retrieved from http://hdl.handle.net/10133/5478

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Science, University of Lethbridge. Faculty of Arts and. “Structure and function of PhyA from Desulfovibrio magneticus and use of its product in affinity pull-down experiments .” 2019. Thesis, University of Lethbridge. Accessed January 24, 2020. http://hdl.handle.net/10133/5478.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Science, University of Lethbridge. Faculty of Arts and. “Structure and function of PhyA from Desulfovibrio magneticus and use of its product in affinity pull-down experiments .” 2019. Web. 24 Jan 2020.

Vancouver:

Science UoLFoAa. Structure and function of PhyA from Desulfovibrio magneticus and use of its product in affinity pull-down experiments . [Internet] [Thesis]. University of Lethbridge; 2019. [cited 2020 Jan 24]. Available from: http://hdl.handle.net/10133/5478.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Science UoLFoAa. Structure and function of PhyA from Desulfovibrio magneticus and use of its product in affinity pull-down experiments . [Thesis]. University of Lethbridge; 2019. Available from: http://hdl.handle.net/10133/5478

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

24. Damasceno, Ticiane Fraga. Função de subsítios de uma catepsina digestiva de Tenebrio molitor.

Degree: Mestrado, Bioquímica, 2014, University of São Paulo

A catepsina L, uma cisteína proteinase da família da papaína, é a principal proteinase digestiva do besouro Tenebrio molitor. Estudos anteriores do nosso grupo mostraram… (more)

Subjects/Keywords: Catepsina L-like proteinase; Cathepsin L-like proteinase; Enzimologia; Enzymology; Especificidade de substrato; Hidrofobicidade de subsítio; Papel de subsítio; Subsite hydrophobicity; Subsite role; Substrate specificity; Tenebrio molitor; Tenebrio molitor

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APA (6th Edition):

Damasceno, T. F. (2014). Função de subsítios de uma catepsina digestiva de Tenebrio molitor. (Masters Thesis). University of São Paulo. Retrieved from http://www.teses.usp.br/teses/disponiveis/46/46131/tde-20012015-143853/ ;

Chicago Manual of Style (16th Edition):

Damasceno, Ticiane Fraga. “Função de subsítios de uma catepsina digestiva de Tenebrio molitor.” 2014. Masters Thesis, University of São Paulo. Accessed January 24, 2020. http://www.teses.usp.br/teses/disponiveis/46/46131/tde-20012015-143853/ ;.

MLA Handbook (7th Edition):

Damasceno, Ticiane Fraga. “Função de subsítios de uma catepsina digestiva de Tenebrio molitor.” 2014. Web. 24 Jan 2020.

Vancouver:

Damasceno TF. Função de subsítios de uma catepsina digestiva de Tenebrio molitor. [Internet] [Masters thesis]. University of São Paulo; 2014. [cited 2020 Jan 24]. Available from: http://www.teses.usp.br/teses/disponiveis/46/46131/tde-20012015-143853/ ;.

Council of Science Editors:

Damasceno TF. Função de subsítios de uma catepsina digestiva de Tenebrio molitor. [Masters Thesis]. University of São Paulo; 2014. Available from: http://www.teses.usp.br/teses/disponiveis/46/46131/tde-20012015-143853/ ;

25. Zhang, Can. Probing substrate specificity of RNA repair protein Pnkp/Hen1 from Anabaena variabilis.

Degree: MS, 0318, 2012, University of Illinois – Urbana-Champaign

 This is an in vitro study of the substrate specificity of a RNA-repair protein Pnkp/Hen1 from bacteria Anabaena Variabilis. Following the previous discovery of a… (more)

Subjects/Keywords: Ribonucleic acid (RNA) repair; substrate specificity; ribotoxin; Pnkp/Hen1

…may exhibit broader substrate specificity than T4 PnkP/Rnl1. Based on the studies presented… …bacterial might have evolved different RNA substrate specificity due to the 24 requirement of… …of the Pnkp/Hen1 RNA repair system. The first highly likely substrate is tRNA because of… …its importance in protein synthesis and because tRNA has been used as substrate during the… …previous study. In order to determine tRNA secondary structure specificity of Pnkp/Hen1, we… 

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APA (6th Edition):

Zhang, C. (2012). Probing substrate specificity of RNA repair protein Pnkp/Hen1 from Anabaena variabilis. (Thesis). University of Illinois – Urbana-Champaign. Retrieved from http://hdl.handle.net/2142/34202

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Zhang, Can. “Probing substrate specificity of RNA repair protein Pnkp/Hen1 from Anabaena variabilis.” 2012. Thesis, University of Illinois – Urbana-Champaign. Accessed January 24, 2020. http://hdl.handle.net/2142/34202.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Zhang, Can. “Probing substrate specificity of RNA repair protein Pnkp/Hen1 from Anabaena variabilis.” 2012. Web. 24 Jan 2020.

Vancouver:

Zhang C. Probing substrate specificity of RNA repair protein Pnkp/Hen1 from Anabaena variabilis. [Internet] [Thesis]. University of Illinois – Urbana-Champaign; 2012. [cited 2020 Jan 24]. Available from: http://hdl.handle.net/2142/34202.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Zhang C. Probing substrate specificity of RNA repair protein Pnkp/Hen1 from Anabaena variabilis. [Thesis]. University of Illinois – Urbana-Champaign; 2012. Available from: http://hdl.handle.net/2142/34202

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation


University of Florida

26. Sileo, Caroline. Characterization of InGaZnO thin films for flexible electronics.

Degree: 2013, University of Florida

 InGaZnO is an ideal material for the fabrication of new flexible electronics for its optical properties, amorphous nature, and ability to grow films at room… (more)

Subjects/Keywords: Amorphous materials; Electronics; Engineering; Materials science; Oxides; Power tools; Room temperature; Substrate specificity; Thin films; Transistors; Ellipsometry; Thin film transistors; Thin films

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APA (6th Edition):

Sileo, C. (2013). Characterization of InGaZnO thin films for flexible electronics. (Thesis). University of Florida. Retrieved from http://ufdc.ufl.edu/AA00057053

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Sileo, Caroline. “Characterization of InGaZnO thin films for flexible electronics.” 2013. Thesis, University of Florida. Accessed January 24, 2020. http://ufdc.ufl.edu/AA00057053.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Sileo, Caroline. “Characterization of InGaZnO thin films for flexible electronics.” 2013. Web. 24 Jan 2020.

Vancouver:

Sileo C. Characterization of InGaZnO thin films for flexible electronics. [Internet] [Thesis]. University of Florida; 2013. [cited 2020 Jan 24]. Available from: http://ufdc.ufl.edu/AA00057053.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Sileo C. Characterization of InGaZnO thin films for flexible electronics. [Thesis]. University of Florida; 2013. Available from: http://ufdc.ufl.edu/AA00057053

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation


Swedish University of Agricultural Sciences

27. Naworyta, Agata. Structure-function studies of epoxide hydrolases.

Degree: 2010, Swedish University of Agricultural Sciences

 Epoxides are three-membered cyclic ethers formed in cells via several metabolic pathways. Epoxide hydrolases (EHs) are enzymes that hydrolyse epoxides to the corresponding diols. The… (more)

Subjects/Keywords: epoxy compounds; hydrolases; enzymatic hydrolysis; chemical structure; crystallization; computer applications; solanum tuberosum; chirality; crystallography; diols; enantioselectivity; enzyme; epoxide; epoxide hydrolases; regioselectivity; substrate specificity; X-ray structure

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Naworyta, A. (2010). Structure-function studies of epoxide hydrolases. (Doctoral Dissertation). Swedish University of Agricultural Sciences. Retrieved from http://pub.epsilon.slu.se/2220/

Chicago Manual of Style (16th Edition):

Naworyta, Agata. “Structure-function studies of epoxide hydrolases.” 2010. Doctoral Dissertation, Swedish University of Agricultural Sciences. Accessed January 24, 2020. http://pub.epsilon.slu.se/2220/.

MLA Handbook (7th Edition):

Naworyta, Agata. “Structure-function studies of epoxide hydrolases.” 2010. Web. 24 Jan 2020.

Vancouver:

Naworyta A. Structure-function studies of epoxide hydrolases. [Internet] [Doctoral dissertation]. Swedish University of Agricultural Sciences; 2010. [cited 2020 Jan 24]. Available from: http://pub.epsilon.slu.se/2220/.

Council of Science Editors:

Naworyta A. Structure-function studies of epoxide hydrolases. [Doctoral Dissertation]. Swedish University of Agricultural Sciences; 2010. Available from: http://pub.epsilon.slu.se/2220/

28. Rathod, Pradipsinh Kesarji. Identification and partial characterization of mammalian aspartate-4-decarboxylase.

Degree: PhD, 1981, Oregon Health Sciences University

Subjects/Keywords: Body Weight; Enzyme Activation; Enzymes  – isolation and purification; Obesity  – etiology; Substrate Specificity

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Rathod, P. K. (1981). Identification and partial characterization of mammalian aspartate-4-decarboxylase. (Doctoral Dissertation). Oregon Health Sciences University. Retrieved from doi:10.6083/M4ZP449M ; http://digitalcommons.ohsu.edu/etd/2237

Chicago Manual of Style (16th Edition):

Rathod, Pradipsinh Kesarji. “Identification and partial characterization of mammalian aspartate-4-decarboxylase.” 1981. Doctoral Dissertation, Oregon Health Sciences University. Accessed January 24, 2020. doi:10.6083/M4ZP449M ; http://digitalcommons.ohsu.edu/etd/2237.

MLA Handbook (7th Edition):

Rathod, Pradipsinh Kesarji. “Identification and partial characterization of mammalian aspartate-4-decarboxylase.” 1981. Web. 24 Jan 2020.

Vancouver:

Rathod PK. Identification and partial characterization of mammalian aspartate-4-decarboxylase. [Internet] [Doctoral dissertation]. Oregon Health Sciences University; 1981. [cited 2020 Jan 24]. Available from: doi:10.6083/M4ZP449M ; http://digitalcommons.ohsu.edu/etd/2237.

Council of Science Editors:

Rathod PK. Identification and partial characterization of mammalian aspartate-4-decarboxylase. [Doctoral Dissertation]. Oregon Health Sciences University; 1981. Available from: doi:10.6083/M4ZP449M ; http://digitalcommons.ohsu.edu/etd/2237


University of Western Ontario

29. Gould, Alister D. ATPase Regulation in the Maltose Transporter.

Degree: 2011, University of Western Ontario

 This thesis investigates the mechanism of activity-coupling in the maltose transporter of Escherichia coli (MalFGK2); the way ATP hydrolysis is prevented in the absence of… (more)

Subjects/Keywords: Active Transport; ATP Binding Cassette; ATPase; Escherichia Coli; Cell Membrane; Maltose Binding Protein; Maltose Transport; Protein Conformation; Substrate Specificity; X-ray Crystallography; Biochemistry; Structural Biology

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APA (6th Edition):

Gould, A. D. (2011). ATPase Regulation in the Maltose Transporter. (Thesis). University of Western Ontario. Retrieved from https://ir.lib.uwo.ca/etd/374

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Gould, Alister D. “ATPase Regulation in the Maltose Transporter.” 2011. Thesis, University of Western Ontario. Accessed January 24, 2020. https://ir.lib.uwo.ca/etd/374.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Gould, Alister D. “ATPase Regulation in the Maltose Transporter.” 2011. Web. 24 Jan 2020.

Vancouver:

Gould AD. ATPase Regulation in the Maltose Transporter. [Internet] [Thesis]. University of Western Ontario; 2011. [cited 2020 Jan 24]. Available from: https://ir.lib.uwo.ca/etd/374.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Gould AD. ATPase Regulation in the Maltose Transporter. [Thesis]. University of Western Ontario; 2011. Available from: https://ir.lib.uwo.ca/etd/374

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation


Queensland University of Technology

30. Milne, Trudy Jane. Purification and characterisation of Tex31, a conotoxin precursor processing protease, isolated from the venom duct of Conus textile.

Degree: 2008, Queensland University of Technology

 The venom of cone snails (predatory marine molluscs of the genus Conus) has yielded a rich source of novel neuroactive peptides or “conotoxins”. Conotoxins are… (more)

Subjects/Keywords: Tex31; protease; Conus; O-superfamily; propeptide precursor; para-nitroanilide; substrate specificity; pathogenesis-related protein; CAP; PR-1; CRISP; homology model; recombinant protein expression

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Milne, T. J. (2008). Purification and characterisation of Tex31, a conotoxin precursor processing protease, isolated from the venom duct of Conus textile. (Thesis). Queensland University of Technology. Retrieved from https://eprints.qut.edu.au/16960/

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Milne, Trudy Jane. “Purification and characterisation of Tex31, a conotoxin precursor processing protease, isolated from the venom duct of Conus textile.” 2008. Thesis, Queensland University of Technology. Accessed January 24, 2020. https://eprints.qut.edu.au/16960/.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Milne, Trudy Jane. “Purification and characterisation of Tex31, a conotoxin precursor processing protease, isolated from the venom duct of Conus textile.” 2008. Web. 24 Jan 2020.

Vancouver:

Milne TJ. Purification and characterisation of Tex31, a conotoxin precursor processing protease, isolated from the venom duct of Conus textile. [Internet] [Thesis]. Queensland University of Technology; 2008. [cited 2020 Jan 24]. Available from: https://eprints.qut.edu.au/16960/.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Milne TJ. Purification and characterisation of Tex31, a conotoxin precursor processing protease, isolated from the venom duct of Conus textile. [Thesis]. Queensland University of Technology; 2008. Available from: https://eprints.qut.edu.au/16960/

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

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