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You searched for +publisher:"University of Illinois – Urbana-Champaign" +contributor:("Gerlt, John A."). Showing records 1 – 19 of 19 total matches.

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University of Illinois – Urbana-Champaign

1. Iiams, Vanessa A. Investigations into the mechanism of orotidine 5'-monophosphate decarboxylase: Sources of substrate destabilization and transition state stabilization.

Degree: MS, 0335, 2011, University of Illinois – Urbana-Champaign

 Orotidine 5′-monophosphate decarboxylase (OMPDC) achieves a rarely paralleled rate acceleration, yet the catalytic basis prompting this enhancement have yet to be fully elucidated. To accomplish… (more)

Subjects/Keywords: Orotidine 5'-monophosphate decarboxylase (OMPDC)

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APA (6th Edition):

Iiams, V. A. (2011). Investigations into the mechanism of orotidine 5'-monophosphate decarboxylase: Sources of substrate destabilization and transition state stabilization. (Thesis). University of Illinois – Urbana-Champaign. Retrieved from http://hdl.handle.net/2142/18424

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):

Iiams, Vanessa A. “Investigations into the mechanism of orotidine 5'-monophosphate decarboxylase: Sources of substrate destabilization and transition state stabilization.” 2011. Thesis, University of Illinois – Urbana-Champaign. Accessed April 03, 2020. http://hdl.handle.net/2142/18424.

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

MLA Handbook (7th Edition):

Iiams, Vanessa A. “Investigations into the mechanism of orotidine 5'-monophosphate decarboxylase: Sources of substrate destabilization and transition state stabilization.” 2011. Web. 03 Apr 2020.

Vancouver:

Iiams VA. Investigations into the mechanism of orotidine 5'-monophosphate decarboxylase: Sources of substrate destabilization and transition state stabilization. [Internet] [Thesis]. University of Illinois – Urbana-Champaign; 2011. [cited 2020 Apr 03]. Available from: http://hdl.handle.net/2142/18424.

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

Council of Science Editors:

Iiams VA. Investigations into the mechanism of orotidine 5'-monophosphate decarboxylase: Sources of substrate destabilization and transition state stabilization. [Thesis]. University of Illinois – Urbana-Champaign; 2011. Available from: http://hdl.handle.net/2142/18424

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


University of Illinois – Urbana-Champaign

2. Wood, Bryant M. In search of catalytic proficiency: The importance of enzyme conformational change to orotidine 5???-monophosphate decarboxylase catalysis.

Degree: PhD, 0318, 2011, University of Illinois – Urbana-Champaign

 The focus of this research is the role of conformational flexibility in catalysis by a TIM-barrel enzyme in pyrimidine biosynthesis, orotidine 5???-monophosphate decarboxylase (OMPDC). OMPDC… (more)

Subjects/Keywords: enzymology; decarboxylase; decarboxylation; orotidine 5???-monophosphate decarboxylase (OMPDC); OMP decarboxylase; site-directed mutagenesis; viscosity effects; catalytic proficiency

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APA (6th Edition):

Wood, B. M. (2011). In search of catalytic proficiency: The importance of enzyme conformational change to orotidine 5???-monophosphate decarboxylase catalysis. (Doctoral Dissertation). University of Illinois – Urbana-Champaign. Retrieved from http://hdl.handle.net/2142/18336

Chicago Manual of Style (16th Edition):

Wood, Bryant M. “In search of catalytic proficiency: The importance of enzyme conformational change to orotidine 5???-monophosphate decarboxylase catalysis.” 2011. Doctoral Dissertation, University of Illinois – Urbana-Champaign. Accessed April 03, 2020. http://hdl.handle.net/2142/18336.

MLA Handbook (7th Edition):

Wood, Bryant M. “In search of catalytic proficiency: The importance of enzyme conformational change to orotidine 5???-monophosphate decarboxylase catalysis.” 2011. Web. 03 Apr 2020.

Vancouver:

Wood BM. In search of catalytic proficiency: The importance of enzyme conformational change to orotidine 5???-monophosphate decarboxylase catalysis. [Internet] [Doctoral dissertation]. University of Illinois – Urbana-Champaign; 2011. [cited 2020 Apr 03]. Available from: http://hdl.handle.net/2142/18336.

Council of Science Editors:

Wood BM. In search of catalytic proficiency: The importance of enzyme conformational change to orotidine 5???-monophosphate decarboxylase catalysis. [Doctoral Dissertation]. University of Illinois – Urbana-Champaign; 2011. Available from: http://hdl.handle.net/2142/18336


University of Illinois – Urbana-Champaign

3. Ghasem pur, Salehe. Mining the enolase superfamily for new functions: investigations of D-glucarate dehydratase related proteins (GlucDRP) and L-lyxonate dehydratase proteins (LyxD).

Degree: PhD, 0318, 2015, University of Illinois – Urbana-Champaign

 Genomic era begins with development of sequencing methods. Genome sequencing is now cost-effective and fast, giving rise to increasing amounts of genomic data. However, the… (more)

Subjects/Keywords: Enolase; L-lyxonate; Heterodimer; Heterospecies; D-Glucarate

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APA (6th Edition):

Ghasem pur, S. (2015). Mining the enolase superfamily for new functions: investigations of D-glucarate dehydratase related proteins (GlucDRP) and L-lyxonate dehydratase proteins (LyxD). (Doctoral Dissertation). University of Illinois – Urbana-Champaign. Retrieved from http://hdl.handle.net/2142/73056

Chicago Manual of Style (16th Edition):

Ghasem pur, Salehe. “Mining the enolase superfamily for new functions: investigations of D-glucarate dehydratase related proteins (GlucDRP) and L-lyxonate dehydratase proteins (LyxD).” 2015. Doctoral Dissertation, University of Illinois – Urbana-Champaign. Accessed April 03, 2020. http://hdl.handle.net/2142/73056.

MLA Handbook (7th Edition):

Ghasem pur, Salehe. “Mining the enolase superfamily for new functions: investigations of D-glucarate dehydratase related proteins (GlucDRP) and L-lyxonate dehydratase proteins (LyxD).” 2015. Web. 03 Apr 2020.

Vancouver:

Ghasem pur S. Mining the enolase superfamily for new functions: investigations of D-glucarate dehydratase related proteins (GlucDRP) and L-lyxonate dehydratase proteins (LyxD). [Internet] [Doctoral dissertation]. University of Illinois – Urbana-Champaign; 2015. [cited 2020 Apr 03]. Available from: http://hdl.handle.net/2142/73056.

Council of Science Editors:

Ghasem pur S. Mining the enolase superfamily for new functions: investigations of D-glucarate dehydratase related proteins (GlucDRP) and L-lyxonate dehydratase proteins (LyxD). [Doctoral Dissertation]. University of Illinois – Urbana-Champaign; 2015. Available from: http://hdl.handle.net/2142/73056


University of Illinois – Urbana-Champaign

4. Groninger-Poe, Fiona. Functional assignments in the enolase superfamily: investigations of two divergent groups of D-galacturonate dehydratases and galactarate dehydratase-III.

Degree: PhD, 0318, 2014, University of Illinois – Urbana-Champaign

 More than a decade after the genomic age, full genome sequencing is cost-effective and fast, allowing for the deposit of an ever increasing number of… (more)

Subjects/Keywords: enolase superfamily; D-galacturonate; D-galacturonate dehydratase; m-galactararate; m-galactarate dehydratase

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APA (6th Edition):

Groninger-Poe, F. (2014). Functional assignments in the enolase superfamily: investigations of two divergent groups of D-galacturonate dehydratases and galactarate dehydratase-III. (Doctoral Dissertation). University of Illinois – Urbana-Champaign. Retrieved from http://hdl.handle.net/2142/50351

Chicago Manual of Style (16th Edition):

Groninger-Poe, Fiona. “Functional assignments in the enolase superfamily: investigations of two divergent groups of D-galacturonate dehydratases and galactarate dehydratase-III.” 2014. Doctoral Dissertation, University of Illinois – Urbana-Champaign. Accessed April 03, 2020. http://hdl.handle.net/2142/50351.

MLA Handbook (7th Edition):

Groninger-Poe, Fiona. “Functional assignments in the enolase superfamily: investigations of two divergent groups of D-galacturonate dehydratases and galactarate dehydratase-III.” 2014. Web. 03 Apr 2020.

Vancouver:

Groninger-Poe F. Functional assignments in the enolase superfamily: investigations of two divergent groups of D-galacturonate dehydratases and galactarate dehydratase-III. [Internet] [Doctoral dissertation]. University of Illinois – Urbana-Champaign; 2014. [cited 2020 Apr 03]. Available from: http://hdl.handle.net/2142/50351.

Council of Science Editors:

Groninger-Poe F. Functional assignments in the enolase superfamily: investigations of two divergent groups of D-galacturonate dehydratases and galactarate dehydratase-III. [Doctoral Dissertation]. University of Illinois – Urbana-Champaign; 2014. Available from: http://hdl.handle.net/2142/50351


University of Illinois – Urbana-Champaign

5. Bouvier, Jason T. Functional discovery in the oxidative D-galacturonate assimilation pathway and development of the enzyme similarity web tool.

Degree: PhD, Biochemistry, 2015, University of Illinois – Urbana-Champaign

 Sequencing technology has improved dramatically over the past few decades. Before the sequencing of complete genomes was possible, the sequencing of a gene was directly… (more)

Subjects/Keywords: Hexuronate degradation; sequence similarity network; Enzyme Function Initiative

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APA (6th Edition):

Bouvier, J. T. (2015). Functional discovery in the oxidative D-galacturonate assimilation pathway and development of the enzyme similarity web tool. (Doctoral Dissertation). University of Illinois – Urbana-Champaign. Retrieved from http://hdl.handle.net/2142/88275

Chicago Manual of Style (16th Edition):

Bouvier, Jason T. “Functional discovery in the oxidative D-galacturonate assimilation pathway and development of the enzyme similarity web tool.” 2015. Doctoral Dissertation, University of Illinois – Urbana-Champaign. Accessed April 03, 2020. http://hdl.handle.net/2142/88275.

MLA Handbook (7th Edition):

Bouvier, Jason T. “Functional discovery in the oxidative D-galacturonate assimilation pathway and development of the enzyme similarity web tool.” 2015. Web. 03 Apr 2020.

Vancouver:

Bouvier JT. Functional discovery in the oxidative D-galacturonate assimilation pathway and development of the enzyme similarity web tool. [Internet] [Doctoral dissertation]. University of Illinois – Urbana-Champaign; 2015. [cited 2020 Apr 03]. Available from: http://hdl.handle.net/2142/88275.

Council of Science Editors:

Bouvier JT. Functional discovery in the oxidative D-galacturonate assimilation pathway and development of the enzyme similarity web tool. [Doctoral Dissertation]. University of Illinois – Urbana-Champaign; 2015. Available from: http://hdl.handle.net/2142/88275


University of Illinois – Urbana-Champaign

6. McLachlan, Michael J. Transcription Factor Engineering: Tools and Applications.

Degree: PhD, 0319, 2011, University of Illinois – Urbana-Champaign

 Transcription factors play a vital role in the biology of every organism. By controlling gene expression they regulate growth, development, metabolism, reproduction, signaling, and response… (more)

Subjects/Keywords: Transcription factor; estrogen receptor alpha; protein engineering; biosensor; vascular endothelial growth factor-A (VEGF-A)

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APA (6th Edition):

McLachlan, M. J. (2011). Transcription Factor Engineering: Tools and Applications. (Doctoral Dissertation). University of Illinois – Urbana-Champaign. Retrieved from http://hdl.handle.net/2142/18624

Chicago Manual of Style (16th Edition):

McLachlan, Michael J. “Transcription Factor Engineering: Tools and Applications.” 2011. Doctoral Dissertation, University of Illinois – Urbana-Champaign. Accessed April 03, 2020. http://hdl.handle.net/2142/18624.

MLA Handbook (7th Edition):

McLachlan, Michael J. “Transcription Factor Engineering: Tools and Applications.” 2011. Web. 03 Apr 2020.

Vancouver:

McLachlan MJ. Transcription Factor Engineering: Tools and Applications. [Internet] [Doctoral dissertation]. University of Illinois – Urbana-Champaign; 2011. [cited 2020 Apr 03]. Available from: http://hdl.handle.net/2142/18624.

Council of Science Editors:

McLachlan MJ. Transcription Factor Engineering: Tools and Applications. [Doctoral Dissertation]. University of Illinois – Urbana-Champaign; 2011. Available from: http://hdl.handle.net/2142/18624


University of Illinois – Urbana-Champaign

7. Mattis, Daiva Maria. Engineering of bacterial exotoxin and endotoxin antagonists.

Degree: PhD, Biochemistry, 2015, University of Illinois – Urbana-Champaign

 Gram negative and positive bacteria have evolved toxins to aid in their ability to colonize host organisms. Some gram-positive bacteria produce exotoxins called superantigens that… (more)

Subjects/Keywords: Yeast-display; Superantigen; Staphylococcal Enterotoxin C; MD-2; Toll-like receptor 4 (TLR4); Lipopolysaccharide (LPS)

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APA (6th Edition):

Mattis, D. M. (2015). Engineering of bacterial exotoxin and endotoxin antagonists. (Doctoral Dissertation). University of Illinois – Urbana-Champaign. Retrieved from http://hdl.handle.net/2142/88242

Chicago Manual of Style (16th Edition):

Mattis, Daiva Maria. “Engineering of bacterial exotoxin and endotoxin antagonists.” 2015. Doctoral Dissertation, University of Illinois – Urbana-Champaign. Accessed April 03, 2020. http://hdl.handle.net/2142/88242.

MLA Handbook (7th Edition):

Mattis, Daiva Maria. “Engineering of bacterial exotoxin and endotoxin antagonists.” 2015. Web. 03 Apr 2020.

Vancouver:

Mattis DM. Engineering of bacterial exotoxin and endotoxin antagonists. [Internet] [Doctoral dissertation]. University of Illinois – Urbana-Champaign; 2015. [cited 2020 Apr 03]. Available from: http://hdl.handle.net/2142/88242.

Council of Science Editors:

Mattis DM. Engineering of bacterial exotoxin and endotoxin antagonists. [Doctoral Dissertation]. University of Illinois – Urbana-Champaign; 2015. Available from: http://hdl.handle.net/2142/88242


University of Illinois – Urbana-Champaign

8. Hung, John. Mechanistic studies to determine the catalytic roles of active site residues in phosphite dehydrogenase.

Degree: PhD, 0335, 2014, University of Illinois – Urbana-Champaign

 Phosphite dehydrogenase (PTDH) catalyzes the oxidation of phosphite to phosphate with the concurrent reduction of NAD+ to NADH. The mechanism of the reaction resembles a… (more)

Subjects/Keywords: Phosphite Dehydrogenase; enzymology; chemical biology; enzymes; enzyme kinetics; enzyme inhibition

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APA (6th Edition):

Hung, J. (2014). Mechanistic studies to determine the catalytic roles of active site residues in phosphite dehydrogenase. (Doctoral Dissertation). University of Illinois – Urbana-Champaign. Retrieved from http://hdl.handle.net/2142/46929

Chicago Manual of Style (16th Edition):

Hung, John. “Mechanistic studies to determine the catalytic roles of active site residues in phosphite dehydrogenase.” 2014. Doctoral Dissertation, University of Illinois – Urbana-Champaign. Accessed April 03, 2020. http://hdl.handle.net/2142/46929.

MLA Handbook (7th Edition):

Hung, John. “Mechanistic studies to determine the catalytic roles of active site residues in phosphite dehydrogenase.” 2014. Web. 03 Apr 2020.

Vancouver:

Hung J. Mechanistic studies to determine the catalytic roles of active site residues in phosphite dehydrogenase. [Internet] [Doctoral dissertation]. University of Illinois – Urbana-Champaign; 2014. [cited 2020 Apr 03]. Available from: http://hdl.handle.net/2142/46929.

Council of Science Editors:

Hung J. Mechanistic studies to determine the catalytic roles of active site residues in phosphite dehydrogenase. [Doctoral Dissertation]. University of Illinois – Urbana-Champaign; 2014. Available from: http://hdl.handle.net/2142/46929


University of Illinois – Urbana-Champaign

9. Evans, Bradley S. Reengineering and Discovery of Nonribosomal Peptide Synthetases.

Degree: PhD, 0318, 2011, University of Illinois – Urbana-Champaign

 Nonribosomal peptides are an important class of natural products including the life-saving antibiotics penicillin and vancomycin and the deadly microcystins and cereulide. This important category… (more)

Subjects/Keywords: nonribosomal peptide synthetases; directed evolution; high-throughput screening; antibiotics; Fourier-transform mass spectrometry; proteomics; natural products

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APA (6th Edition):

Evans, B. S. (2011). Reengineering and Discovery of Nonribosomal Peptide Synthetases. (Doctoral Dissertation). University of Illinois – Urbana-Champaign. Retrieved from http://hdl.handle.net/2142/18572

Chicago Manual of Style (16th Edition):

Evans, Bradley S. “Reengineering and Discovery of Nonribosomal Peptide Synthetases.” 2011. Doctoral Dissertation, University of Illinois – Urbana-Champaign. Accessed April 03, 2020. http://hdl.handle.net/2142/18572.

MLA Handbook (7th Edition):

Evans, Bradley S. “Reengineering and Discovery of Nonribosomal Peptide Synthetases.” 2011. Web. 03 Apr 2020.

Vancouver:

Evans BS. Reengineering and Discovery of Nonribosomal Peptide Synthetases. [Internet] [Doctoral dissertation]. University of Illinois – Urbana-Champaign; 2011. [cited 2020 Apr 03]. Available from: http://hdl.handle.net/2142/18572.

Council of Science Editors:

Evans BS. Reengineering and Discovery of Nonribosomal Peptide Synthetases. [Doctoral Dissertation]. University of Illinois – Urbana-Champaign; 2011. Available from: http://hdl.handle.net/2142/18572


University of Illinois – Urbana-Champaign

10. Wichelecki, Daniel. Functional and physiological discovery in the mannonate dehydratase subgroup of the enolase superfamily.

Degree: PhD, 0318, 2015, University of Illinois – Urbana-Champaign

 In the current post-genomic world, the exponential amassing of protein sequences is overwhelming the scientific community’s ability to experimentally assign each protein’s function. The use… (more)

Subjects/Keywords: Enzyme Function Initiative; enzyme; D-mannonate; L-gulonate; L-idonate; D-gluconate; mannonate dehydratase; gluconate dehydratase; Reverse Thymidylate Synthase (rTS); Enolase Superfamily Member 1 (ENOSF1); functional discovery; physiological discovery; enzyme evolution; Caulobacter; Salmonella; Chromohalobacter; enolase superfamily

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APA (6th Edition):

Wichelecki, D. (2015). Functional and physiological discovery in the mannonate dehydratase subgroup of the enolase superfamily. (Doctoral Dissertation). University of Illinois – Urbana-Champaign. Retrieved from http://hdl.handle.net/2142/73007

Chicago Manual of Style (16th Edition):

Wichelecki, Daniel. “Functional and physiological discovery in the mannonate dehydratase subgroup of the enolase superfamily.” 2015. Doctoral Dissertation, University of Illinois – Urbana-Champaign. Accessed April 03, 2020. http://hdl.handle.net/2142/73007.

MLA Handbook (7th Edition):

Wichelecki, Daniel. “Functional and physiological discovery in the mannonate dehydratase subgroup of the enolase superfamily.” 2015. Web. 03 Apr 2020.

Vancouver:

Wichelecki D. Functional and physiological discovery in the mannonate dehydratase subgroup of the enolase superfamily. [Internet] [Doctoral dissertation]. University of Illinois – Urbana-Champaign; 2015. [cited 2020 Apr 03]. Available from: http://hdl.handle.net/2142/73007.

Council of Science Editors:

Wichelecki D. Functional and physiological discovery in the mannonate dehydratase subgroup of the enolase superfamily. [Doctoral Dissertation]. University of Illinois – Urbana-Champaign; 2015. Available from: http://hdl.handle.net/2142/73007


University of Illinois – Urbana-Champaign

11. Dunbar, Kyle. Revealing the molecular details of azoline formation in ribosomal natural product biosynthesis.

Degree: PhD, 0335, 2015, University of Illinois – Urbana-Champaign

 The thiazole/oxazole-modified microcins (TOMMs) are a recently grouped class of ribosomally synthesized and posttranslationally modified peptides. Encoded by many bacteria and archaea, these natural products… (more)

Subjects/Keywords: Azoline Biosynthesis; ribosomally synthesized and post-translationally modified peptide (RiPP) Biosynthesis; thiazole/oxazole-modified microcin (TOMM) Biosynthesis; Cyclodehydratase; YcaO

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APA (6th Edition):

Dunbar, K. (2015). Revealing the molecular details of azoline formation in ribosomal natural product biosynthesis. (Doctoral Dissertation). University of Illinois – Urbana-Champaign. Retrieved from http://hdl.handle.net/2142/73109

Chicago Manual of Style (16th Edition):

Dunbar, Kyle. “Revealing the molecular details of azoline formation in ribosomal natural product biosynthesis.” 2015. Doctoral Dissertation, University of Illinois – Urbana-Champaign. Accessed April 03, 2020. http://hdl.handle.net/2142/73109.

MLA Handbook (7th Edition):

Dunbar, Kyle. “Revealing the molecular details of azoline formation in ribosomal natural product biosynthesis.” 2015. Web. 03 Apr 2020.

Vancouver:

Dunbar K. Revealing the molecular details of azoline formation in ribosomal natural product biosynthesis. [Internet] [Doctoral dissertation]. University of Illinois – Urbana-Champaign; 2015. [cited 2020 Apr 03]. Available from: http://hdl.handle.net/2142/73109.

Council of Science Editors:

Dunbar K. Revealing the molecular details of azoline formation in ribosomal natural product biosynthesis. [Doctoral Dissertation]. University of Illinois – Urbana-Champaign; 2015. Available from: http://hdl.handle.net/2142/73109


University of Illinois – Urbana-Champaign

12. Okesli, Ayse. Biosynthesis and engineering of lanthipeptides.

Degree: PhD, 0335, 2014, University of Illinois – Urbana-Champaign

 The emergence of antibiotic-resistant bacterial strains is a growing concern as antimicrobial drug discovery is not proceeding at the same pace as the growth of… (more)

Subjects/Keywords: Lanthipeptides; cinnamycin; nisin; Phage display; biosynthesis of natural products; Lantibiotics

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APA (6th Edition):

Okesli, A. (2014). Biosynthesis and engineering of lanthipeptides. (Doctoral Dissertation). University of Illinois – Urbana-Champaign. Retrieved from http://hdl.handle.net/2142/50336

Chicago Manual of Style (16th Edition):

Okesli, Ayse. “Biosynthesis and engineering of lanthipeptides.” 2014. Doctoral Dissertation, University of Illinois – Urbana-Champaign. Accessed April 03, 2020. http://hdl.handle.net/2142/50336.

MLA Handbook (7th Edition):

Okesli, Ayse. “Biosynthesis and engineering of lanthipeptides.” 2014. Web. 03 Apr 2020.

Vancouver:

Okesli A. Biosynthesis and engineering of lanthipeptides. [Internet] [Doctoral dissertation]. University of Illinois – Urbana-Champaign; 2014. [cited 2020 Apr 03]. Available from: http://hdl.handle.net/2142/50336.

Council of Science Editors:

Okesli A. Biosynthesis and engineering of lanthipeptides. [Doctoral Dissertation]. University of Illinois – Urbana-Champaign; 2014. Available from: http://hdl.handle.net/2142/50336


University of Illinois – Urbana-Champaign

13. Yu, Yi. Mechanistic studies of class II lanthipeptide synthetases and yeast surface display of lanthipeptide leader peptides.

Degree: PhD, Biochemistry, 2015, University of Illinois – Urbana-Champaign

 Lanthipeptides are natural products that belong to the family of ribosomally synthesized and posttranslationally modified peptides (RiPPs). They contain the characteristic lanthionine (Lan) or methyllanthionine… (more)

Subjects/Keywords: Lanthipeptide; Lanthionine synthetase; Yeast surface display

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APA (6th Edition):

Yu, Y. (2015). Mechanistic studies of class II lanthipeptide synthetases and yeast surface display of lanthipeptide leader peptides. (Doctoral Dissertation). University of Illinois – Urbana-Champaign. Retrieved from http://hdl.handle.net/2142/89191

Chicago Manual of Style (16th Edition):

Yu, Yi. “Mechanistic studies of class II lanthipeptide synthetases and yeast surface display of lanthipeptide leader peptides.” 2015. Doctoral Dissertation, University of Illinois – Urbana-Champaign. Accessed April 03, 2020. http://hdl.handle.net/2142/89191.

MLA Handbook (7th Edition):

Yu, Yi. “Mechanistic studies of class II lanthipeptide synthetases and yeast surface display of lanthipeptide leader peptides.” 2015. Web. 03 Apr 2020.

Vancouver:

Yu Y. Mechanistic studies of class II lanthipeptide synthetases and yeast surface display of lanthipeptide leader peptides. [Internet] [Doctoral dissertation]. University of Illinois – Urbana-Champaign; 2015. [cited 2020 Apr 03]. Available from: http://hdl.handle.net/2142/89191.

Council of Science Editors:

Yu Y. Mechanistic studies of class II lanthipeptide synthetases and yeast surface display of lanthipeptide leader peptides. [Doctoral Dissertation]. University of Illinois – Urbana-Champaign; 2015. Available from: http://hdl.handle.net/2142/89191


University of Illinois – Urbana-Champaign

14. Frank, Daniel J. Global deconvolution of heterotropic cooperativity in cytochrome P450 3A4.

Degree: PhD, 0318, 2011, University of Illinois – Urbana-Champaign

 Cytochrome P450 3A4 (CYP3A4) plays a central role in xenobiotic metabolism, and is of critical importance to both human health and the pharmaceutical industry. Its… (more)

Subjects/Keywords: cooperativity; cytochrome P450 3A4; drug-drug interactions

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APA (6th Edition):

Frank, D. J. (2011). Global deconvolution of heterotropic cooperativity in cytochrome P450 3A4. (Doctoral Dissertation). University of Illinois – Urbana-Champaign. Retrieved from http://hdl.handle.net/2142/24520

Chicago Manual of Style (16th Edition):

Frank, Daniel J. “Global deconvolution of heterotropic cooperativity in cytochrome P450 3A4.” 2011. Doctoral Dissertation, University of Illinois – Urbana-Champaign. Accessed April 03, 2020. http://hdl.handle.net/2142/24520.

MLA Handbook (7th Edition):

Frank, Daniel J. “Global deconvolution of heterotropic cooperativity in cytochrome P450 3A4.” 2011. Web. 03 Apr 2020.

Vancouver:

Frank DJ. Global deconvolution of heterotropic cooperativity in cytochrome P450 3A4. [Internet] [Doctoral dissertation]. University of Illinois – Urbana-Champaign; 2011. [cited 2020 Apr 03]. Available from: http://hdl.handle.net/2142/24520.

Council of Science Editors:

Frank DJ. Global deconvolution of heterotropic cooperativity in cytochrome P450 3A4. [Doctoral Dissertation]. University of Illinois – Urbana-Champaign; 2011. Available from: http://hdl.handle.net/2142/24520

15. Warlick, Benjamin. Functional discovery and promiscuity in the RuBisCO superfamily.

Degree: PhD, 0318, 2013, University of Illinois – Urbana-Champaign

 To keep pace with large scale sequencing projects that are filling sequence databases with misannotated sequences, a new method of functional annotation is necessary. The… (more)

Subjects/Keywords: D-Ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO); RuBisCO-like proteins (RLPs)

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APA (6th Edition):

Warlick, B. (2013). Functional discovery and promiscuity in the RuBisCO superfamily. (Doctoral Dissertation). University of Illinois – Urbana-Champaign. Retrieved from http://hdl.handle.net/2142/45444

Chicago Manual of Style (16th Edition):

Warlick, Benjamin. “Functional discovery and promiscuity in the RuBisCO superfamily.” 2013. Doctoral Dissertation, University of Illinois – Urbana-Champaign. Accessed April 03, 2020. http://hdl.handle.net/2142/45444.

MLA Handbook (7th Edition):

Warlick, Benjamin. “Functional discovery and promiscuity in the RuBisCO superfamily.” 2013. Web. 03 Apr 2020.

Vancouver:

Warlick B. Functional discovery and promiscuity in the RuBisCO superfamily. [Internet] [Doctoral dissertation]. University of Illinois – Urbana-Champaign; 2013. [cited 2020 Apr 03]. Available from: http://hdl.handle.net/2142/45444.

Council of Science Editors:

Warlick B. Functional discovery and promiscuity in the RuBisCO superfamily. [Doctoral Dissertation]. University of Illinois – Urbana-Champaign; 2013. Available from: http://hdl.handle.net/2142/45444

16. Desai, Bijoy. Structural requirements for enzymatic efficiency in cofactor-independent decarboxylation.

Degree: PhD, 0318, 2015, University of Illinois – Urbana-Champaign

 Orotidine 5’-monophosphate decarboxylase (OMPDC) is the last enzyme in the de novo pyrimidine biosynthetic pathway. It catalyzes the decarboxylation of orotidine 5’-monophosphate (OMP) to uridine… (more)

Subjects/Keywords: Enzymology; catalysis; Orotidine 5'-monophosphate decarboxylase; in vitro translation; orthogonal translation system; non natural protein residue; conformational change; intrinsic binding energy; frsA

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APA (6th Edition):

Desai, B. (2015). Structural requirements for enzymatic efficiency in cofactor-independent decarboxylation. (Doctoral Dissertation). University of Illinois – Urbana-Champaign. Retrieved from http://hdl.handle.net/2142/72911

Chicago Manual of Style (16th Edition):

Desai, Bijoy. “Structural requirements for enzymatic efficiency in cofactor-independent decarboxylation.” 2015. Doctoral Dissertation, University of Illinois – Urbana-Champaign. Accessed April 03, 2020. http://hdl.handle.net/2142/72911.

MLA Handbook (7th Edition):

Desai, Bijoy. “Structural requirements for enzymatic efficiency in cofactor-independent decarboxylation.” 2015. Web. 03 Apr 2020.

Vancouver:

Desai B. Structural requirements for enzymatic efficiency in cofactor-independent decarboxylation. [Internet] [Doctoral dissertation]. University of Illinois – Urbana-Champaign; 2015. [cited 2020 Apr 03]. Available from: http://hdl.handle.net/2142/72911.

Council of Science Editors:

Desai B. Structural requirements for enzymatic efficiency in cofactor-independent decarboxylation. [Doctoral Dissertation]. University of Illinois – Urbana-Champaign; 2015. Available from: http://hdl.handle.net/2142/72911

17. El Haj Hassan, Bachar H. Lipoic acid assembly on 2-oxoacid dehydrogenases in E.coli.

Degree: PhD, 0318, 2011, University of Illinois – Urbana-Champaign

 Lipoic acid is a covalently attached cofactor essential for the activity of 2-oxoacid dehydrogenases and the glycine cleavage system. In the absence of lipoic acid… (more)

Subjects/Keywords: Lipoic acid; pyruvate dehydrogenase; 2-oxoglutarate dehydrogenase; LipB; LipA; LplA; GroEL

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

APA (6th Edition):

El Haj Hassan, B. H. (2011). Lipoic acid assembly on 2-oxoacid dehydrogenases in E.coli. (Doctoral Dissertation). University of Illinois – Urbana-Champaign. Retrieved from http://hdl.handle.net/2142/24473

Chicago Manual of Style (16th Edition):

El Haj Hassan, Bachar H. “Lipoic acid assembly on 2-oxoacid dehydrogenases in E.coli.” 2011. Doctoral Dissertation, University of Illinois – Urbana-Champaign. Accessed April 03, 2020. http://hdl.handle.net/2142/24473.

MLA Handbook (7th Edition):

El Haj Hassan, Bachar H. “Lipoic acid assembly on 2-oxoacid dehydrogenases in E.coli.” 2011. Web. 03 Apr 2020.

Vancouver:

El Haj Hassan BH. Lipoic acid assembly on 2-oxoacid dehydrogenases in E.coli. [Internet] [Doctoral dissertation]. University of Illinois – Urbana-Champaign; 2011. [cited 2020 Apr 03]. Available from: http://hdl.handle.net/2142/24473.

Council of Science Editors:

El Haj Hassan BH. Lipoic acid assembly on 2-oxoacid dehydrogenases in E.coli. [Doctoral Dissertation]. University of Illinois – Urbana-Champaign; 2011. Available from: http://hdl.handle.net/2142/24473

18. Duncan-Gould, Nathan W. An investigation of phase transfer catalysis employing quantitative structure-activity relationships.

Degree: PhD, 0335, 2011, University of Illinois – Urbana-Champaign

 The application of quantitative structure activity relationships to phase transfer catalysis (PTC) has been explored. The primary focus was on hydroxide-initiated PTC reactions, such as… (more)

Subjects/Keywords: phase transfer catalysis; quantitative structure-activity relationship

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

APA (6th Edition):

Duncan-Gould, N. W. (2011). An investigation of phase transfer catalysis employing quantitative structure-activity relationships. (Doctoral Dissertation). University of Illinois – Urbana-Champaign. Retrieved from http://hdl.handle.net/2142/26285

Chicago Manual of Style (16th Edition):

Duncan-Gould, Nathan W. “An investigation of phase transfer catalysis employing quantitative structure-activity relationships.” 2011. Doctoral Dissertation, University of Illinois – Urbana-Champaign. Accessed April 03, 2020. http://hdl.handle.net/2142/26285.

MLA Handbook (7th Edition):

Duncan-Gould, Nathan W. “An investigation of phase transfer catalysis employing quantitative structure-activity relationships.” 2011. Web. 03 Apr 2020.

Vancouver:

Duncan-Gould NW. An investigation of phase transfer catalysis employing quantitative structure-activity relationships. [Internet] [Doctoral dissertation]. University of Illinois – Urbana-Champaign; 2011. [cited 2020 Apr 03]. Available from: http://hdl.handle.net/2142/26285.

Council of Science Editors:

Duncan-Gould NW. An investigation of phase transfer catalysis employing quantitative structure-activity relationships. [Doctoral Dissertation]. University of Illinois – Urbana-Champaign; 2011. Available from: http://hdl.handle.net/2142/26285


University of Illinois – Urbana-Champaign

19. Lukk, Tiit. Discovery of function in the enolase superfamily.

Degree: PhD, 0318, 2010, University of Illinois – Urbana-Champaign

 In the genomic era, advanced sequencing techniques have enabled an exponential growth of the protein sequence databases. Although the abundance of genomic sequences is valuable,… (more)

Subjects/Keywords: enolase superfamily; discovery of function; dipeptide epimerase; glucarate dehydratase; acid sugar dehydratase; x-ray crystal structure; novel function

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

APA (6th Edition):

Lukk, T. (2010). Discovery of function in the enolase superfamily. (Doctoral Dissertation). University of Illinois – Urbana-Champaign. Retrieved from http://hdl.handle.net/2142/14751

Chicago Manual of Style (16th Edition):

Lukk, Tiit. “Discovery of function in the enolase superfamily.” 2010. Doctoral Dissertation, University of Illinois – Urbana-Champaign. Accessed April 03, 2020. http://hdl.handle.net/2142/14751.

MLA Handbook (7th Edition):

Lukk, Tiit. “Discovery of function in the enolase superfamily.” 2010. Web. 03 Apr 2020.

Vancouver:

Lukk T. Discovery of function in the enolase superfamily. [Internet] [Doctoral dissertation]. University of Illinois – Urbana-Champaign; 2010. [cited 2020 Apr 03]. Available from: http://hdl.handle.net/2142/14751.

Council of Science Editors:

Lukk T. Discovery of function in the enolase superfamily. [Doctoral Dissertation]. University of Illinois – Urbana-Champaign; 2010. Available from: http://hdl.handle.net/2142/14751

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