subject:(oligosaccharyltransferase)

NSYSU

1. Chen, Chien-ming. A study of OSTC/DC2, a novel subunit of oligosaccharyltransferase, after heat shock.

Degree: PhD, Biological Sciences, 2014, NSYSU

URL: http://etd.lib.nsysu.edu.tw/ETD-db/ETD-search/view_etd?URN=etd-0111114-133314

► OSTC, a Homo sapiens OSTC/DC2 protein, belongs to a new subunit of mammalian oligosaccharyltransferase (OST). OST transfers the high-mannose sugars to nascent polypeptides during N-linked… (more)

Subjects/Keywords: oligosaccharyltransferase; polyclonal antibody; gene knockdown; heat shock; glycosylation; glycoprotein

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

APA (6^th Edition):

Chen, C. (2014). A study of OSTC/DC2, a novel subunit of oligosaccharyltransferase, after heat shock. (Doctoral Dissertation). NSYSU. Retrieved from http://etd.lib.nsysu.edu.tw/ETD-db/ETD-search/view_etd?URN=etd-0111114-133314

Chicago Manual of Style (16^th Edition):

Chen, Chien-ming. “A study of OSTC/DC2, a novel subunit of oligosaccharyltransferase, after heat shock.” 2014. Doctoral Dissertation, NSYSU. Accessed January 18, 2021. http://etd.lib.nsysu.edu.tw/ETD-db/ETD-search/view_etd?URN=etd-0111114-133314.

MLA Handbook (7^th Edition):

Chen, Chien-ming. “A study of OSTC/DC2, a novel subunit of oligosaccharyltransferase, after heat shock.” 2014. Web. 18 Jan 2021.

Vancouver:

Chen C. A study of OSTC/DC2, a novel subunit of oligosaccharyltransferase, after heat shock. [Internet] [Doctoral dissertation]. NSYSU; 2014. [cited 2021 Jan 18]. Available from: http://etd.lib.nsysu.edu.tw/ETD-db/ETD-search/view_etd?URN=etd-0111114-133314.

Council of Science Editors:

Chen C. A study of OSTC/DC2, a novel subunit of oligosaccharyltransferase, after heat shock. [Doctoral Dissertation]. NSYSU; 2014. Available from: http://etd.lib.nsysu.edu.tw/ETD-db/ETD-search/view_etd?URN=etd-0111114-133314

Universidade do Rio Grande do Sul

2. Pedebos, Conrado. Estrutura e dinâmica de oligossacariltransferases procarióticas.

Degree: 2017, Universidade do Rio Grande do Sul

URL: http://hdl.handle.net/10183/180493

►

A N-glicosilação é uma modificação distribuída de forma abundante nos domínios da vida, e é caracterizada pelo reconhecimento de uma assinatura N-X-S/T nas proteínas-alvo. O… (more)

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A N-glicosilação é uma modificação distribuída de forma abundante nos domínios da vida, e é caracterizada pelo reconhecimento de uma assinatura N-X-S/T nas proteínas-alvo. O último passo dessa via biossintética é a transferência em bloco da cadeia glicídica para a asparagina da assinatura de N-glicosilação, sendo realizada pelas oligossacariltransferases (OSTs) PglB (Bacteria), AglB (Archaea) e STT3 (Eukarya). Dados cristalográficos para essas enzimas identificaram suas divisões em subunidades estruturais, como o núcleo central (CC), a sequência inserida (IS) e a periferia (P1 e P2). A unidade CC é fundamental para a interação com o substrato e a catálise, enquanto hipóteses da literatura sugerem que as outras unidades são importantes para a estabilidade estrutural das OSTs. Em decorrência do emprego desses sistemas enzimáticos em glicoengenharia de proteínas e no desenvolvimento de vacinas, a compreensão da origem estrutural para suas propriedades catalíticas e para a seletividade por substratos pode contribuir diretamente para o desenvolvimento de novas aplicações tecnológicas. Nesse âmbito, a presente tese avalia aspectos estruturais e conformacionais das OSTs, assim como a potencial função de suas unidades estruturais. Para tanto, empregamos a técnica de dinâmica molecular nas duas OSTs caracterizadas até o momento: a PglB de Campylobacter lari e a AglB de Archaeoglobus fulgidus. Desta forma, observamos a plasticidade conformacional do sítio ativo da PglB, com variações em elementos importantes, como a alça externa 5(EL5) e os resíduos catalíticos, sob influência da complexação dos substratos. Verificamos ainda que interações com as N-acetilações da glicana podem influenciar na seletividade desse substrato. Quanto à AglB, obtivemos evidências estruturais para propostas prévias da literatura de um papel termoestabilizador das unidades IS e P1 em relação à unidade CC. Nesse sentido, a presente tese esclareceu importantes aspectos estruturais e funcionais de OSTs, oferecendo suporte para o planejamento de novos experimentos e de aplicações tecnológicas. As novas informações sobre o mecanismo de seletividade da PglB podem auxiliar no desenvolvimento de glicoproteínas portando monossacarídeos específicos, potencialmente úteis para a produção de vacinas e de biomoléculas com uso terapêutico.

N-glycosylation is a modification broadly distributed in all domains of life. It is characterized by a sequence motif N-X-S/T in proteins that portray this glycan chain. The last step of the oligosaccharide biosynthetic pathway is the en bloc transfer of the glycan chain to the Asn from the motif. This reactions is performed by enzimes named oligosaccharyltransferases PglB (Bacteria), AglB (Archaea), and STT3 (Eukarya). Previous crystallography data identified subdivisions in the OST domains, such as the central core (CC), the inserted sequence (IS), and the peripheries (P1 and P2). CC unit is essential to the interaction with substrates and catalysis. Hypothesis from the literature suggests that the other units are important…

Advisors/Committee Members: Verli, Hugo.

Subjects/Keywords: Oligossacariltransferase; Oligosaccharyltransferase; Glicosilação; Molecular Dynamics; Dinâmica molecular; N-glycosylation

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APA (6^th Edition):

Pedebos, C. (2017). Estrutura e dinâmica de oligossacariltransferases procarióticas. (Thesis). Universidade do Rio Grande do Sul. Retrieved from http://hdl.handle.net/10183/180493

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

Chicago Manual of Style (16^th Edition):

Pedebos, Conrado. “Estrutura e dinâmica de oligossacariltransferases procarióticas.” 2017. Thesis, Universidade do Rio Grande do Sul. Accessed January 18, 2021. http://hdl.handle.net/10183/180493.

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

MLA Handbook (7^th Edition):

Pedebos, Conrado. “Estrutura e dinâmica de oligossacariltransferases procarióticas.” 2017. Web. 18 Jan 2021.

Vancouver:

Pedebos C. Estrutura e dinâmica de oligossacariltransferases procarióticas. [Internet] [Thesis]. Universidade do Rio Grande do Sul; 2017. [cited 2021 Jan 18]. Available from: http://hdl.handle.net/10183/180493.

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

Council of Science Editors:

Pedebos C. Estrutura e dinâmica de oligossacariltransferases procarióticas. [Thesis]. Universidade do Rio Grande do Sul; 2017. Available from: http://hdl.handle.net/10183/180493

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

Cornell University

3. Pampuro, Richard. Expanding A Toolkit For Characterization Of Transmembrane Proteins.

Degree: M.S., Chemical Engineering, Chemical Engineering, 2014, Cornell University

URL: http://hdl.handle.net/1813/38917

Subjects/Keywords: protein engineering; membrane proteins; antibody engineering; oligosaccharyltransferase

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APA (6^th Edition):

Pampuro, R. (2014). Expanding A Toolkit For Characterization Of Transmembrane Proteins. (Masters Thesis). Cornell University. Retrieved from http://hdl.handle.net/1813/38917

Chicago Manual of Style (16^th Edition):

Pampuro, Richard. “Expanding A Toolkit For Characterization Of Transmembrane Proteins.” 2014. Masters Thesis, Cornell University. Accessed January 18, 2021. http://hdl.handle.net/1813/38917.

MLA Handbook (7^th Edition):

Pampuro, Richard. “Expanding A Toolkit For Characterization Of Transmembrane Proteins.” 2014. Web. 18 Jan 2021.

Vancouver:

Pampuro R. Expanding A Toolkit For Characterization Of Transmembrane Proteins. [Internet] [Masters thesis]. Cornell University; 2014. [cited 2021 Jan 18]. Available from: http://hdl.handle.net/1813/38917.

Council of Science Editors:

Pampuro R. Expanding A Toolkit For Characterization Of Transmembrane Proteins. [Masters Thesis]. Cornell University; 2014. Available from: http://hdl.handle.net/1813/38917

4. TU HAITAO. A GLOBAL PROFILE OF YEAST GENES INVOLVED IN AGROBACTERIUM- YEAST GENE TRANFER.

Degree: 2010, National University of Singapore

URL: http://scholarbank.nus.edu.sg/handle/10635/25922

Subjects/Keywords: Agrobacterium tumefaciens; yeast; gene transfer; oligosaccharyltransferase; glycosylation; OST3

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

APA (6^th Edition):

HAITAO, T. (2010). A GLOBAL PROFILE OF YEAST GENES INVOLVED IN AGROBACTERIUM- YEAST GENE TRANFER. (Thesis). National University of Singapore. Retrieved from http://scholarbank.nus.edu.sg/handle/10635/25922

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

Chicago Manual of Style (16^th Edition):

HAITAO, TU. “A GLOBAL PROFILE OF YEAST GENES INVOLVED IN AGROBACTERIUM- YEAST GENE TRANFER.” 2010. Thesis, National University of Singapore. Accessed January 18, 2021. http://scholarbank.nus.edu.sg/handle/10635/25922.

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

MLA Handbook (7^th Edition):

HAITAO, TU. “A GLOBAL PROFILE OF YEAST GENES INVOLVED IN AGROBACTERIUM- YEAST GENE TRANFER.” 2010. Web. 18 Jan 2021.

Vancouver:

HAITAO T. A GLOBAL PROFILE OF YEAST GENES INVOLVED IN AGROBACTERIUM- YEAST GENE TRANFER. [Internet] [Thesis]. National University of Singapore; 2010. [cited 2021 Jan 18]. Available from: http://scholarbank.nus.edu.sg/handle/10635/25922.

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

Council of Science Editors:

HAITAO T. A GLOBAL PROFILE OF YEAST GENES INVOLVED IN AGROBACTERIUM- YEAST GENE TRANFER. [Thesis]. National University of Singapore; 2010. Available from: http://scholarbank.nus.edu.sg/handle/10635/25922

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

ETH Zürich

5. Spirig, Urs. The oligosaccharyltransferase complex of Saccharomyces cerevisiae.

Degree: 1999, ETH Zürich

URL: http://hdl.handle.net/20.500.11850/144014

Subjects/Keywords: BIERHEFE (MIKROBIOTECHNOLOGIE); OLIGOSACCHARYLTRANSFERASE (ENZYME); BREWERS YEAST (MICROBIOTECHNOLOGY); OLIGOSACCHARYLTRANSFERASE (ENZYMES); info:eu-repo/classification/ddc/570; Life sciences

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

APA (6^th Edition):

Spirig, U. (1999). The oligosaccharyltransferase complex of Saccharomyces cerevisiae. (Doctoral Dissertation). ETH Zürich. Retrieved from http://hdl.handle.net/20.500.11850/144014

Chicago Manual of Style (16^th Edition):

Spirig, Urs. “The oligosaccharyltransferase complex of Saccharomyces cerevisiae.” 1999. Doctoral Dissertation, ETH Zürich. Accessed January 18, 2021. http://hdl.handle.net/20.500.11850/144014.

MLA Handbook (7^th Edition):

Spirig, Urs. “The oligosaccharyltransferase complex of Saccharomyces cerevisiae.” 1999. Web. 18 Jan 2021.

Vancouver:

Spirig U. The oligosaccharyltransferase complex of Saccharomyces cerevisiae. [Internet] [Doctoral dissertation]. ETH Zürich; 1999. [cited 2021 Jan 18]. Available from: http://hdl.handle.net/20.500.11850/144014.

Council of Science Editors:

Spirig U. The oligosaccharyltransferase complex of Saccharomyces cerevisiae. [Doctoral Dissertation]. ETH Zürich; 1999. Available from: http://hdl.handle.net/20.500.11850/144014

University of Michigan

6. Khanna, Hemant. Studies towards the photoaffinity labeling of oligosaccharyltransferase (OST).

Degree: PhD, Pure Sciences, 2002, University of Michigan

URL: http://hdl.handle.net/2027.42/129756

► This thesis investigates the feasibility of a kinetic method to detect photoaffinity labeling of the enzyme, oligosaccharyltransferase (OST) by an alternate substrate, Bz-Asn-Bpa-Thr-NH₂. Additionally, photoaffinity… (more)

Subjects/Keywords: Benzophenone; Enzyme Inactivation; Lipid-linked Disaccharides; Oligosaccharyltransferase; Ost; Photoaffinity Labeling; Studies; Towards

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

APA (6^th Edition):

Khanna, H. (2002). Studies towards the photoaffinity labeling of oligosaccharyltransferase (OST). (Doctoral Dissertation). University of Michigan. Retrieved from http://hdl.handle.net/2027.42/129756

Chicago Manual of Style (16^th Edition):

Khanna, Hemant. “Studies towards the photoaffinity labeling of oligosaccharyltransferase (OST).” 2002. Doctoral Dissertation, University of Michigan. Accessed January 18, 2021. http://hdl.handle.net/2027.42/129756.

MLA Handbook (7^th Edition):

Khanna, Hemant. “Studies towards the photoaffinity labeling of oligosaccharyltransferase (OST).” 2002. Web. 18 Jan 2021.

Vancouver:

Khanna H. Studies towards the photoaffinity labeling of oligosaccharyltransferase (OST). [Internet] [Doctoral dissertation]. University of Michigan; 2002. [cited 2021 Jan 18]. Available from: http://hdl.handle.net/2027.42/129756.

Council of Science Editors:

Khanna H. Studies towards the photoaffinity labeling of oligosaccharyltransferase (OST). [Doctoral Dissertation]. University of Michigan; 2002. Available from: http://hdl.handle.net/2027.42/129756

University of Michigan

7. Lee, Jung S. Chemical and biochemical studies on oligosaccharyltransferase: A key enzyme in N-linked glycoprotein biosynthesis.

Degree: PhD, Pure Sciences, 1991, University of Michigan

URL: http://hdl.handle.net/2027.42/128754

► To elucidate the mechanism of the reaction catalyzed by yeast oligosaccharyl-transferase (OST, E.C. 2.4.1.119), the substrates have been truncated to meet the minimum requirements for… (more)

Subjects/Keywords: Biochemical; Biosynthesis; Chemical; Enzyme; Glycoprotein; Key; Linked; Oligosaccharyltransferas; Oligosaccharyltransferase; Studies

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

APA (6^th Edition):

Lee, J. S. (1991). Chemical and biochemical studies on oligosaccharyltransferase: A key enzyme in N-linked glycoprotein biosynthesis. (Doctoral Dissertation). University of Michigan. Retrieved from http://hdl.handle.net/2027.42/128754

Chicago Manual of Style (16^th Edition):

Lee, Jung S. “Chemical and biochemical studies on oligosaccharyltransferase: A key enzyme in N-linked glycoprotein biosynthesis.” 1991. Doctoral Dissertation, University of Michigan. Accessed January 18, 2021. http://hdl.handle.net/2027.42/128754.

MLA Handbook (7^th Edition):

Lee, Jung S. “Chemical and biochemical studies on oligosaccharyltransferase: A key enzyme in N-linked glycoprotein biosynthesis.” 1991. Web. 18 Jan 2021.

Vancouver:

Lee JS. Chemical and biochemical studies on oligosaccharyltransferase: A key enzyme in N-linked glycoprotein biosynthesis. [Internet] [Doctoral dissertation]. University of Michigan; 1991. [cited 2021 Jan 18]. Available from: http://hdl.handle.net/2027.42/128754.

Council of Science Editors:

Lee JS. Chemical and biochemical studies on oligosaccharyltransferase: A key enzyme in N-linked glycoprotein biosynthesis. [Doctoral Dissertation]. University of Michigan; 1991. Available from: http://hdl.handle.net/2027.42/128754

ETH Zürich

8. Wacker, Michael. N-linked protein glycosylation: from eukaroytes to bacteria.

Degree: 2002, ETH Zürich

URL: http://hdl.handle.net/20.500.11850/146715

Subjects/Keywords: GLYKOSYLIERUNGSREAKTIONEN + GLYKOSYLIERUNG (BIOCHEMIE); EUKARYOTEN (BIOLOGIE); OLIGOSACCHARYLTRANSFERASE (ENZYME); GLYCOSYLATION REACTIONS + GLYCOSYLATION (BIOCHEMISTRY); EUCARYOTES (BIOLOGY); OLIGOSACCHARYLTRANSFERASE (ENZYMES); info:eu-repo/classification/ddc/570; Life sciences

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

APA (6^th Edition):

Wacker, M. (2002). N-linked protein glycosylation: from eukaroytes to bacteria. (Doctoral Dissertation). ETH Zürich. Retrieved from http://hdl.handle.net/20.500.11850/146715

Chicago Manual of Style (16^th Edition):

Wacker, Michael. “N-linked protein glycosylation: from eukaroytes to bacteria.” 2002. Doctoral Dissertation, ETH Zürich. Accessed January 18, 2021. http://hdl.handle.net/20.500.11850/146715.

MLA Handbook (7^th Edition):

Wacker, Michael. “N-linked protein glycosylation: from eukaroytes to bacteria.” 2002. Web. 18 Jan 2021.

Vancouver:

Wacker M. N-linked protein glycosylation: from eukaroytes to bacteria. [Internet] [Doctoral dissertation]. ETH Zürich; 2002. [cited 2021 Jan 18]. Available from: http://hdl.handle.net/20.500.11850/146715.

Council of Science Editors:

Wacker M. N-linked protein glycosylation: from eukaroytes to bacteria. [Doctoral Dissertation]. ETH Zürich; 2002. Available from: http://hdl.handle.net/20.500.11850/146715

University of Michigan

9. Srinivasan, Anjali. Oligosaccharyltransferase: Development of a new assay and the synthesis of isotopically labeled substrates for use in the determination of kinetic isotope effects.

Degree: PhD, Pure Sciences, 2004, University of Michigan

URL: http://hdl.handle.net/2027.42/124187

► This research has focused on determining if the enzyme oligosaccharyl-transferase (OST, EC 2.4.1.119) operates through an electrophilic-activation mechanism. OST catalyzes the transfer of a saccharide… (more)

Subjects/Keywords: Assay; Biotin-capture Assays; Determination; Development; Effects; Glycosylation; Isotopically Labeled Substrates; Kinetic Isotope; New; Oligosaccharyl Transferase; Oligosaccharyltransferase; Synthesis; Use

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

APA (6^th Edition):

Srinivasan, A. (2004). Oligosaccharyltransferase: Development of a new assay and the synthesis of isotopically labeled substrates for use in the determination of kinetic isotope effects. (Doctoral Dissertation). University of Michigan. Retrieved from http://hdl.handle.net/2027.42/124187

Chicago Manual of Style (16^th Edition):

Srinivasan, Anjali. “Oligosaccharyltransferase: Development of a new assay and the synthesis of isotopically labeled substrates for use in the determination of kinetic isotope effects.” 2004. Doctoral Dissertation, University of Michigan. Accessed January 18, 2021. http://hdl.handle.net/2027.42/124187.

MLA Handbook (7^th Edition):

Srinivasan, Anjali. “Oligosaccharyltransferase: Development of a new assay and the synthesis of isotopically labeled substrates for use in the determination of kinetic isotope effects.” 2004. Web. 18 Jan 2021.

Vancouver:

Srinivasan A. Oligosaccharyltransferase: Development of a new assay and the synthesis of isotopically labeled substrates for use in the determination of kinetic isotope effects. [Internet] [Doctoral dissertation]. University of Michigan; 2004. [cited 2021 Jan 18]. Available from: http://hdl.handle.net/2027.42/124187.

Council of Science Editors:

Srinivasan A. Oligosaccharyltransferase: Development of a new assay and the synthesis of isotopically labeled substrates for use in the determination of kinetic isotope effects. [Doctoral Dissertation]. University of Michigan; 2004. Available from: http://hdl.handle.net/2027.42/124187

University of Michigan

10. Xu, Tong. Design, synthesis, and evaluation of unnatural amino acid-containing peptides as mechanistic probes and inhibitors of oligosaccharyltransferase.

Degree: PhD, Pure Sciences, 1998, University of Michigan

URL: http://hdl.handle.net/2027.42/131136

► Oligosaccharyltransferase (OST, EC 2.4.1.119), is a membrane-bound, multimeric enzyme which catalyzes a key reaction in the formation of N-linked glycoproteins. During the OST-catalyzed reaction, the… (more)

▼ Oligosaccharyltransferase (OST, EC 2.4.1.119), is a membrane-bound, multimeric enzyme which catalyzes a key reaction in the formation of N-linked glycoproteins. During the OST-catalyzed reaction, the oligosaccharyl portion of Glc₃Man₉GlcNAc₂-PP-Dolichol is transferred to the β-amido group of an asparagine moiety in the growing polypeptide chain. The catalytic mechanism of OST is not clear, and unnatural amino acid-containing peptides have been synthesized and used to study this intriguing reaction. The carboxamide moiety that links the carbohydrate and protein moieties has been unambiguously determined to arise intact from asparagine by the use of chemically synthesized Bz- (4-¹³C, ¹⁵N) Asn-Leu-Thr-NH₂ as an OST substrate. Bz- (4-¹³C) Asn-Leu-Thr-NH₂ was also synthesized and used to evaluate a proposed mechanism of OST catalysis similar to glutamine-dependent amidotransferases using ¹⁵NH₄OAc as a potential external nucleophile. Analysis of NMR and MS spectra of the isotopically-labeled peptides and the resulting biosynthesized glycopeptides indicates that free ¹⁵NH₃ is not lost from the doubly labeled substrate during catalysis nor can exogenous ¹⁵NH₃ intercept any of several postulated enzyme-bound species. These results indicate that OST-catalyzed glycosylation does not follow a mechanism involving the transient generation of exchangeable NH₃. 5-diazo-4-oxo-L-norvaline, 4-oxo-L-norvaline, and S-methanesulfinyl-L-alanine have been incorporated into three separate tripeptides wherein these non-natural amino acids replace Asn in a known tripeptide substrate of OST. The three synthetic tripeptides showed no activity as substrates and only weak activity as inhibitors of OST at concentrations that were 10-35 times the K_m for the corresponding Asn-containing tripeptide substrate. A benzophenone photophore was incorporated into peptides as potential photoaffinity labels of OST. Bz-Asn-Bpa-Thr-NH₂ and Bz-Asn-Lys ((4-Bz)Bz) -Thr-NH₂ were found to be good alternate substrates. They were also good competitive inhibitors vs standard peptide substrate (¹⁴C) Bz-Asn-Leu-Thr-NH₂ and their K_i values were determined. Advisors/Committee Members: Coward, James K. (advisor).

Subjects/Keywords: Acid; Amino; Containing; Design; Enzyme Inhibition; Evaluation; Inhibitionamino; Inhibitors; Mechanistic; Oligosaccharyltransferas; Oligosaccharyltransferase; Peptides; Probes; Synthesis; Unnatural

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

APA (6^th Edition):

Xu, T. (1998). Design, synthesis, and evaluation of unnatural amino acid-containing peptides as mechanistic probes and inhibitors of oligosaccharyltransferase. (Doctoral Dissertation). University of Michigan. Retrieved from http://hdl.handle.net/2027.42/131136

Chicago Manual of Style (16^th Edition):

Xu, Tong. “Design, synthesis, and evaluation of unnatural amino acid-containing peptides as mechanistic probes and inhibitors of oligosaccharyltransferase.” 1998. Doctoral Dissertation, University of Michigan. Accessed January 18, 2021. http://hdl.handle.net/2027.42/131136.

MLA Handbook (7^th Edition):

Xu, Tong. “Design, synthesis, and evaluation of unnatural amino acid-containing peptides as mechanistic probes and inhibitors of oligosaccharyltransferase.” 1998. Web. 18 Jan 2021.

Vancouver:

Xu T. Design, synthesis, and evaluation of unnatural amino acid-containing peptides as mechanistic probes and inhibitors of oligosaccharyltransferase. [Internet] [Doctoral dissertation]. University of Michigan; 1998. [cited 2021 Jan 18]. Available from: http://hdl.handle.net/2027.42/131136.

Council of Science Editors:

Xu T. Design, synthesis, and evaluation of unnatural amino acid-containing peptides as mechanistic probes and inhibitors of oligosaccharyltransferase. [Doctoral Dissertation]. University of Michigan; 1998. Available from: http://hdl.handle.net/2027.42/131136

ETH Zürich

11. Schwarz, Flavio. Reading and engineering N-linked protein glycosilation in Escherichia coli.

Degree: 2010, ETH Zürich

URL: http://hdl.handle.net/20.500.11850/152358

Subjects/Keywords: GLYKOSYLIERUNGSREAKTIONEN + GLYKOSYLIERUNG (BIOCHEMIE); POSTTRANSLATIONELLE PROTEINMODIFIKATION; POLYSACCHARIDE (BIOCHEMIE); OLIGOSACCHARYLTRANSFERASE (ENZYME); CAMPYLOBACTER (MIKROBIOLOGIE); GLYKOPROTEINE + GLYKOPEPTIDE (BIOCHEMIE); ENZYMAKTIVITÄT (BIOCHEMIE); GLYCOSYLATION REACTIONS + GLYCOSYLATION (BIOCHEMISTRY); POST-TRANSLATIONAL PROTEIN MODIFICATION; POLYSACCHARIDES (BIOCHEMISTRY); OLIGOSACCHARYLTRANSFERASE (ENZYMES); CAMPYLOBACTER (MICROBIOLOGY); GLYCOPROTEINS + GLYCOPEPTIDES (BIOCHEMISTRY); ENZYMATIC ACTIVITY (BIOCHEMISTRY); info:eu-repo/classification/ddc/570; Life sciences

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

APA (6^th Edition):

Schwarz, F. (2010). Reading and engineering N-linked protein glycosilation in Escherichia coli. (Doctoral Dissertation). ETH Zürich. Retrieved from http://hdl.handle.net/20.500.11850/152358

Chicago Manual of Style (16^th Edition):

Schwarz, Flavio. “Reading and engineering N-linked protein glycosilation in Escherichia coli.” 2010. Doctoral Dissertation, ETH Zürich. Accessed January 18, 2021. http://hdl.handle.net/20.500.11850/152358.

MLA Handbook (7^th Edition):

Schwarz, Flavio. “Reading and engineering N-linked protein glycosilation in Escherichia coli.” 2010. Web. 18 Jan 2021.

Vancouver:

Schwarz F. Reading and engineering N-linked protein glycosilation in Escherichia coli. [Internet] [Doctoral dissertation]. ETH Zürich; 2010. [cited 2021 Jan 18]. Available from: http://hdl.handle.net/20.500.11850/152358.

Council of Science Editors:

Schwarz F. Reading and engineering N-linked protein glycosilation in Escherichia coli. [Doctoral Dissertation]. ETH Zürich; 2010. Available from: http://hdl.handle.net/20.500.11850/152358

ETH Zürich

12. Ngwa, Elsy Mankah. Eukaryotic Oligosaccharyltransferase - A structure-function characterisation of Saccharomyces cerevisiae Stt3 protein.

Degree: 2017, ETH Zürich

URL: http://hdl.handle.net/20.500.11850/156312

Subjects/Keywords: BIERHEFE (MIKROBIOTECHNOLOGIE); OLIGOSACCHARYLTRANSFERASE (ENZYME); STRUKTUR-FUNKTIONSBEZIEHUNG DER PROTEINE UND PEPTIDE; GLYKOSYLIERUNGSREAKTIONEN + GLYKOSYLIERUNG (BIOCHEMIE); POSTTRANSLATIONELLE PROTEINMODIFIKATION; BREWERS YEAST (MICROBIOTECHNOLOGY); OLIGOSACCHARYLTRANSFERASE (ENZYMES); STRUCTURE-FUNCTION RELATIONSHIP OF PROTEINS AND PEPTIDES; GLYCOSYLATION REACTIONS + GLYCOSYLATION (BIOCHEMISTRY); POST-TRANSLATIONAL PROTEIN MODIFICATION; info:eu-repo/classification/ddc/570; Life sciences

Record Details Similar Records Cite « Share

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

APA (6^th Edition):

Ngwa, E. M. (2017). Eukaryotic Oligosaccharyltransferase - A structure-function characterisation of Saccharomyces cerevisiae Stt3 protein. (Doctoral Dissertation). ETH Zürich. Retrieved from http://hdl.handle.net/20.500.11850/156312

Chicago Manual of Style (16^th Edition):

Ngwa, Elsy Mankah. “Eukaryotic Oligosaccharyltransferase - A structure-function characterisation of Saccharomyces cerevisiae Stt3 protein.” 2017. Doctoral Dissertation, ETH Zürich. Accessed January 18, 2021. http://hdl.handle.net/20.500.11850/156312.

MLA Handbook (7^th Edition):

Ngwa, Elsy Mankah. “Eukaryotic Oligosaccharyltransferase - A structure-function characterisation of Saccharomyces cerevisiae Stt3 protein.” 2017. Web. 18 Jan 2021.

Vancouver:

Ngwa EM. Eukaryotic Oligosaccharyltransferase - A structure-function characterisation of Saccharomyces cerevisiae Stt3 protein. [Internet] [Doctoral dissertation]. ETH Zürich; 2017. [cited 2021 Jan 18]. Available from: http://hdl.handle.net/20.500.11850/156312.

Council of Science Editors:

Ngwa EM. Eukaryotic Oligosaccharyltransferase - A structure-function characterisation of Saccharomyces cerevisiae Stt3 protein. [Doctoral Dissertation]. ETH Zürich; 2017. Available from: http://hdl.handle.net/20.500.11850/156312

University of Queensland

13. Zhuang, Aowen. Novel role of AGE-R1/OST48 in the metabolome and proteome promoting ER stress in the kidney and liver.

Degree: School of Medicine, 2018, University of Queensland

URL: http://espace.library.uq.edu.au/view/UQ:540

Subjects/Keywords: Diabetic kidney disease; Diabetes; Advanced glycation end-products (AGEs); Oligosaccharyltransferase-48 (OST48); Advanced Glycation End-product Receptor-1 (AGE-R1); Liver fibrosis; Endoplasmic reticulum (ER) stress; Glucose homeostasis; Glomerulosclerosis; Tubulointerstitial Fibrosis (TIF); 0601 Biochemistry and Cell Biology; 0606 Physiology

Record Details Similar Records Cite « Share

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

APA (6^th Edition):

Zhuang, A. (2018). Novel role of AGE-R1/OST48 in the metabolome and proteome promoting ER stress in the kidney and liver. (Thesis). University of Queensland. Retrieved from http://espace.library.uq.edu.au/view/UQ:540

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

Chicago Manual of Style (16^th Edition):

Zhuang, Aowen. “Novel role of AGE-R1/OST48 in the metabolome and proteome promoting ER stress in the kidney and liver.” 2018. Thesis, University of Queensland. Accessed January 18, 2021. http://espace.library.uq.edu.au/view/UQ:540.

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

MLA Handbook (7^th Edition):

Zhuang, Aowen. “Novel role of AGE-R1/OST48 in the metabolome and proteome promoting ER stress in the kidney and liver.” 2018. Web. 18 Jan 2021.

Vancouver:

Zhuang A. Novel role of AGE-R1/OST48 in the metabolome and proteome promoting ER stress in the kidney and liver. [Internet] [Thesis]. University of Queensland; 2018. [cited 2021 Jan 18]. Available from: http://espace.library.uq.edu.au/view/UQ:540.

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

Council of Science Editors:

Zhuang A. Novel role of AGE-R1/OST48 in the metabolome and proteome promoting ER stress in the kidney and liver. [Thesis]. University of Queensland; 2018. Available from: http://espace.library.uq.edu.au/view/UQ:540

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

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Open Access Theses and Dissertations