Role of then+1 amino acid residue on the deamidation of asparagine in pentapeptides-Reference-Cited by-同舟云学术

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Role of then+1 amino acid residue on the deamidation of asparagine in pentapeptides

Published:2015-07-27 Issue:23 Volume:113 Page:3839-3848
ISSN:0026-8976
Container-title:Molecular Physics
language:en
Short-container-title:Molecular Physics

Author:

Ince Hasan H.,Konuklar F. Aylin Sungur,Ugur Ilke,Ozcan Ö. Alaz,Sayadi Maryam,Feig Michael,Aviyente Viktorya

Funder

TUBITAK

ULAKBIM High Performance and Grid Computing Center, DPT

Boğaziçi University

Publisher

Informa UK Limited

Subject

Physical and Theoretical Chemistry,Condensed Matter Physics,Molecular Biology,Biophysics

Link

http://www.tandfonline.com/doi/pdf/10.1080/00268976.2015.1068394

Reference55 articles.

1. Structure-dependent nonenzymatic deamidation of glutaminyl and asparaginyl pentapeptides

2. Formulation considerations for proteins susceptible to asparagine deamidation and aspartate isomerization

3. Deamidation of Glutaminyl and Asparaginyl Residues in Peptides and Proteins

4. Deamidation Affects Structural and Functional Properties of Human αA-Crystallin and Its Oligomerization with αB-Crystallin

5. Deamidation of labile asparagine residues in the autoregulatory sequence of human phenylalanine hydroxylase

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1. Stability of Protein Pharmaceuticals: Recent Advances;Pharmaceutical Research;2024-06-27

2. Predicting deamidation and isomerization sites in therapeutic antibodies using structure-based in silico approaches;mAbs;2024-03-28

3. Protein deamidation in biopharmaceutical manufacture: understanding, control and impact;Journal of Chemical Technology & Biotechnology;2015-12-08

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