Literature DB >> 20221930

Prediction of posttranslational modification of proteins from their amino acid sequence.

Birgit Eisenhaber1, Frank Eisenhaber.   

Abstract

If posttranslational modifications (PTMs) are chemical alterations of the protein primary structure during the protein's life cycle as a result of an enzymatic reaction, then the motif in the substrate protein sequence that is recognized by the enzyme can serve as basis for predictor construction that recognizes PTM sites in database sequences. The recognition motif consists generally of two regions: first, a small, central segment that enters the catalytic cleft of the enzyme and that is specific for this type of PTM and, second, a sequence environment of about 10 or more residues with linker characteristics (a trend for small and polar residues with flexible backbone) on either side of the central part that are needed to provide accessibility of the central segment to the enzyme's catalytic site. In this review, we consider predictors for cleavage of targeting signals, lipid PTMs, phosphorylation, and glycosylation.

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Year:  2010        PMID: 20221930     DOI: 10.1007/978-1-60327-241-4_21

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  23 in total

1.  PIRSitePredict for protein functional site prediction using position-specific rules.

Authors:  Chuming Chen; Qinghua Wang; Hongzhan Huang; Cholanayakanahalli R Vinayaka; John S Garavelli; Cecilia N Arighi; Darren A Natale; Cathy H Wu
Journal:  Database (Oxford)       Date:  2019-01-01       Impact factor: 3.451

2.  A novel model to predict O-glycosylation sites using a highly unbalanced dataset.

Authors:  Kun Zhou; Chunzhi Ai; Peipei Dong; Xuran Fan; Ling Yang
Journal:  Glycoconj J       Date:  2012-08-03       Impact factor: 2.916

Review 3.  Conditionally and transiently disordered proteins: awakening cryptic disorder to regulate protein function.

Authors:  Ursula Jakob; Richard Kriwacki; Vladimir N Uversky
Journal:  Chem Rev       Date:  2014-02-06       Impact factor: 60.622

4.  The structural and functional signatures of proteins that undergo multiple events of post-translational modification.

Authors:  Vikas Pejaver; Wei-Lun Hsu; Fuxiao Xin; A Keith Dunker; Vladimir N Uversky; Predrag Radivojac
Journal:  Protein Sci       Date:  2014-06-11       Impact factor: 6.725

Review 5.  Mathematical descriptions of biochemical networks: stability, stochasticity, evolution.

Authors:  Simon Rosenfeld
Journal:  Prog Biophys Mol Biol       Date:  2011-03-22       Impact factor: 3.667

6.  Purification and crystallization of yeast glycosylphosphatidylinositol transamidase subunit PIG-S (PIG-S(71-467)).

Authors:  Neelagandan Kamariah; Frank Eisenhaber; Sharmila Adhikari; Birgit Eisenhaber; Gerhard Grüber
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2011-07-19

7.  dictyBase 2015: Expanding data and annotations in a new software environment.

Authors:  Siddhartha Basu; Petra Fey; David Jimenez-Morales; Robert J Dodson; Rex L Chisholm
Journal:  Genesis       Date:  2015-07-08       Impact factor: 2.487

8.  Comprehensive Quantification of Carboxymethyllysine-Modified Peptides in Human Plasma.

Authors:  Arvind M Korwar; Qibin Zhang
Journal:  J Am Soc Mass Spectrom       Date:  2021-01-29       Impact factor: 3.109

Review 9.  Classification of intrinsically disordered regions and proteins.

Authors:  Robin van der Lee; Marija Buljan; Benjamin Lang; Robert J Weatheritt; Gary W Daughdrill; A Keith Dunker; Monika Fuxreiter; Julian Gough; Joerg Gsponer; David T Jones; Philip M Kim; Richard W Kriwacki; Christopher J Oldfield; Rohit V Pappu; Peter Tompa; Vladimir N Uversky; Peter E Wright; M Madan Babu
Journal:  Chem Rev       Date:  2014-04-29       Impact factor: 60.622

10.  Identification of Peptide lv, a novel putative neuropeptide that regulates the expression of L-type voltage-gated calcium channels in photoreceptors.

Authors:  Liheng Shi; Michael L Ko; Louise C Abbott; Gladys Y-P Ko
Journal:  PLoS One       Date:  2012-08-13       Impact factor: 3.240

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