Literature DB >> 21227875

Molecular evolution of ubiquitin genes.

P M Sharp1, W H Li.   

Abstract

Ubiquitin is a singular protein with multiple functions. It is probably the most slowly evolving protein known, is encoded by genes with a unique structure, and provides an intriguing case study for various aspects of molecular evolution. In particular, the multiple ubiquitin-coding repeats which have been characterized in man, yeast and a slime mould graphically illustrate the dynamics of concerted evolution, but cast doubts on the effectiveness of this process for unlinked arrays in this repeat family.
Copyright © 1987. Published by Elsevier Ltd.

Entities:  

Year:  1987        PMID: 21227875     DOI: 10.1016/0169-5347(87)90108-X

Source DB:  PubMed          Journal:  Trends Ecol Evol        ISSN: 0169-5347            Impact factor:   17.712


  7 in total

1.  Structure and expression of sunflower ubiquitin genes.

Authors:  M N Binet; J H Weil; L H Tessier
Journal:  Plant Mol Biol       Date:  1991-09       Impact factor: 4.076

2.  Phylogenetic relationship of ubiquitin repeats in the polyubiquitin gene from the marine sponge Geodia cydonium.

Authors:  W E Müller; H C Schröder; I M Müller; V Gamulin
Journal:  J Mol Evol       Date:  1994-10       Impact factor: 2.395

Review 3.  Ubiquitin-independent proteasomal degradation.

Authors:  Jenny Erales; Philip Coffino
Journal:  Biochim Biophys Acta       Date:  2013-05-14

Review 4.  Origin and function of ubiquitin-like proteins.

Authors:  Mark Hochstrasser
Journal:  Nature       Date:  2009-03-26       Impact factor: 49.962

5.  Facile Semisynthesis of Ubiquitylated Peptides with the Ligation Auxiliary 2-Aminooxyethanethiol.

Authors:  Caroline E Weller; Champak Chatterjee
Journal:  Methods Mol Biol       Date:  2020

6.  Facile synthesis of native and protease-resistant ubiquitylated peptides.

Authors:  Caroline E Weller; Wei Huang; Champak Chatterjee
Journal:  Chembiochem       Date:  2014-05-18       Impact factor: 3.164

7.  Aromatic thiol-mediated cleavage of N-O bonds enables chemical ubiquitylation of folded proteins.

Authors:  Caroline E Weller; Abhinav Dhall; Feizhi Ding; Edlaine Linares; Samuel D Whedon; Nicholas A Senger; Elizabeth L Tyson; John D Bagert; Xiaosong Li; Ohara Augusto; Champak Chatterjee
Journal:  Nat Commun       Date:  2016-09-29       Impact factor: 14.919

  7 in total

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