Results 341 to 350 of about 574,104 (383)
Some of the next articles are maybe not open access.

The Ubiquitin Code

Annual Review of Biochemistry, 2012
The posttranslational modification with ubiquitin, a process referred to as ubiquitylation, controls almost every process in cells. Ubiquitin can be attached to substrate proteins as a single moiety or in the form of polymeric chains in which successive ubiquitin molecules are connected through specific isopeptide bonds.
David Komander, Michael Rape
openaire   +4 more sources

The Ubiquitin Code in the Ubiquitin-Proteasome System and Autophagy

Trends in Biochemical Sciences, 2017
The conjugation of the 76 amino acid protein ubiquitin to other proteins can alter the metabolic stability or non-proteolytic functions of the substrate. Once attached to a substrate (monoubiquitination), ubiquitin can itself be ubiquitinated on any of its seven lysine (Lys) residues or its N-terminal methionine (Met1).
Aaron Ciechanover   +2 more
openaire   +3 more sources

The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction.

Physiological Reviews, 2002
Between the 1960s and 1980s, most life scientists focused their attention on studies of nucleic acids and the translation of the coded information. Protein degradation was a neglected area, considered to be a nonspecific, dead-end process.
M. Glickman, A. Ciechanover
semanticscholar   +1 more source

The measurement of ubiquitin and ubiquitinated proteins

Electrophoresis, 1999
Ubiquitination of key cellular proteins involved in signal transduction, gene transcription and cell-cycle regulation usually condemns those proteins to proteasomal or lysosomal degradation. Additionally, cycles of reversible ubiquitination regulate the function of certain proteins in a manner analogous to phosphorylation.
Len Neckers   +2 more
openaire   +3 more sources

RING domain E3 ubiquitin ligases.

Annual Review of Biochemistry, 2009
E3 ligases confer specificity to ubiquitination by recognizing target substrates and mediating transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to substrate.
R. Deshaies, C. Joazeiro
semanticscholar   +1 more source

Ubiquitin and ubiquitin conjugates in human lens

Experimental Eye Research, 1992
Ubiquitin, an 8.5 kDa polypeptide found almost universally in plants and animals, is a normal component in the lens. The best documented function for ubiquitin involves its conjugation to proteins as a signal to initiate degradation. Conjugates for ubiquitin-dependent degradation tend to be of very high molecular mass and are rapidly degraded.
Deanna E. Cyr   +3 more
openaire   +3 more sources

THE UBIQUITIN SYSTEM [PDF]

open access: possibleAnnual Review of Biochemistry, 1998
The selective degradation of many short-lived proteins in eukaryotic cells is carried out by the ubiquitin system. In this pathway, proteins are targeted for degradation by covalent ligation to ubiquitin, a highly conserved small protein. Ubiquitin-mediated degradation of regulatory proteins plays important roles in the control of numerous processes ...
Aaron Ciechanover, Avram Hershko
openaire   +2 more sources

Ubiquitin Ligases: Structure, Function, and Regulation.

Annual Review of Biochemistry, 2017
Ubiquitin E3 ligases control every aspect of eukaryotic biology by promoting protein ubiquitination and degradation. At the end of a three-enzyme cascade, ubiquitin ligases mediate the transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to ...
N. Zheng, N. Shabek
semanticscholar   +1 more source

Activation of Ubiquitin and Ubiquitin-Like Proteins

2010
Attachment of ubiquitin and ubiquitin-like proteins to cellular targets represents a fundamental regulatory strategy within eukaryotes and exhibits remarkably pleiotropic effects on cell function. These posttranslational modifications share a common mechanism comprised of three steps: an activating enzyme to couple ATP hydrolysis to formation of a high-
Frederick C. Streich, Arthur L. Haas
openaire   +2 more sources

Home - About - Disclaimer - Privacy