Ubiquitin not only serves as a tag but also assists degradation by inducing protein unfolding.
about
Genome-Wide Survey of Gut Fungi (Harpellales) Reveals the First Horizontally Transferred Ubiquitin Gene from a Mosquito HostArginine phosphorylation marks proteins for degradation by a Clp proteaseDisordered proteinaceous machinesNon-degradative Ubiquitination of Protein Kinases.Direct ubiquitin independent recognition and degradation of a folded protein by the eukaryotic proteasomes-origin of intrinsic degradation signals.Protein unfolding by biological unfoldases: insights from modeling.Paradigms of protein degradation by the proteasome.PolyUbiquitin chain linkage topology selects the functions from the underlying binding landscapeModulation of folding kinetics of repeat proteins: interplay between intra- and interdomain interactions.Nonnative interactions regulate folding and switching of myristoylated protein.The ubiquitin ligase Ubr4 controls stability of podocin/MEC-2 supercomplexes.The E3 ubiquitin ligase UBE3C enhances proteasome processivity by ubiquitinating partially proteolyzed substrates.Context-dependent resistance to proteolysis of intrinsically disordered proteins.Protein quality control in the ER: balancing the ubiquitin checkbook.Structural insights into specificity and diversity in mechanisms of ubiquitin recognition by ubiquitin-binding domains.Site-specific monoubiquitination activates Ras by impeding GTPase-activating protein functionThe direction of protein entry into the proteasome determines the variety of products and depends on the force needed to unfold its two termini.Biological and Physicochemical Functions of Ubiquitylation Revealed by Synthetic Chemistry Approaches.Ubiquitylation Directly Induces Fold Destabilization of ProteinsNonspecific yet decisive: Ubiquitination can affect the native-state dynamics of the modified protein.Structural propensities of human ubiquitination sites: accessibility, centrality and local conformation.Thermodynamic Protein Destabilization by GFP Tagging: A Case of Interdomain Allostery.Sequence composition of disordered regions fine-tunes protein half-life.Tripartite degrons confer diversity and specificity on regulated protein degradation in the ubiquitin-proteasome system.The origins and evolution of ubiquitination sites.Hsp70 chaperones use ATP to remodel native protein oligomers and stable aggregates by entropic pulling.
P2860
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P2860
Ubiquitin not only serves as a tag but also assists degradation by inducing protein unfolding.
description
2010 nî lūn-bûn
@nan
2010 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Ubiquitin not only serves as a ...... by inducing protein unfolding.
@ast
Ubiquitin not only serves as a ...... by inducing protein unfolding.
@en
type
label
Ubiquitin not only serves as a ...... by inducing protein unfolding.
@ast
Ubiquitin not only serves as a ...... by inducing protein unfolding.
@en
prefLabel
Ubiquitin not only serves as a ...... by inducing protein unfolding.
@ast
Ubiquitin not only serves as a ...... by inducing protein unfolding.
@en
P2860
P356
P1476
Ubiquitin not only serves as a ...... by inducing protein unfolding.
@en
P2093
Tzachi Hagai
Yaakov Levy
P2860
P304
P356
10.1073/PNAS.0912335107
P407
P577
2010-01-13T00:00:00Z