Structural basis of the specificity of USP18 toward ISG15.
about
ISGylation - a key to lock the cell gates for preventing the spread of threats.The Role of Interferons in Inflammation and Inflammasome Activation.A Naturally Occurring Recombinant Enterovirus Expresses a Torovirus Deubiquitinase.Regulation of the Tumor-Suppressor BECLIN 1 by Distinct Ubiquitination Cascades.Extracellular ISG15 Signals Cytokine Secretion through the LFA-1 Integrin Receptor.How USP18 deals with ISG15-modified proteins: structural basis for the specificity of the protease.Irreversible inactivation of ISG15 by a viral leader protease enables alternative infection detection strategies.Evidence for the ISG15-Specific Deubiquitinase USP18 as an Antineoplastic Target.The structure of the deubiquitinase USP15 reveals a misaligned catalytic triad and an open ubiquitin-binding channelSpecificity for deubiquitination of monoubiquitinated FANCD2 is driven by the N-terminus of USP1
P2860
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P2860
Structural basis of the specificity of USP18 toward ISG15.
description
2017 nî lūn-bûn
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2017年の論文
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2017年学术文章
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2017年学术文章
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Structural basis of the specificity of USP18 toward ISG15.
@en
type
label
Structural basis of the specificity of USP18 toward ISG15.
@en
prefLabel
Structural basis of the specificity of USP18 toward ISG15.
@en
P2093
P2860
P356
P1476
Structural basis of the specificity of USP18 toward ISG15.
@en
P2093
Anja Basters
Annika Röcker
Günter Fritz
Katharina F Witting
Klaus-Peter Knobeloch
Marta S Semrau
Paola Storici
Roya Tadayon
Sandra Hess
P2860
P2888
P304
P356
10.1038/NSMB.3371
P577
2017-02-06T00:00:00Z