Mutations in the Hydrophobic Core of Ubiquitin Differentially Affect Its Recognition by Receptor Proteins - sprookjes - yvandenbroek - TriplyDB

Mutations in the Hydrophobic Core of Ubiquitin Differentially Affect Its Recognition by Receptor Proteins

Mutations in the Hydrophobic Core of Ubiquitin Differentially Affect Its Recognition by Receptor Proteins

http://www.wikidata.org/entity/Q27649198

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Conformational Dynamics and Structural Plasticity Play Critical Roles in the Ubiquitin Recognition of a UIM Domain Structural Dissection of a Gating Mechanism Preventing Misactivation of Ubiquitin by NEDD8’s E1 † ‡Conformational dynamics control ubiquitin-deubiquitinase interactions and influence in vivo signaling Solution structure of lysine-free (K0) ubiquitin Systematic exploration of ubiquitin sequence, E1 activation efficiency, and experimental fitness in yeast Long-lived states to monitor protein unfolding by proton NMR A high throughput mutagenic analysis of yeast sumo structure and function.Using protein motion to read, write, and erase ubiquitin signals.Analyses of the effects of all ubiquitin point mutants on yeast growth rate.Allosteric switch regulates protein-protein binding through collective motion.Pressure effects on the ensemble dynamics of ubiquitin inspected with molecular dynamics simulations and isotropic reorientational eigenmode dynamics.Alanine scan of core positions in ubiquitin reveals links between dynamics, stability, and function.The role of ubiquitin-binding domains in human pathophysiology.ESA-UbiSite: accurate prediction of human ubiquitination sites by identifying a set of effective negatives.The degradation of p53 and its major E3 ligase Mdm2 is differentially dependent on the proteasomal ubiquitin receptor S5a.A designed conformational shift to control protein binding specificity.DNA-damage-inducible 1 protein (Ddi1) contains an uncharacteristic ubiquitin-like domain that binds ubiquitin.When the Scaffold Cannot Be Ignored: The Role of the Hydrophobic Core in Ligand Binding and Specificity.Binding affinities controlled by shifting conformational equilibria: opportunities and limitations.Together, Rpn10 and Dsk2 can serve as a polyubiquitin chain-length sensor.Phosphorylation of ubiquitin at Ser65 affects its polymerization, targets, and proteome-wide turnover.Interactions Controlling the Slow Dynamic Conformational Motions of Ubiquitin.

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P2860

Mutations in the Hydrophobic Core of Ubiquitin Differentially Affect Its Recognition by Receptor Proteins

http://www.wikidata.org/entity/Q27649198

description

2008 nî lūn-bûn

@nan

2008 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2008年の論文

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2008年論文

@yue

2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

name

Mutations in the Hydrophobic C ...... cognition by Receptor Proteins

@ast

Mutations in the Hydrophobic C ...... cognition by Receptor Proteins

@en

Mutations in the Hydrophobic C ...... cognition by Receptor Proteins

@nl

type

label

Mutations in the Hydrophobic C ...... cognition by Receptor Proteins

@ast

Mutations in the Hydrophobic C ...... cognition by Receptor Proteins

@en

Mutations in the Hydrophobic C ...... cognition by Receptor Proteins

@nl

prefLabel

Mutations in the Hydrophobic C ...... cognition by Receptor Proteins

@ast

Mutations in the Hydrophobic C ...... cognition by Receptor Proteins

@en

Mutations in the Hydrophobic C ...... cognition by Receptor Proteins

@nl

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J.JMB.2007.11.016

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Journal of Molecular Biology

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Mutations in the Hydrophobic C ...... cognition by Receptor Proteins

@en

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Aydin Haririnia

http://www.w3.org/2001/XMLSchema#string

David Fushman

http://www.w3.org/2001/XMLSchema#string

Michael Z Twarog

http://www.w3.org/2001/XMLSchema#string

Nisha Purohit

http://www.w3.org/2001/XMLSchema#string

Rati Verma

http://www.w3.org/2001/XMLSchema#string

Raymond J Deshaies

http://www.w3.org/2001/XMLSchema#string

P2860

Isolation of a polypeptide that has lymphocyte-differentiating properties and is probably represented universally in living cells

Cdc53/cullin and the essential Hrt1 RING-H2 subunit of SCF define a ubiquitin ligase module that activates the E2 enzyme Cdc34

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Solution structure and dynamics of a designed hydrophobic core variant of ubiquitin

Binding surface mapping of intra- and interdomain interactions among hHR23B, ubiquitin, and polyubiquitin binding site 2 of S5a

Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra

Protein backbone angle restraints from searching a database for chemical shift and sequence homology

Proteasome subunit Rpn1 binds ubiquitin-like protein domains.

Identification of ubiquitin-like protein-binding subunits of the 26S proteasome.

Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome.

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979-96

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10.1016/J.JMB.2007.11.016

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375

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18054791

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2254529

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