Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine. - Wikidata - thesis-toulmin - TriplyDB

Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine.

Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine.

http://www.wikidata.org/entity/Q30473723

about

A polypeptide-DNA hybrid with selective linking capability applied to single molecule nano-mechanical measurements using optical tweezers Cellobiohydrolase 1 from Trichoderma reesei degrades cellulose in single cellobiose steps Nucleotide Binding and Conformational Switching in the Hexameric Ring of a AAA+ Machine Spiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocation Mitochondrial protein quality control: the mechanisms guarding mitochondrial health Cooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregation An asymmetric interface between the regulatory and core particles of the proteasome Complete subunit architecture of the proteasome regulatory particle Conformational switching of the 26S proteasome enables substrate degradation Common features at the start of the neurodegeneration cascade Disordered proteinaceous machines Direct observation of a force-induced switch in the anisotropic mechanical unfolding pathway of a protein.Stepwise unfolding of a β barrel protein by the AAA+ ClpXP protease.High-resolution optical tweezers for single-molecule manipulation.Atomic force microscopy with sub-picoNewton force stability for biological applications.Optical trapping of individual human immunodeficiency viruses in culture fluid reveals heterogeneity with single-molecule resolution.Mechanical operation and intersubunit coordination of ring-shaped molecular motors: insights from single-molecule studies Protein folding and unfolding under force The N-end rule pathway and regulation by proteolysis ClpXP, an ATP-powered unfolding and protein-degradation machine Dynamic and static components power unfolding in topologically closed rings of a AAA+ proteolytic machine.Differentiation of the DnaA-oriC subcomplex for DNA unwinding in a replication initiation complex.Mechanochemical basis of protein degradation by a double-ring AAA+ machine Protein unfolding by biological unfoldases: insights from modeling.Mechanisms of cellular proteostasis: insights from single-molecule approaches A force-activated trip switch triggers rapid dissociation of a colicin from its immunity protein.Computer simulation of assembly and co-operativity of hexameric AAA ATPases Regulated protein turnover: snapshots of the proteasome in action.Proteasomal degradation from internal sites favors partial proteolysis via remote domain stabilization.Assaying the kinetics of protein denaturation catalyzed by AAA+ unfolding machines and proteases Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpX Spring-loaded unraveling of a single SNARE complex by NSF in one round of ATP turnover Dynamics of equilibrium folding and unfolding transitions of titin immunoglobulin domain under constant forces.The molten globule state is unusually deformable under mechanical force.Protein unfolding and degradation by the AAA+ Lon protease.Coarse-Grained Simulations of Topology-Dependent Mechanisms of Protein Unfolding and Translocation Mediated by ClpY ATPase Nanomachines Processive ATP-driven substrate disassembly by the N-ethylmaleimide-sensitive factor (NSF) molecular machine.The mechanochemistry of copper reports on the directionality of unfolding in model cupredoxin proteins.Ubp6 deubiquitinase controls conformational dynamics and substrate degradation of the 26S proteasome.Sequence- and species-dependence of proteasomal processivity.

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Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine.

http://www.wikidata.org/entity/Q30473723

description

2011 nî lūn-bûn

@nan

2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2011年の論文

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2011年論文

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2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

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name

Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine.

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Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine.

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type

label

Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine.

@ast

Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine.

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prefLabel

Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine.

@ast

Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine.

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J.CELL.2011.03.036

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Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine

@en

P2093

Adrian O Olivares

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

Marie-Eve Aubin-Tam

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

Matthew J Lang

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

Tania A Baker

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

P2860

Direct observation of base-pair stepping by RNA polymerase

The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system

Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine.

The repeating segments of the F-actin cross-linking gelation factor (ABP-120) have an immunoglobulin-like fold

The bacteriophage straight phi29 portal motor can package DNA against a large internal force

Entropic elasticity of lambda-phage DNA

Targeting proteins for degradation

AAA+ proteins: have engine, will work

Exploring the energy landscape of GFP by single-molecule mechanical experiments.

Adhesion through single peptide aptamers.

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257-267

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10.1016/J.CELL.2011.03.036

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3108460

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