Probing the affinity of SecA for signal peptide in different environments. - Wikidata - awgldk - TriplyDB

Probing the affinity of SecA for signal peptide in different environments.

Probing the affinity of SecA for signal peptide in different environments.

http://www.wikidata.org/entity/Q34979875

about

SecA, a remarkable nanomachine Use of synthetic signal sequences to explore the protein export machinery.Analysis of SecA dimerization in solution.Mapping of the signal peptide-binding domain of Escherichia coli SecA using Förster resonance energy transfer.Energetics of SecA dimerization.Mapping of the SecA signal peptide binding site and dimeric interface by using the substituted cysteine accessibility method The use of analytical sedimentation velocity to extract thermodynamic linkage.In Vitro Interaction of the Housekeeping SecA1 with the Accessory SecA2 Protein of Mycobacterium tuberculosis.Selective photoaffinity labeling identifies the signal peptide binding domain on SecA Oligomeric states of the SecA and SecYEG core components of the bacterial Sec translocon Interactions that drive Sec-dependent bacterial protein transport.Conserved SecA Signal Peptide-Binding Site Revealed by Engineered Protein Chimeras and Förster Resonance Energy Transfer.Defining the solution state dimer structure of Escherichia coli SecA using Förster resonance energy transfer Cryo-electron microscopic structure of SecA protein bound to the 70S ribosome.Fluorescence spectroscopy of soluble E. coli SPase I Δ2-75 reveals conformational changes in response to ligand binding.The Canonical and Accessory Sec System of Gram-positive Bacteria.Characterization of the Escherichia coli SecA signal peptide-binding site.Defining the Escherichia coli SecA dimer interface residues through in vivo site-specific photo-cross-linking.Alignment of the protein substrate hairpin along the SecA two-helix finger primes protein transport in Escherichia coli.In vivo membrane topology of Escherichia coli SecA ATPase reveals extensive periplasmic exposure of multiple functionally important domains clustering on one face of SecA.

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P2860

Probing the affinity of SecA for signal peptide in different environments.

http://www.wikidata.org/entity/Q34979875

description

2005 nî lūn-bûn

@nan

2005 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2005年の論文

@ja

2005年論文

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2005年論文

@zh-hant

2005年論文

@zh-hk

2005年論文

@zh-mo

2005年論文

@zh-tw

2005年论文

@wuu

name

Probing the affinity of SecA for signal peptide in different environments.

@ast

Probing the affinity of SecA for signal peptide in different environments.

@en

Probing the affinity of SecA for signal peptide in different environments.

@nl

type

label

Probing the affinity of SecA for signal peptide in different environments.

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Probing the affinity of SecA for signal peptide in different environments.

@en

Probing the affinity of SecA for signal peptide in different environments.

@nl

prefLabel

Probing the affinity of SecA for signal peptide in different environments.

@ast

Probing the affinity of SecA for signal peptide in different environments.

@en

Probing the affinity of SecA for signal peptide in different environments.

@nl

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Probing the affinity of SecA for signal peptide in different environments.

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Debra A Kendall

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

Monika Musial-Siwek

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

Sharyn L Rusch

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

P2860

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA

Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase

X-ray structure of a protein-conducting channel

Sam35 of the mitochondrial protein sorting and assembly machinery is a peripheral outer membrane protein essential for cell viability.

Cross-talk between catalytic and regulatory elements in a DEAD motor domain is essential for SecA function.

Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis

How to measure and analyze tryptophan fluorescence in membranes properly, and why bother?

A large conformational change of the translocation ATPase SecA

The Sec system.

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13987-13996

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

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scholarly article

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10.1021/BI050882K

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42

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44

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2005-10-01T00:00:00Z

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7537908

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16229488

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3094106

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