Functional characterization of a small heat shock protein from Mycobacterium leprae - Wikidata - wikimedia - TriplyDB

Functional characterization of a small heat shock protein from Mycobacterium leprae

Functional characterization of a small heat shock protein from Mycobacterium leprae

http://www.wikidata.org/entity/Q33387974

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Interaction of ATP with a small heat shock protein from Mycobacterium leprae: effect on its structure and function Small heat-shock protein HspL is induced by VirB protein(s) and promotes VirB/D4-mediated DNA transfer in Agrobacterium tumefaciens.Characterization of rice small heat shock proteins targeted to different cellular organelles.Role of Subunit Exchange and Electrostatic Interactions on the Chaperone Activity of Mycobacterium leprae HSP18 A S52P mutation in the 'α-crystallin domain' of Mycobacterium leprae HSP18 reduces its oligomeric size and chaperone function.Regulation of the 18 kDa heat shock protein in Mycobacterium ulcerans: an alpha-crystallin orthologue that promotes biofilm formation.

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P2860

Functional characterization of a small heat shock protein from Mycobacterium leprae

http://www.wikidata.org/entity/Q33387974

description

2008 nî lūn-bûn

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2008 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

Functional characterization of a small heat shock protein from Mycobacterium leprae

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Functional characterization of a small heat shock protein from Mycobacterium leprae

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type

label

Functional characterization of a small heat shock protein from Mycobacterium leprae

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Functional characterization of a small heat shock protein from Mycobacterium leprae

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prefLabel

Functional characterization of a small heat shock protein from Mycobacterium leprae

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Functional characterization of a small heat shock protein from Mycobacterium leprae

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1471-2180-8-208

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BMC Microbiology

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Functional characterization of a small heat shock protein from Mycobacterium leprae

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Elengikal Abdul Azeez Rehna

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Jayapal Jeya Maheshwari

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Kuppamuthu Dharmalingam

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Nallakandy Panagadan Shankernarayan

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Nirmala Lini

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

Sugathan Shiburaj

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P2860

Massive gene decay in the leprosy bacillus

Synechocystis HSP17 is an amphitropic protein that stabilizes heat-stressed membranes and binds denatured proteins for subsequent chaperone-mediated refolding

Encapsulated Escherichia coli in alginate beads capable of secreting a heterologous pectin lyase

The stress-responsive chaperone alpha-crystallin 2 is required for pathogenesis of Mycobacterium tuberculosis

Mycobacterium tuberculosis 16-kDa antigen (Hsp16.3) functions as an oligomeric structure in vitro to suppress thermal aggregation

The Mycobacterium tuberculosis small heat shock protein Hsp16.3 exposes hydrophobic surfaces at mild conditions: conformational flexibility and molecular chaperone activity

The use of protein structure/activity relationships in the rational design of stable particulate delivery systems.

The small heat shock proteins and their role in human disease.

Serum proteome of leprosy patients undergoing erythema nodosum leprosum reaction: regulation of expression of the isoforms of haptoglobin.

Molecular chaperones: small heat shock proteins in the limelight.

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1471-2180-8-208

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208

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scholarly article

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10.1186/1471-2180-8-208

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8

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2008-11-28T00:00:00Z

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23553698

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1051822148

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19040732

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Mycobacterium leprae

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2629775

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