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Kinetic and structural characterization of human mortalin

Kinetic and structural characterization of human mortalin

http://www.wikidata.org/entity/Q33919575

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Crystal structure of the nucleotide-binding domain of mortalin, the mitochondrial Hsp70 chaperone Human mitochondrial Hsp70 (mortalin): shedding light on ATPase activity, interaction with adenosine nucleotides, solution structure and domain organization Overproduction and biophysical characterization of human HSP70 proteins.Ubiquitin-like (UBX)-domain-containing protein, UBXN2A, promotes cell death by interfering with the p53-Mortalin interactions in colon cancer cells Regulation of human Nfu activity in Fe-S cluster delivery-characterization of the interaction between Nfu and the HSPA9/Hsc20 chaperone complex.Understanding the Molecular Basis of Multiple Mitochondrial Dysfunctions Syndrome 1 (MMDS1)-Impact of a Disease-Causing Gly208Cys Substitution on Structure and Activity of NFU1 in the Fe/S Cluster Biosynthetic Pathway.TP53 status regulates ACSL5-induced expression of mitochondrial mortalin in enterocytes and colorectal adenocarcinomas.

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Kinetic and structural characterization of human mortalin

http://www.wikidata.org/entity/Q33919575

description

2010 nî lūn-bûn

@nan

2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի փետրվարին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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Kinetic and structural characterization of human mortalin

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Kinetic and structural characterization of human mortalin

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Kinetic and structural characterization of human mortalin

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Kinetic and structural characterization of human mortalin

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Kinetic and structural characterization of human mortalin

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Kinetic and structural characterization of human mortalin

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J.PEP.2010.02.003

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Protein Expression and Purification

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Kinetic and structural characterization of human mortalin

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Eric Dizin

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James A Cowan

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Taejin Yoon

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Wen-I Luo

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Mechanisms of tryptophan fluorescence shifts in proteins

Crystal Structures of the 70-kDa Heat Shock Proteins in Domain Disjoining Conformation

Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate

How to measure and predict the molar absorption coefficient of a protein

Ssq1, a mitochondrial Hsp70 involved in iron-sulfur (Fe/S) center biogenesis. Similarities to and differences from its bacterial counterpart.

Role of the mitochondrial Hsp70s, Ssc1 and Ssq1, in the maturation of Yfh1

Mortalin: present and prospective

Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function

Kinetics of molecular chaperone action

Solubilization and refolding of bacterial inclusion body proteins

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