Human MutS homologue MSH4 physically interacts with von Hippel-Lindau tumor suppressor-binding protein 1 - Test2 - elhamkhani - TriplyDB

Human MutS homologue MSH4 physically interacts with von Hippel-Lindau tumor suppressor-binding protein 1

Human MutS homologue MSH4 physically interacts with von Hippel-Lindau tumor suppressor-binding protein 1

http://www.wikidata.org/entity/Q28210368

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MutS homologue hMSH4: interaction with eIF3f and a role in NHEJ-mediated DSB repair MutS homologue hMSH5: role in cisplatin-induced DNA damage response Evidence for a direct involvement of hMSH5 in promoting ionizing radiation induced apoptosis Meiotic failure in male mice lacking an X-linked factor MEIOB exhibits single-stranded DNA-binding and exonuclease activities and is essential for meiotic recombination Sex, Scavengers, and Chaperones: Transcriptome Secrets of Divergent Symbiodinium Thermal Tolerances.Chaperonin CCT-mediated AIB1 folding promotes the growth of ERα-positive breast cancer cells on hard substrates hMSH5 is a nucleocytoplasmic shuttling protein whose stability depends on its subcellular localization.MBD4 cooperates with DNMT1 to mediate methyl-DNA repression and protects mammalian cells from oxidative stress.MutS homologue hMSH5: recombinational DSB repair and non-synonymous polymorphic variants Prefoldin subunits are protected from ubiquitin-proteasome system-mediated degradation by forming complex with other constituent subunits.Clusterin is a secreted marker for a hypoxia-inducible factor-independent function of the von Hippel-Lindau tumor suppressor protein.MutS Homologues hMSH4 and hMSH5: Genetic Variations, Functions, and Implications in Human Diseases DNA damage induced MutS homologue hMSH4 acetylation.VBP1 facilitates proteasome and autophagy-mediated degradation of MutS homologue hMSH4.Molecular clamp mechanism of substrate binding by hydrophobic coiled-coil residues of the archaeal chaperone prefoldin.Nuclear functions of prefoldin.Systematic Identification of Determinants for Single Strand Annealing Mediated Deletion Formation in Saccharomyces cerevisiae Localization of MLH3 at the centrosomes Heterologous Complementation Studies With the YscX and YscY Protein Families Reveals a Specificity for Yersinia pseudotuberculosis Type III Secretion.

P2860

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P2860

Human MutS homologue MSH4 physically interacts with von Hippel-Lindau tumor suppressor-binding protein 1

http://www.wikidata.org/entity/Q28210368

description

2003 nî lūn-bûn

@nan

2003 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2003年の論文

@ja

2003年論文

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2003年論文

@zh-hant

2003年論文

@zh-hk

2003年論文

@zh-mo

2003年論文

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2003年论文

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name

Human MutS homologue MSH4 phys ...... r suppressor-binding protein 1

@ast

Human MutS homologue MSH4 phys ...... r suppressor-binding protein 1

@en

Human MutS homologue MSH4 phys ...... r suppressor-binding protein 1

@nl

type

label

Human MutS homologue MSH4 phys ...... r suppressor-binding protein 1

@ast

Human MutS homologue MSH4 phys ...... r suppressor-binding protein 1

@en

Human MutS homologue MSH4 phys ...... r suppressor-binding protein 1

@nl

prefLabel

Human MutS homologue MSH4 phys ...... r suppressor-binding protein 1

@ast

Human MutS homologue MSH4 phys ...... r suppressor-binding protein 1

@en

Human MutS homologue MSH4 phys ...... r suppressor-binding protein 1

@nl

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Cancer Research

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Human MutS homologue MSH4 phys ...... r suppressor-binding protein 1

@en

P2093

Chengtao Her

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Feng Zhou

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Michael D Griswold

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Xiling Wu

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scholarly article

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4

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63

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2003-02-01T00:00:00Z

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12591739

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