Multimodal assessment of protein functional deficiency supports pathogenicity of BRCA1 p.V1688del. - Wikidata - awgldk - TriplyDB

Multimodal assessment of protein functional deficiency supports pathogenicity of BRCA1 p.V1688del.

Multimodal assessment of protein functional deficiency supports pathogenicity of BRCA1 p.V1688del.

http://www.wikidata.org/entity/Q37356517

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P.Arg82Leu von Hippel-Lindau (VHL) gene mutation among three members of a family with familial bilateral pheochromocytoma in India: molecular analysis and in silico characterization.A natural product-like JAK2/STAT3 inhibitor induces apoptosis of malignant melanoma cells.Prognostic value of CtIP/RBBP8 expression in breast cancer.Edgotype: a fundamental link between genotype and phenotype.A comparison of cosegregation analysis methods for the clinical setting.Novel synthetic derivatives of the natural product berbamine inhibit Jak2/Stat3 signaling and induce apoptosis of human melanoma cells.Collective evidence supports neutrality of BRCA1 V1687I, a novel sequence variant in the conserved THV motif of the first BRCT repeat.

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Multimodal assessment of protein functional deficiency supports pathogenicity of BRCA1 p.V1688del.

http://www.wikidata.org/entity/Q37356517

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 25 August 2009

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Multimodal assessment of prote ...... ogenicity of BRCA1 p.V1688del.

@en

Multimodal assessment of prote ...... ogenicity of BRCA1 p.V1688del.

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type

label

Multimodal assessment of prote ...... ogenicity of BRCA1 p.V1688del.

@en

Multimodal assessment of prote ...... ogenicity of BRCA1 p.V1688del.

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prefLabel

Multimodal assessment of prote ...... ogenicity of BRCA1 p.V1688del.

@en

Multimodal assessment of prote ...... ogenicity of BRCA1 p.V1688del.

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0008-5472.CAN-09-1440

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Cancer Research

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Multimodal assessment of prote ...... ogenicity of BRCA1 p.V1688del.

@en

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Arcangela De Nicolo

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

Emilio Parisini

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

Judy E Garber

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Kathryn A Stoeckert

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Marc Vidal

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Maurizia Dalla Palma

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Michael E Cusick

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

Quan Zhong

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P2860

BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function

BRCA1 interacts with FHL2 and enhances FHL2 transactivation function

The BRCT domain is a phospho-protein binding domain

DNA damage-induced cell cycle checkpoint control requires CtIP, a phosphorylation-dependent binding partner of BRCA1 C-terminal domains

Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains

BRCA1 interacts with components of the histone deacetylase complex

BRCA1: cell cycle checkpoint, genetic instability, DNA damage response and cancer evolution

Crystal structure of the BRCT repeat region from the breast cancer-associated protein BRCA1

Comparative protein modelling by satisfaction of spatial restraints

The RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutation

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7030-7037

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scholarly article

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10.1158/0008-5472.CAN-09-1440

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17

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69

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Katherine L Nathanson

Maria Adelaide Caligo

Susan M Domchek

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2009-08-25T00:00:00Z

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19706752

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2748232

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