Characterization of the VHL tumor suppressor gene product: localization, complex formation, and the effect of natural inactivating mutations
about
Human N-myristoyltransferase amino-terminal domain involved in targeting the enzyme to the ribosomal subcellular fractionInhibition of transcription elongation by the VHL tumor suppressor proteinBinding of the von Hippel-Lindau tumor suppressor protein to Elongin B and CTranscription-dependent nuclear-cytoplasmic trafficking is required for the function of the von Hippel-Lindau tumor suppressor proteinThe von Hippel-Lindau tumor-suppressor gene product forms a stable complex with human CUL-2, a member of the Cdc53 family of proteinsDown-regulation of transmembrane carbonic anhydrases in renal cell carcinoma cell lines by wild-type von Hippel-Lindau transgenesComputational and experimental characterization of dVHL establish a Drosophila model of VHL syndromeThe novel WD-repeat protein Morg1 acts as a molecular scaffold for hypoxia-inducible factor prolyl hydroxylase 3 (PHD3)The inducible elongin A elongation activation domain: structure, function and interaction with the elongin BC complexOxygen-dependent ubiquitination and degradation of hypoxia-inducible factor requires nuclear-cytoplasmic trafficking of the von Hippel-Lindau tumor suppressor proteinVHL induces renal cell differentiation and growth arrest through integration of cell-cell and cell-extracellular matrix signaling.Characterization of the expression, localization, and secretion of PANDER in alpha-cells.Von Hippel-Lindau gene deletion and expression of hypoxia-inducible factor and ubiquitin in optic nerve hemangioma.Tumor suppression and transcription elongation: the dire consequences of changing partners.Diverse effects of mutations in exon II of the von Hippel-Lindau (VHL) tumor suppressor gene on the interaction of pVHL with the cytosolic chaperonin and pVHL-dependent ubiquitin ligase activity.Regulation of microtubule stability by the von Hippel-Lindau tumour suppressor protein pVHL.Hypoxia inducible factor activates the transforming growth factor-alpha/epidermal growth factor receptor growth stimulatory pathway in VHL(-/-) renal cell carcinoma cells.The von Hippel-Lindau tumor suppressor protein: roles in cancer and oxygen sensing.The von Hippel-Lindau tumor suppressor gene is required for cell cycle exit upon serum withdrawalpVHL19 is a biologically active product of the von Hippel-Lindau gene arising from internal translation initiationThe von Hippel-Lindau tumor suppressor protein is a component of an E3 ubiquitin-protein ligase activity.The Elongin BC complex interacts with the conserved SOCS-box motif present in members of the SOCS, ras, WD-40 repeat, and ankyrin repeat familiesA second major native von Hippel-Lindau gene product, initiated from an internal translation start site, functions as a tumor suppressor.Neurologic manifestations of von Hippel-Lindau diseaseAllosteric effects in the marginally stable von Hippel-Lindau tumor suppressor protein and allostery-based rescue mutant design.Current understanding of the molecular mechanisms of kidney cancer: a primer for urologists.Structural insights into the folding defects of oncogenic pVHL lead to correction of its function in vitro.Emerging drugs for the treatment of metastatic renal cancer.Elongin BC complex prevents degradation of von Hippel-Lindau tumor suppressor gene products.Nuclear/cytoplasmic localization of the von Hippel-Lindau tumor suppressor gene product is determined by cell density.Pancreatic lesions in von Hippel-Lindau disease? A systematic review and meta-synthesis of the literature.Phosphorylation-dependent cleavage regulates von Hippel Lindau proteostasis and function.Structure, function and regulation of jade family PHD finger 1 (JADE1).The von Hippel-Lindau tumor suppressor gene product interacts with Sp1 to repress vascular endothelial growth factor promoter activity.Hypoxia-inducible factor linked to differential kidney cancer risk seen with type 2A and type 2B VHL mutations.Development of a cell-based reporter assay for screening of inhibitors of hypoxia-inducible factor 2-induced gene expression.Subcellular localization of the von Hippel-Lindau disease gene product is cell cycle-dependent.Gene knockout and transgenic technologies in risk assessment: the next generation.An integrated computational approach can classify VHL missense mutations according to risk of clear cell renal carcinoma.William Kaelin, Peter Ratcliffe, and Gregg Semenza receive the 2016 Albert Lasker Basic Medical Research Award.
P2860
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P2860
Characterization of the VHL tumor suppressor gene product: localization, complex formation, and the effect of natural inactivating mutations
description
1995 nî lūn-bûn
@nan
1995 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Characterization of the VHL tu ...... natural inactivating mutations
@ast
Characterization of the VHL tu ...... natural inactivating mutations
@en
Characterization of the VHL tu ...... natural inactivating mutations
@en-gb
Characterization of the VHL tu ...... natural inactivating mutations
@nl
type
label
Characterization of the VHL tu ...... natural inactivating mutations
@ast
Characterization of the VHL tu ...... natural inactivating mutations
@en
Characterization of the VHL tu ...... natural inactivating mutations
@en-gb
Characterization of the VHL tu ...... natural inactivating mutations
@nl
prefLabel
Characterization of the VHL tu ...... natural inactivating mutations
@ast
Characterization of the VHL tu ...... natural inactivating mutations
@en
Characterization of the VHL tu ...... natural inactivating mutations
@en-gb
Characterization of the VHL tu ...... natural inactivating mutations
@nl
P2093
P2860
P356
P1476
Characterization of the VHL tu ...... natural inactivating mutations
@en
P2093
J R Gnarra
J S Humphrey
J Sukegawa
R D Klausner
W M Linehan
P2860
P304
P356
10.1073/PNAS.92.14.6459
P407
P577
1995-07-03T00:00:00Z