The family of hepatoma-derived growth factor proteins: characterization of a new member HRP-4 and classification of its subfamilies. - Wikidata - wikimedia - TriplyDB

The family of hepatoma-derived growth factor proteins: characterization of a new member HRP-4 and classification of its subfamilies.

The family of hepatoma-derived growth factor proteins: characterization of a new member HRP-4 and classification of its subfamilies.

http://www.wikidata.org/entity/Q31054311

about

Hepatoma-derived growth factor represses SET and MYND domain containing 1 gene expression through interaction with C-terminal binding protein Lens epithelium-derived growth factor deSumoylation by Sumo-specific protease-1 regulates its transcriptional activation of small heat shock protein and the cellular response Transient and stable knockdown of the integrase cofactor LEDGF/p75 reveals its role in the replication cycle of human immunodeficiency virus Virological and cellular roles of the transcriptional coactivator LEDGF/p75 Expression of hepatoma-derived growth factor family members in the adult central nervous system.Impact of Chromatin on HIV Replication HIV-1 integrase forms stable tetramers and associates with LEDGF/p75 protein in human cells Identification of an evolutionarily conserved domain in human lens epithelium-derived growth factor/transcriptional co-activator p75 (LEDGF/p75) that binds HIV-1 integrase Solution structure of the PWWP domain of the hepatoma-derived growth factor family Hepatoma-derived growth factor is a neurotrophic factor harbored in the nucleus Hepatoma-derived growth factor-related protein-3 interacts with microtubules and promotes neurite outgrowth in mouse cortical neurons Interaction of HRP-2 isoforms with HDGF: chromatin binding of a specific heteromer Expression patterns and different subcellular localization of the growth factors HDGF (hepatoma-derived growth factor) and HRP-3 (HDGF-related protein-3) suggest functions in addition to their mitogenic activity Characterization of LEDGF/p75 genetic variants and association with HIV-1 disease progression.Dynamics of the ternary complex formed by c-Myc interactor JPO2, transcriptional co-activator LEDGF/p75, and chromatin.LEDGF hybrids efficiently retarget lentiviral integration into heterochromatin.LEDGF/p75-independent HIV-1 replication demonstrates a role for HRP-2 and remains sensitive to inhibition by LEDGINs Hepatoma-derived growth factor and nucleolin exist in the same ribonucleoprotein complex.The same site on the integrase-binding domain of lens epithelium-derived growth factor is a therapeutic target for MLL leukemia and HIV.Association of polymorphisms in the LEDGF/p75 gene (PSIP1) with susceptibility to HIV-1 infection and disease progression.Rationale for clinical trials of coagulation: reactive drugs in hepatocellular carcinoma.Hepatoma-derived growth factor-related protein 2 promotes DNA repair by homologous recombination.Alternative splicing and caspase-mediated cleavage generate antagonistic variants of the stress oncoprotein LEDGF/p75.Heparan sulfate proteoglycans: structure, protein interactions and cell signaling.The significance of autoantibodies to DFS70/LEDGFp75 in health and disease: integrating basic science with clinical understanding.Hepatoma-Derived Growth Factor: Its Possible Involvement in the Progression of Hepatocellular Carcinoma.LEDGF (p75) promotes DNA-end resection and homologous recombination.Secretion of hepatoma-derived growth factor is regulated by N-terminal processing.Docetaxel-induced prostate cancer cell death involves concomitant activation of caspase and lysosomal pathways and is attenuated by LEDGF/p75.RNA-sequencing of bipolar disorder lymphoblastoid cell lines implicates the neurotrophic factor HRP-3 in lithium's clinical efficacy.Cellular cofactors of lentiviral integrase: from target validation to drug discovery.SUMOylation of the hepatoma-derived growth factor negatively influences its binding to chromatin.Cell surface heparan sulfates mediate internalization of the PWWP/HATH domain of HDGF via macropinocytosis to fine-tune cell signalling processes involved in fibroblast cell migration.Insight into the inhibitory mechanism and binding mode between D77 and HIV-1 integrase by molecular modeling methods.Domain swapping and SMYD1 interactions with the PWWP domain of human hepatoma-derived growth factor.

P2860

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P2860

The family of hepatoma-derived growth factor proteins: characterization of a new member HRP-4 and classification of its subfamilies.

http://www.wikidata.org/entity/Q31054311

description

2002 nî lūn-bûn

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2002 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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2002 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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Biochemical Journal

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The family of hepatoma-derived ...... sification of its subfamilies.

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P2093

Frank Dietz

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Hideji Nakamura

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Joachim Kappler

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Kenya Yoshida

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Sebastian Franken

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Volkmar Gieselmann

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P2860

Isolation of cDNAs encoding novel transcription coactivators p52 and p75 reveals an alternate regulatory mechanism of transcriptional activation

A new member of a hepatoma-derived growth factor gene family can translocate to the nucleus

Molecular cloning of complementary DNA for a novel human hepatoma-derived growth factor. Its homology with high mobility group-1 protein

Arylsulfatase A pseudodeficiency: loss of a polyadenylylation signal and N-glycosylation site

Nuclear activities of basic fibroblast growth factor: potentiation of low-serum growth mediated by natural or chimeric nuclear localization signals

Lens epithelium-derived growth factor (LEDGF/p75) and p52 are derived from a single gene by alternative splicing

Lens epithelium-derived growth factor: effects on growth and survival of lens epithelial cells, keratinocytes, and fibroblasts

Hepatoma-derived growth factor stimulates cell growth after translocation to the nucleus by nuclear localization signals

Interactions of neural glycosaminoglycans and proteoglycans with protein ligands: assessment of selectivity, heterogeneity and the participation of core proteins in binding

Hepatoma-derived growth factor belongs to a gene family in mice showing significant homology in the amino terminus

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491-500

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10.1042/BJ20011811

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P433

Pt 2

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P478

366

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2002-09-01T00:00:00Z

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11365157

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12006088

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1222785

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