HIV-1 Tat protein-mediated transactivation of the HIV-1 long terminal repeat promoter is potentiated by a novel nuclear Tat-interacting protein of 110 kDa, Tip110 (Q28215081)

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scientific article (publication date: 28 June 2002)

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English	HIV-1 Tat protein-mediated transactivation of the HIV-1 long terminal repeat promoter is potentiated by a novel nuclear Tat-interacting protein of 110 kDa, Tip110	scientific article (publication date: 28 June 2002)

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scholarly article

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HIV-1 Tat protein-mediated transactivation of the HIV-1 long terminal repeat promoter is potentiated by a novel nuclear Tat-interacting protein of 110 kDa, Tip110 (English)

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object named as

Betty S Pace

4

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author name string

Ying Liu

1

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Jinliang Li

2

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Byung Oh Kim

3

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Johnny J He

5

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language of work or name

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publication date

28 June 2002

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Journal of Biological Chemistry

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277

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23854-63

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26

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Taking a new TAK on tat transactivation

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HIV-1 Tat overcomes inefficient transcriptional elongation in vitro

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A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA

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HIV-1 Tat acts as a processivity factor in vitro in conjunction with cellular elongation factors

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Anti-termination of transcription within the long terminal repeat of HIV-1 by tat gene product

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The structure of the human immunodeficiency virus type-1 TAR RNA reveals principles of RNA recognition by Tat protein

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Fragments of the HIV-1 Tat protein specifically bind TAR RNA.

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Arginine-mediated RNA recognition: the arginine fork.

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A compilation of cellular transcription factor interactions with the HIV-1 LTR promoter

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The interaction between HIV-1 Tat and human cyclin T1 requires zinc and a critical cysteine residue that is not conserved in the murine CycT1 protein

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Novel substrate specificity of the histone acetyltransferase activity of HIV-1-Tat interactive protein Tip60

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A cofactor, TIP30, specifically enhances HIV-1 Tat-activated transcription

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Identification of a novel human zinc finger protein that specifically interacts with the activation domain of lentiviral Tat proteins

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CA150, a nuclear protein associated with the RNA polymerase II holoenzyme, is involved in Tat-activated human immunodeficiency virus type 1 transcription

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The HIV-1 Tat cellular coactivator Tat-SF1 is a general transcription elongation factor

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Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat

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An inducible transcription factor activates expression of human immunodeficiency virus in T cells

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Identification of a putative regulator of early T cell activation genes

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A human binding site for transcription factor USF/MLTF mimics the negative regulatory element of human immunodeficiency virus type 1.

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Uptake of HIV-1 tat protein mediated by low-density lipoprotein receptor-related protein disrupts the neuronal metabolic balance of the receptor ligands

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The Nck SH2/SH3 adaptor protein is present in the nucleus and associates with the nuclear protein SAM68

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CCR3 and CCR5 are co-receptors for HIV-1 infection of microglia

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Trans-acting transcriptional regulation of human T-cell leukemia virus type III long terminal repeat

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Isolation and characterization of a new 110 kDa human nuclear RNA-binding protein (p110nrb).

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An RNA recognition motif (RRM) is required for the localization of PTB-associated splicing factor (PSF) to subnuclear speckles

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Phosphoinositide signaling pathways in nuclei are associated with nuclear speckles containing pre-mRNA processing factors

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Dynamic relocation of transcription and splicing factors dependent upon transcriptional activity

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Tat is required for efficient HIV-1 reverse transcription

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Identifiers

10.1074/JBC.M200773200

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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