Evidence for conformational flexibility in the Tat-TAR recognition motif of cyclin T1. (Q42831352)

8 November 2017

Evidence for conformational flexibility in the Tat-TAR recognition motif of cyclin T1. (English)

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8 November 2017

Chandreyee Das

1

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8 November 2017

Stephen P Edgcomb

2

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8 November 2017

Ralph Peteranderl

3

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8 November 2017

Lily Chen

4

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8 November 2017

Alan D Frankel

5

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8 November 2017

language of work or name

English

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publication date

1 January 2004

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8 November 2017

12

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inferred from page(s)

published in

Virology

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8 November 2017

318

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8 November 2017

1

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8 November 2017

306-317

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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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Canine cyclin T1 rescues equine infectious anemia virus tat trans-activation in human cells

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The crystal structure of human cyclin H

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The structure of cyclin H: common mode of kinase activation and specific features

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Binding of Tat to TAR and recruitment of positive transcription elongation factor b occur independently in bovine immunodeficiency virus

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Recruitment of a protein complex containing Tat and cyclin T1 to TAR governs the species specificity of HIV-1 Tat.

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Functional differences between human and bovine immunodeficiency virus Tat transcription factors

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The crystal structure of cyclin A

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Arginine-mediated RNA recognition: the arginine fork.

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Crystal structure of a gamma-herpesvirus cyclin-cdk complex

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An RNA-binding peptide from bovine immunodeficiency virus Tat protein recognizes an unusual RNA structure

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A peptide interaction in the major groove of RNA resembles protein interactions in the minor groove of DNA.

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Determination of the helix and beta form of proteins in aqueous solution by circular dichroism.

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Specific interaction of Tat with the human but not rodent P-TEFb complex mediates the species-specific Tat activation of HIV-1 transcription

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HIV-1 tat trans-activation requires the loop sequence within tar.

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Fitting peptides into the RNA world

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Cellular uptake of the tat protein from human immunodeficiency virus

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Induced folding in RNA-protein recognition: more than a simple molecular handshake

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Tat protein from human immunodeficiency virus forms a metal-linked dimer

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Interactions between human cyclin T, Tat, and the transactivation response element (TAR) are disrupted by a cysteine to tyrosine substitution found in mouse cyclin T

7 January 2021

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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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CDK9 autophosphorylation regulates high-affinity binding of the human immunodeficiency virus type 1 tat-P-TEFb complex to TAR RNA

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Evidence for a protein domain superfamily shared by the cyclins, TFIIB and RB/p107.

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Visualizing tertiary folding of RNA and RNA-protein interactions by a tethered iron chelate: analysis ofHIV-1 Tat-TAR complex

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Cyclin T1 domains involved in complex formation with Tat and TAR RNA are critical for tat-activation

7 January 2021

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Taking a new TAK on tat transactivation

7 January 2021

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7 January 2021

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Three-dimensional structure of human cyclin H, a positive regulator of the CDK-activating kinase

7 January 2021

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Identification of the domains in cyclin A required for binding to, and activation of, p34cdc2 and p32cdk2 protein kinase subunits

7 January 2021

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A minimal chimera of human cyclin T1 and tat binds TAR and activates human immunodeficiency virus transcription in murine cells.

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MOLMOL: a program for display and analysis of macromolecular structures

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Role of the human and murine cyclin T proteins in regulating HIV-1 tat-activation

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Current topics in RNA-protein recognition: control of specificity and biological function through induced fit and conformational capture

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Characterization of the solution conformations of unbound and Tat peptide-bound forms of HIV-1 TAR RNA

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Transcriptional regulation by targeted recruitment of cyclin-dependent CDK9 kinase in vivo

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Ubiquitous expression of goat cyclin T1 in transgenic mice

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Transcriptional activity of positive transcription elongation factor b kinase in vivo requires the C-terminal domain of RNA polymerase II.

7 January 2021

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7SK small nuclear RNA binds to and inhibits the activity of CDK9/cyclin T complexes

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The cyclin box fold: protein recognition in cell-cycle and transcription control

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P-TEFb, a cyclin-dependent kinase controlling elongation by RNA polymerase II

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Conformation of the TAR RNA-Arginine Complex by NMR Spectroscopy

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Solution structure of a bovine immunodeficiency virus Tat-TAR peptide-RNA complex

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Specific HIV-1 TAR RNA loop sequence and functional groups are required for human cyclin T1-Tat-TAR ternary complex formation

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TAR RNA loop: a scaffold for the assembly of a regulatory switch in HIV replication

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A bulge structure in HIV-1 TAR RNA is required for Tat binding and Tat-mediated trans-activation

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Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex

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Crystal structure of a viral cyclin, a positive regulator of cyclin-dependent kinase 6

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

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Interactions between equine cyclin T1, Tat, and TAR are disrupted by a leucine-to-valine substitution found in human cyclin T1.

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RNA recognition by Tat-derived peptides: interaction in the major groove?

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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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Proteins that bind RNA and the labs who love them

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The 7SK small nuclear RNA inhibits the CDK9/cyclin T1 kinase to control transcription

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Molecular recognition in the bovine immunodeficiency virus Tat peptide-TAR RNA complex

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Transcription elongation factor P-TEFb mediates Tat activation of HIV-1 transcription at multiple stages

7 January 2021

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Mutational analysis of the conserved cysteine-rich region of the human immunodeficiency virus type 1 Tat protein

7 January 2021

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inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1016/J.VIROL.2003.10.003

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8 November 2017

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