The structure of P-TEFb (CDK9/cyclin T1), its complex with flavopiridol and regulation by phosphorylation
about
Dual function of histone H3 lysine 36 methyltransferase ASH1 in regulation of Hox gene expressionAnalysis of substrate specificity and cyclin Y binding of PCTAIRE-1 kinaseInteraction of cyclin-dependent kinase 12/CrkRS with cyclin K1 is required for the phosphorylation of the C-terminal domain of RNA polymerase IICrystal structure of HIV-1 Tat complexed with human P-TEFbCrystal structure of human CDK4 in complex with a D-type cyclinThe structure of CDK4/cyclin D3 has implications for models of CDK activationStructures of the Dual Bromodomains of the P-TEFb-activating Protein Brd4 at Atomic ResolutionCDK Inhibitors Roscovitine and CR8 Trigger Mcl-1 Down-Regulation and Apoptotic Cell Death in Neuroblastoma CellsThe CDK9 Tail Determines the Reaction Pathway of Positive Transcription Elongation Factor bComparative Structural and Functional Studies of 4-(Thiazol-5-yl)-2-(phenylamino)pyrimidine-5-carbonitrile CDK9 Inhibitors Suggest the Basis for Isotype SelectivitySubstituted 4-(Thiazol-5-yl)-2-(phenylamino)pyrimidines Are Highly Active CDK9 Inhibitors: Synthesis, X-ray Crystal Structures, Structure–Activity Relationship, and Anticancer ActivitiesThe AFF4 scaffold binds human P-TEFb adjacent to HIV TatThe CDK9 C-helix Exhibits Conformational Plasticity That May Explain the Selectivity of CAN508The structure and substrate specificity of human Cdk12/Cyclin KCrystal structure of HIV-1 Tat complexed with human P-TEFb and AFF4AFF4 binding to Tat-P-TEFb indirectly stimulates TAR recognition of super elongation complexes at the HIV promoterMolecular mechanism of Aurora A kinase autophosphorylation and its allosteric activation by TPX2Phosphorylation of CDK9 at Ser175 enhances HIV transcription and is a marker of activated P-TEFb in CD4(+) T lymphocytesFlavonoids as CDK1 Inhibitors: Insights in Their Binding Orientations and Structure-Activity RelationshipThe case for open-access chemical biology. A strategy for pre-competitive medicinal chemistry to promote drug discoveryVisualizing the Ensemble Structures of Protein Complexes Using Chemical Cross-Linking Coupled with Mass Spectrometry8-Amino-adenosine inhibits multiple mechanisms of transcription.Caffeine prevents transcription inhibition and P-TEFb/7SK dissociation following UV-induced DNA damage.Antisense-mediated FLC transcriptional repression requires the P-TEFb transcription elongation factor.SEL120-34A is a novel CDK8 inhibitor active in AML cells with high levels of serine phosphorylation of STAT1 and STAT5 transactivation domainsAn inhibitor's-eye view of the ATP-binding site of CDKs in different regulatory states.Mechanism and factors that control HIV-1 transcription and latency activationProtein phosphatase-1 activates CDK9 by dephosphorylating Ser175.Modifications in host cell cytoskeleton structure and function mediated by intracellular HIV-1 Tat protein are greatly dependent on the second coding exonT-loop phosphorylated Cdk9 localizes to nuclear speckle domains which may serve as sites of active P-TEFb function and exchange between the Brd4 and 7SK/HEXIM1 regulatory complexes.Antitumor activity of a novel oncrasin analogue is mediated by JNK activation and STAT3 inhibitionThe impact of CDK inhibition in human malignancies associated with pronounced defects in apoptosis: advantages of multi-targeting small molecules.The RNA polymerase II CTD coordinates transcription and RNA processing.HEXIM1 targets a repeated GAUC motif in the riboregulator of transcription 7SK and promotes base pair rearrangementsA Cyclin T1 point mutation that abolishes positive transcription elongation factor (P-TEFb) binding to Hexim1 and HIV tatEffect of mimetic CDK9 inhibitors on HIV-1-activated transcription.A role for CDK9-cyclin K in maintaining genome integrityAnalogues and derivatives of oncrasin-1, a novel inhibitor of the C-terminal domain of RNA polymerase II and their antitumor activities.G-actin participates in RNA polymerase II-dependent transcription elongation by recruiting positive transcription elongation factor b (P-TEFb).Polo-like kinase 1 inhibits the activity of positive transcription elongation factor of RNA Pol II b (P-TEFb).
P2860
Q21134949-F854FABA-7814-4F7E-BA00-F5876E83A3B0Q24293247-6B3F27C3-F776-400C-AEE1-72BCF9F87B3AQ24299038-A4326739-DE20-427B-B910-68AAB6362E20Q24634569-B5C242C2-7413-43A2-908A-8058321AD012Q24656160-F1296187-D3B9-4F06-A8A9-4E1A2C04E49BQ27653913-1225B054-29B1-4D7C-AC5D-DEE3A159A37EQ27657784-4D74E787-7526-4A0E-BA74-35B4335D05DBQ27670943-9E5A6A3A-058E-4FC5-91A7-EEBA07BC5401Q27672752-405B0C5D-477F-4CF5-A0B7-4518D190B5AAQ27675539-04794E49-1DFB-4C5A-91F0-4873DCAF13DAQ27675842-622B1194-D251-49A8-8907-FB1BEB760839Q27676733-F2C8F59A-F4BD-40D5-A22E-E36F0C9A6805Q27676963-C2CD7225-D9C9-475B-9E9A-EFA305299106Q27682428-38D0AB41-C1D9-46FD-A815-E1CC2EE67B01Q27683254-77322C70-386C-49C9-BC1B-5A5E54D31FE9Q27683845-F7B3BD52-8DFF-4274-A0C9-157874D3D3E2Q27683971-21390A77-30A5-42A2-B13D-BA8E5D2F9289Q28487524-C2EFDD81-B867-412E-B283-B1A994878C57Q28553502-3775B076-611C-4F40-8C24-69A0625AFD30Q28751328-489ED2BC-0029-45CB-99BE-0E5978838994Q28833842-2F9B019B-BB65-4361-9D80-2E0EDC3ACC50Q33590629-48A376AB-1D78-454F-9FF3-829D265186D9Q33614701-00556304-B3DE-413E-8CBA-64EF437E34F3Q33665562-EFF42FDC-4C18-4007-89F3-D61C0840459CQ33779684-E256ABA6-B6AB-4B3C-90DE-AC2DEE671EE9Q33797218-86FEE81F-2D83-4C29-AAC9-A31175AFF884Q33826920-87BA2735-4CC4-4875-A108-CE4F752145FAQ33886004-B98ECC6B-EE02-460D-9B0B-CE81CC220037Q33889326-048D2D7D-C985-4C81-98BC-A0A08F7B5A44Q33922921-B5C250BA-F490-493B-8C62-FA1102E07454Q34103117-5E051AA3-3984-4EE4-A0DF-54D9E7362DD0Q34195072-B445E456-89EA-4AAE-B0A3-92829895A12EQ34303212-86AD1BDA-07CF-4FEA-B722-7E6C768E1C6EQ34368113-A18C9555-E5CB-4DEF-B1B6-5DC14E4E6C82Q34486331-33861566-D6A8-470B-A266-1C3907D9544EQ34514689-6D68D3B6-0634-4E00-B1D7-7320CF45C539Q34621011-FEAA1B4C-6B14-4935-A9BF-2C05F061404AQ34857289-2C0CB451-0F66-40B2-8D0B-C52C5B652FB1Q34869767-FBDBE5EC-D6CF-4880-85F4-62E4FB4C2D4DQ34973763-4833EB9D-087B-4B6C-B279-0A2F366A3B31
P2860
The structure of P-TEFb (CDK9/cyclin T1), its complex with flavopiridol and regulation by phosphorylation
description
2008 nî lūn-bûn
@nan
2008 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
The structure of P-TEFb (CDK9/ ...... regulation by phosphorylation
@ast
The structure of P-TEFb (CDK9/ ...... regulation by phosphorylation
@en
The structure of P-TEFb (CDK9/ ...... regulation by phosphorylation
@en-gb
The structure of P-TEFb (CDK9/ ...... regulation by phosphorylation
@nl
type
label
The structure of P-TEFb (CDK9/ ...... regulation by phosphorylation
@ast
The structure of P-TEFb (CDK9/ ...... regulation by phosphorylation
@en
The structure of P-TEFb (CDK9/ ...... regulation by phosphorylation
@en-gb
The structure of P-TEFb (CDK9/ ...... regulation by phosphorylation
@nl
prefLabel
The structure of P-TEFb (CDK9/ ...... regulation by phosphorylation
@ast
The structure of P-TEFb (CDK9/ ...... regulation by phosphorylation
@en
The structure of P-TEFb (CDK9/ ...... regulation by phosphorylation
@en-gb
The structure of P-TEFb (CDK9/ ...... regulation by phosphorylation
@nl
P2093
P2860
P3181
P356
P1433
P1476
The structure of P-TEFb (CDK9/ ...... regulation by phosphorylation
@en
P2093
Alex N Bullock
Edward D Lowe
Judit E Debreczeni
Louise N Johnson
Luisa Rusconi
Sonia Troiani
Sonja Baumli
P2860
P304
P3181
P356
10.1038/EMBOJ.2008.121
P407
P577
2008-07-09T00:00:00Z