An overlapping kinase and phosphatase docking site regulates activity of the retinoblastoma protein - Test2 - elhamkhani - TriplyDB

An overlapping kinase and phosphatase docking site regulates activity of the retinoblastoma protein

An overlapping kinase and phosphatase docking site regulates activity of the retinoblastoma protein

http://www.wikidata.org/entity/Q27663961

about

The retinoblastoma family of proteins and their regulatory functions in the mammalian cell division cycle Motif co-regulation and co-operativity are common mechanisms in transcriptional, post-transcriptional and post-translational regulation PP2A: more than a reset switch to activate pRB proteins during the cell cycle and in response to signaling cues.Short linear motifs - ex nihilo evolution of protein regulation PP1 and PP2A phosphatases--cooperating partners in modulating retinoblastoma protein activation Molecular mechanisms underlying RB protein function Understanding the antagonism of retinoblastoma protein dephosphorylation by PNUTS provides insights into the PP1 regulatory code Ssu72 phosphatase-dependent erasure of phospho-Ser7 marks on the RNA polymerase II C-terminal domain is essential for viability and transcription termination.Getting to S: CDK functions and targets on the path to cell-cycle commitment The human SKA complex drives the metaphase-anaphase cell cycle transition by recruiting protein phosphatase 1 to kinetochores RSS1 regulates the cell cycle and maintains meristematic activity under stress conditions in rice.Targeting tumor suppressor networks for cancer therapeutics.The calcineurin signaling network evolves via conserved kinase-phosphatase modules that transcend substrate identity Integrating phosphoproteomics in systems biology.Cryptochrome 1 regulates the circadian clock through dynamic interactions with the BMAL1 C terminus.The Discovery of Novel 10,11-Dihydro-5H-dibenz[b,f]azepine SIRT2 Inhibitors.Structural basis for protein phosphatase 1 regulation and specificity Retinoblastoma tumor-suppressor protein phosphorylation and inactivation depend on direct interaction with Pin1.Calcium-calmodulin kinase I cooperatively regulates nucleocytoplasmic shuttling of CCTα by accessing a nuclear export signal.Substrate Affinity Differentially Influences Protein Kinase C Regulation and Inhibitor Potency.Activation of p107 by fibroblast growth factor, which is essential for chondrocyte cell cycle exit, is mediated by the protein phosphatase 2A/B55α holoenzyme.Molecular Insights into the Fungus-Specific Serine/Threonine Protein Phosphatase Z1 in Candida albicans Conserved RB functions in development and tumor suppression.Diversity within the pRb pathway: is there a code of conduct?Understanding the targeting of the RB family proteins by viral oncoproteins to defeat their oncogenic machinery.Deciphering the retinoblastoma protein phosphorylation code.PP2A as a master regulator of the cell cycle.Cyclin-specific docking motifs promote phosphorylation of yeast signaling proteins by G1/S Cdk complexes.Revisiting protein kinase-substrate interactions: Toward therapeutic development.The B55α regulatory subunit of protein phosphatase 2A mediates fibroblast growth factor-induced p107 dephosphorylation and growth arrest in chondrocytes.The role of the NORE1A tumor suppressor in Oncogene-Induced Senescence.The crucial role of protein phosphorylation in cell signaling and its use as targeted therapy (Review).Analysis of cell cycle position in mammalian cells.Structural Conservation and E2F Binding Specificity within the Retinoblastoma Pocket Protein Family Multisite phosphorylation networks as signal processors for Cdk1.A "fuzzy"-logic language for encoding multiple physical traits in biomolecules.Structural basis of divergent cyclin-dependent kinase activation by Spy1/RINGO proteins.Response to DNA damage: why do we need to focus on protein phosphatases?Theoretical studies on the reaction mechanism of PP1 and the effects of different oxidation states of the Mn-Mn center on the mechanism.Distinct Cell-Cycle Control in Two Different States of Mouse Pluripotency.

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P2860

An overlapping kinase and phosphatase docking site regulates activity of the retinoblastoma protein

http://www.wikidata.org/entity/Q27663961

description

2010 nî lūn-bûn

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2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

An overlapping kinase and phos ...... of the retinoblastoma protein

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An overlapping kinase and phos ...... of the retinoblastoma protein

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An overlapping kinase and phos ...... of the retinoblastoma protein

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type

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An overlapping kinase and phos ...... of the retinoblastoma protein

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An overlapping kinase and phos ...... of the retinoblastoma protein

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An overlapping kinase and phos ...... of the retinoblastoma protein

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An overlapping kinase and phos ...... of the retinoblastoma protein

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An overlapping kinase and phos ...... of the retinoblastoma protein

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An overlapping kinase and phos ...... of the retinoblastoma protein

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Nature Structural & Molecular Biology

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An overlapping kinase and phos ...... of the retinoblastoma protein

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P2093

Alexander Hirschi

http://www.w3.org/2001/XMLSchema#string

Frederick A Dick

http://www.w3.org/2001/XMLSchema#string

Matthew Cecchini

http://www.w3.org/2001/XMLSchema#string

Michael R Schamber

http://www.w3.org/2001/XMLSchema#string

Rachel C Steinhardt

http://www.w3.org/2001/XMLSchema#string

Seth M Rubin

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P2860

Direct interaction between the catalytic subunit of Protein Phosphatase 1 and pRb.

Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism for phosphorylation-induced E2F release

A C-terminal protein-binding domain in the retinoblastoma protein regulates nuclear c-Abl tyrosine kinase in the cell cycle

Interaction between the retinoblastoma protein and the oncoprotein MDM2

Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1

An amplified sensitivity arising from covalent modification in biological systems

Specificity determinants of recruitment peptides bound to phospho-CDK2/cyclin A

Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1

The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit

The retinoblastoma protein and cell cycle control

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1051-7

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scholarly article

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3333645

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10.1038/NSMB.1868

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9

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17

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2010-09-01T00:00:00Z

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45538616

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1007081028

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20694007

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structural biology

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2933323

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