Dual phosphorylation controls Cdc25 phosphatases and mitotic entry
about
Growth factor pleiotropy is controlled by a receptor Tyr/Ser motif that acts as a binary switchThe tumor suppressor CYLD regulates entry into mitosisAurora B and 14-3-3 coordinately regulate clustering of centralspindlin during cytokinesisSpecialized roles of the two mitotic cyclins in somatic cells: cyclin A as an activator of M phase-promoting factorHeterogenic final cell cycle by chicken retinal Lim1 horizontal progenitor cells leads to heteroploid cells with a remaining replicated genomeRegulation of yeast Yak1 kinase by PKA and autophosphorylation-dependent 14-3-3 binding.Phospho-Ser/Thr-binding domains: navigating the cell cycle and DNA damage responseATM/ATR checkpoint activation downregulates CDC25C to prevent mitotic entry with uncapped telomeresKinase Inhibition Leads to Hormesis in a Dual Phosphorylation-Dephosphorylation CycleDistinct pools of cdc25C are phosphorylated on specific TP sites and differentially localized in human mitotic cellsOverexpression of CDC25B, CDC25C and phospho-CDC25C (Ser216) in vulvar squamous cell carcinomas are associated with malignant features and aggressive cancer phenotypesNPM phosphorylation stimulates Cdk1, overrides G2/M checkpoint and increases leukemic blasts in miceCo-occurring protein phosphorylation are functionally associated.Effects of the kava chalcone flavokawain A differ in bladder cancer cells with wild-type versus mutant p53.Activation of NAG-1 via JNK signaling revealed an isochaihulactone-triggered cell death in human LNCaP prostate cancer cells.Cell cycle G2/M arrest through an S phase-dependent mechanism by HIV-1 viral protein R.Changes in regulatory phosphorylation of Cdc25C Ser287 and Wee1 Ser549 during normal cell cycle progression and checkpoint arrests.Cyclin E deregulation impairs mitotic progression through premature activation of Cdc25C.Loss of CCDC6 affects cell cycle through impaired intra-S-phase checkpoint controlMitotic phosphorylation of Cdc25B Ser321 disrupts 14-3-3 binding to the high affinity Ser323 siteERK1/2 signaling plays an important role in topoisomerase II poison-induced G2/M checkpoint activation.A role for PP1 in the Cdc2/Cyclin B-mediated positive feedback activation of Cdc25.Sulforaphane induces cell cycle arrest and apoptosis in acute lymphoblastic leukemia cellsSTK295900, a dual inhibitor of topoisomerase 1 and 2, induces G(2) arrest in the absence of DNA damage.Cyclic nucleotide-dependent protein kinases inhibit binding of 14-3-3 to the GTPase-activating protein Rap1GAP2 in platelets.Inhibition of RAC1 GTPase sensitizes pancreatic cancer cells to γ-irradiation.S100A8/A9 (calprotectin) negatively regulates G2/M cell cycle progression and growth of squamous cell carcinoma.Alpinia pricei Rhizome Extracts Induce Cell Cycle Arrest in Human Squamous Carcinoma KB Cells and Suppress Tumor Growth in Nude Mice.Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes.The ATM/ATR signaling effector Chk2 is targeted by Epstein-Barr virus nuclear antigen 3C to release the G2/M cell cycle blockCell cycle-dependent Cdc25C phosphatase determines cell survival by regulating apoptosis signal-regulating kinase 1RAC1 GTPase plays an important role in γ-irradiation induced G2/M checkpoint activation.An Asymmetrically Balanced Organization of Kinases versus Phosphatases across Eukaryotes Determines Their Distinct ImpactsPotential Therapeutic Role of Z-Isochaihulactone in Lung Cancer through Induction of Apoptosis via Notch Signaling.Human 14-3-3 gamma protein results in abnormal cell proliferation in the developing eye of Drosophila melanogaster.HPV16-E2 induces prophase arrest and activates the cellular DNA damage response in vitro and in precursor lesions of cervical carcinoma.The ascidian natural product eusynstyelamide B is a novel topoisomerase II poison that induces DNA damage and growth arrest in prostate and breast cancer cellsProteomic applications of protein quantification by isotope-dilution mass spectrometry.Phosphorylation of Cdc25C at Ser216 by CHEK2Phosphatases and kinases regulating CDC25 activity in the cell cycle: clinical implications of CDC25 overexpression and potential treatment strategies
P2860
Q24302076-FD5E8B6E-66B1-42D3-AC0F-8B04CEC4F91CQ24305326-D86ACE77-F1B5-4407-AB7B-D8BE0545652FQ24310798-09383F31-16D5-4901-91DE-C419941B8435Q24681581-F48751BE-A2FB-4944-9DE4-CE42EE37143AQ27334307-558BEBCA-A5A0-4835-AD2E-D4BB5AC5C5EDQ27940266-831A6B00-399D-4A6F-BBB1-13F1141E066AQ28297156-5F9C7CFC-E4CB-4548-8368-A19B8F3F4853Q28387570-CA0F6614-2518-40CE-8409-4A6D750FE765Q28554490-844278FD-7536-4329-A7BF-4D43A5D45CA5Q30435385-A6D06F38-F4FB-4131-8D0F-172220778CCBQ33586710-74E28347-4A50-4EE8-A42F-879F2737434AQ33615300-E06BF601-69E9-49B2-A0E0-9E07EB6BDF1FQ33688357-F43423AF-60B1-47E3-8357-7F89CA7FF2C0Q33697172-E2290A81-A82E-4AFF-812D-3A70AF7C1000Q33877005-E50538EC-5A91-4C38-871A-826635CFE58DQ34016503-A6DDBCC1-548D-40AA-8F09-E51D0A3CB037Q34148207-1797F8DF-8432-4901-85DF-1A9F3BC08491Q34157822-2A8649FA-ED90-4AA2-A6C2-804CED4C25F4Q34170428-AD523116-33A0-4C57-B832-8D6B75F93663Q34251067-3BF08E36-4CCC-4C1F-9F1D-E77DED0A17C8Q34483120-0FFAEF0C-6924-4701-A7EC-1E70DD3FB58FQ34483664-D8AB38A9-0E63-4171-A263-5C10FB90F6C7Q34516308-6284AE2F-F0B0-4818-92CF-9E722F1AF00CQ34562426-F396C6BB-60C0-45E3-9185-D08E03DA29E3Q34718342-710A226F-68DE-4926-8E7F-4A40F3A51078Q34786416-F2F9A07C-83CD-4077-81C0-5724FE146B66Q34854105-FB7BD737-769A-43FB-BADA-FC0D55ADB28AQ35104779-217593C5-A849-4788-A069-8E89365B0A33Q35787179-741F8801-A7CA-427A-9976-55F1E0B6A899Q35857290-29C49EB1-18B4-4F15-B1BB-99BF8AD291F7Q36040597-58F3B7CF-87AD-4662-954F-6B8FA2559311Q36245598-CA1A7A63-9C6D-4B5F-A80F-255278F7CDB0Q36263765-67CAC5BB-C41C-4812-94CC-682087CAC40DQ36291949-D354E489-F821-47F2-BA78-77486CC9B56BQ36465139-17076E58-84AF-44A2-883C-4ADBE7B78C11Q36544275-6DC25919-71DC-48BB-B347-FE9E6FBFB3FFQ36685541-45B82B15-89D1-4C16-AF79-42510CAF7AE9Q36689092-171E6739-EA17-4082-B9B9-2F99042FFC20Q36811974-534605E5-D193-42E8-9574-0C88A4FE113BQ36889310-F440EA37-6476-40B0-8CBF-74D3720561A5
P2860
Dual phosphorylation controls Cdc25 phosphatases and mitotic entry
description
2003 nî lūn-bûn
@nan
2003 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
name
Dual phosphorylation controls Cdc25 phosphatases and mitotic entry
@ast
Dual phosphorylation controls Cdc25 phosphatases and mitotic entry
@en
Dual phosphorylation controls Cdc25 phosphatases and mitotic entry
@en-gb
Dual phosphorylation controls Cdc25 phosphatases and mitotic entry
@nl
type
label
Dual phosphorylation controls Cdc25 phosphatases and mitotic entry
@ast
Dual phosphorylation controls Cdc25 phosphatases and mitotic entry
@en
Dual phosphorylation controls Cdc25 phosphatases and mitotic entry
@en-gb
Dual phosphorylation controls Cdc25 phosphatases and mitotic entry
@nl
prefLabel
Dual phosphorylation controls Cdc25 phosphatases and mitotic entry
@ast
Dual phosphorylation controls Cdc25 phosphatases and mitotic entry
@en
Dual phosphorylation controls Cdc25 phosphatases and mitotic entry
@en-gb
Dual phosphorylation controls Cdc25 phosphatases and mitotic entry
@nl
P2093
P2860
P50
P3181
P356
P1433
P1476
Dual phosphorylation controls Cdc25 phosphatases and mitotic entry
@en
P2093
Crissy Phillips
Dmitry V Bulavin
Helen Piwnica-Worms
Paul Graves
Sarah Meek
Zoya N Demidenko
P2860
P2888
P304
P3181
P356
10.1038/NCB994
P407
P577
2003-06-01T00:00:00Z
P5875
P6179
1045135417