Substrate binding on the APC/C occurs between the coactivator Cdh1 and the processivity factor Doc1. - Test2 - elhamkhani - TriplyDB

Substrate binding on the APC/C occurs between the coactivator Cdh1 and the processivity factor Doc1.

Substrate binding on the APC/C occurs between the coactivator Cdh1 and the processivity factor Doc1.

http://www.wikidata.org/entity/Q41792135

about

Mechanisms controlling the temporal degradation of Nek2A and Kif18A by the APC/C-Cdc20 complex Functional characterization of Anaphase Promoting Complex/Cyclosome (APC/C) E3 ubiquitin ligases in tumorigenesis The Renaissance or the cuckoo clock Structure of a Glomulin-RBX1-CUL1 Complex: Inhibition of a RING E3 Ligase through Masking of Its E2-Binding Surface Structural analysis of human Cdc20 supports multisite degron recognition by APC/C Electron microscopy structure of human APC/CCDH1–EMI1 reveals multimodal mechanism of E3 ligase shutdown The APC/C subunit Mnd2/Apc15 promotes Cdc20 autoubiquitination and spindle assembly checkpoint inactivation.Spatiotemporal regulation of the anaphase-promoting complex in mitosis Experimental validation of Ankrd17 and Anapc10, two novel meiotic genes predicted by computational models in mice Microtubule-dependent regulation of mitotic protein degradation.Synergistic blockade of mitotic exit by two chemical inhibitors of the APC/C.Molecular architecture and mechanism of the anaphase-promoting complex Activation of the APC/C ubiquitin ligase by enhanced E2 efficiency SNW1 enables sister chromatid cohesion by mediating the splicing of sororin and APC2 pre-mRNAs.The Cdc20-binding Phe box of the spindle checkpoint protein BubR1 maintains the mitotic checkpoint complex during mitosis.The biochemistry of mitosis RING E3 mechanism for ubiquitin ligation to a disordered substrate visualized for human anaphase-promoting complex Mutual regulation between the spindle checkpoint and APC/C.An APC/C inhibitor stabilizes cyclin B1 by prematurely terminating ubiquitination Regulation of E2F1 by APC/C Cdh1 via K11 linkage-specific ubiquitin chain formation.Dephosphorylation of Cdc20 is required for its C-box-dependent activation of the APC/C Mad2 and the APC/C compete for the same site on Cdc20 to ensure proper chromosome segregation Control of APC/C-dependent ubiquitin chain elongation by reversible phosphorylation State of the APC/C: organization, function, and structure.Mechanism of APC/CCDC20 activation by mitotic phosphorylation.Mutually dependent degradation of Ama1p and Cdc20p terminates APC/C ubiquitin ligase activity at the completion of meiotic development in yeast.Substrate Recognition by the Cdh1 Destruction Box Receptor Is a General Requirement for APC/CCdh1-mediated Proteolysis Processive ubiquitin chain formation by the anaphase-promoting complex.Structural insights into anaphase-promoting complex function and mechanism.Panta rhei: the APC/C at steady state.Flipping the switch from g1 to s phase with e3 ubiquitin ligases Control the host cell cycle: viral regulation of the anaphase-promoting complex.Assays to Monitor Autophagy in Saccharomyces cerevisiae The Bub1-Plk1 kinase complex promotes spindle checkpoint signalling through Cdc20 phosphorylation.Building a Regulatory Network with Short Linear Sequence Motifs: Lessons from the Degrons of the Anaphase-Promoting Complex.Recombinant expression, reconstitution and structure of human anaphase-promoting complex (APC/C).Cdc20 control of cell fate during prolonged mitotic arrest: do Cdc20 protein levels affect cell fate in response to antimitotic compounds?BubR1 blocks substrate recruitment to the APC/C in a KEN-box-dependent manner.Structure of an APC3-APC16 complex: insights into assembly of the anaphase-promoting complex/cyclosome.The mitotic checkpoint complex (MCC): looking back and forth after 15 years.

P2860

1729dbbde198053c7fe65546e667f1924b9cb18f 808943147e4c924b37bd65e472e9d4ad4e65937d 8ddfa1a91abf66b17755a3b3694085021943bd56 a32ba23d5dcac69b379b8e934bda4398248676d3 a64aac12a9746bf01fc95b15ba98d31759e35704 c2c7d85ad91f7047318f5e18b6514d8228f019ec d67348d99fc8bd1ca30e8e537e23954bde4edfc5 f97cf23a87aa064cb3d3da0e09515ae815194c36

P248

Q24307635-B9470AE4-95D1-4391-A299-2EA4B29A3BE3 Q26998944-324FCB5F-6C42-43A4-9E9F-B943D92C67D9 Q27000712-B9C62ED3-E979-4C30-9612-83F3226F5F32 Q27670574-C0050A75-AD56-407C-83A9-E07FBB32D1EF Q27674687-91FE120B-1E07-4978-89B9-4292DBDAA2A4 Q27678304-3C548A48-3DE6-40B7-9D36-29EC710929CC Q27932569-FD01E28D-3100-43F8-881A-4228C9D8A2AE Q28081253-943DDFC0-0D3B-4641-B7EA-5A588791C8C9 Q28512932-3E738550-6ADF-4FDB-B35E-E9D65EAD1B68 Q30572037-A7AB9A20-9B73-4542-BC46-7EC9953F712C Q30596621-BE1C01EC-6B4D-49B7-9A2B-4060C2DB06F1 Q30653286-C015056F-0045-4EF7-A91C-563B67A674E8 Q33875519-FE5DF1F7-80ED-456B-A108-8604F5C0D424 Q34806974-85ADF116-39DF-44CC-9340-987664AB406F Q35003017-74E51CB8-248F-41F1-A45C-E353A63E9711 Q35164326-A8705109-444C-41BE-9B50-B47A053B27E9 Q35567086-10D66853-B68F-4609-B038-303CD33F4CBF Q35576429-029E9566-DED7-4391-BA8B-E8C05F38AC7E Q35840276-53DA3CA0-8C7E-4609-9474-5434552201BA Q35984095-57E30FA1-CDE5-4AB3-B404-D2B56F094528 Q36137572-B79C3CFE-65E1-4314-A99E-204CEE078761 Q36289100-738E6072-BC51-4D3C-89C0-44245DE8B4A7 Q36598924-043D6476-481E-41D6-9931-3D7DCECBA121 Q36867692-A79DD1E2-51E0-491E-B813-7549AA520199 Q36905102-84C14F15-9466-49A5-ABB2-5618831C2F04 Q37071780-91722627-A195-4254-AE37-3D24F31B625D Q37117276-EA4919B4-9FA5-4CCC-AA18-FD16E2E25CEF Q37863285-A5972454-9912-4C21-B490-D9D7BD6A78E1 Q37956288-EE9786B5-4755-4F92-AD00-54F2374FFA83 Q38099298-30E55754-AA71-4ABC-94D1-18249431C2F9 Q38103251-1CE92285-A16B-4CB8-B32C-0ECA6D66886E Q38113943-84DC10AE-0CD7-4EE1-A473-A114EE1D6D79 Q38681200-45C8A0AE-D922-402E-BF23-4D0D927F8C55 Q38707137-9B7E45CD-EA1D-47FB-AAD1-945272F81EEF Q38975034-B3935AD6-36A1-46DD-B45C-4F5F6D39670A Q39256977-6A00D049-3296-48FF-804B-010A222947FE Q39449351-A3B2F5F8-084A-44DB-9080-44FD117E16B7 Q40394371-334D3CD9-5873-4E81-9580-E63F9E507BEE Q41100050-DDEF661C-827C-46DC-94FF-D11B30AFD224 Q41146841-C28200A4-BE54-4815-BBCD-5B899CB64555

P2860

Substrate binding on the APC/C occurs between the coactivator Cdh1 and the processivity factor Doc1.

http://www.wikidata.org/entity/Q41792135

description

2010 nî lūn-bûn

@nan

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

2010年论文

@zh

2010年论文

@zh-cn

name

Substrate binding on the APC/C ...... the processivity factor Doc1.

@en

type

label

Substrate binding on the APC/C ...... the processivity factor Doc1.

@en

prefLabel

Substrate binding on the APC/C ...... the processivity factor Doc1.

@en

P1433

Q41792135-06D03340-69E8-4A58-B702-9220BDFB083D

P1476

Q41792135-DEF37E46-26A4-4C0A-A8DE-4EB23ADFBB41

P2093

Q41792135-01D2C82F-27A8-441D-911E-00B307613360

Q41792135-44FF5B99-B747-43F8-8E68-DADAA406425A

Q41792135-8CDD51E6-D0D4-41F9-9A64-5A88204219A8

Q41792135-B30DCF14-DBC0-4584-99DE-25235354BDA4

Q41792135-B3254EB6-4D54-4283-A55B-10AB3E01FB35

Q41792135-D4DAADF1-C8BD-4A30-96F1-C36CE36C7330

P2860

Q41792135-0B5BE58C-7037-4849-AF20-94AF4508308E

Q41792135-12F6E0B0-52A8-4811-B858-16289B955915

Q41792135-16B74D45-0325-49CA-8521-14EECE076914

Q41792135-1AA26A10-0ECB-46A3-A6B9-CF7443E515D3

Q41792135-22A613BA-128C-4998-830A-DC283734A870

Q41792135-27D7D485-13C8-4C8E-B40B-A90E023E5D73

Q41792135-2FF5DFF0-B129-4E1C-810C-949C3CE0D6D6

Q41792135-3079E679-93A9-4CF8-9F0D-1CEF2EBE2924

Q41792135-30EA323B-5A33-4A71-AA42-DAA4BC5FB828

Q41792135-32CE642A-7127-4BBA-99AC-9D9D5794FD92

P2888

Q41792135-7C6FD249-1286-406B-8054-139708D8A79E

P304

Q41792135-C4C4C81A-9536-428F-81B3-CD40A5A661D7

P31

Q41792135-EEB45791-4DB3-43E7-83CF-1FC18D94E093

P356

Q41792135-BFB81126-FE7C-424A-803F-2C5985C20172

P433

Q41792135-E9C6A3CD-869E-441B-B2D3-D14B2152DBBC

P478

Q41792135-5432E1C3-CA73-49AD-99A3-15AA100FD758

P50

Q41792135-6D92D472-F758-4548-BF64-419508CA54DA

Q41792135-AC6B2C0D-5911-4264-A953-047E28885070

P577

Q41792135-A2E4EE6F-0864-4101-9B08-A0DAD53BD68E

P5875

Q41792135-0839FFD8-ACCA-41AD-BFAE-1E69B83F18B4

P698

Q41792135-09EE09AB-CB38-4329-9549-8D82DACB0B1E

P932

Q41792135-C1B04C8D-C9DC-402C-84BA-146B3364D46E

P356

P1433

Nature Structural & Molecular Biology

P1476

Substrate binding on the APC/C ...... d the processivity factor Doc1

@en

P2093

Bettina A Buschhorn

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

Franz Herzog

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

Holger Stark

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

Jan-Michael Peters

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

Marta Galova

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

Prakash Dube

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

P2860

Characterization of the DOC1/APC10 subunit of the yeast and the human anaphase-promoting complex

Localization of the coactivator Cdh1 and the cullin subunit Apc2 in a cryo-electron microscopy model of vertebrate APC/C

An architectural map of the anaphase-promoting complex

Crystal structure of the APC10/DOC1 subunit of the human anaphase-promoting complex

Implications for the ubiquitination reaction of the anaphase-promoting complex from the crystal structure of the Doc1/Apc10 subunit

Insights into anaphase promoting complex TPR subdomain assembly from a CDC26–APC6 structure

Molecular structure of the N-terminal domain of the APC/C subunit Cdc27 reveals a homo-dimeric tetratricopeptide repeat architecture

The spindle-assembly checkpoint in space and time

Doc1 mediates the activity of the anaphase-promoting complex by contributing to substrate recognition.

Identification of subunits of the anaphase-promoting complex of Saccharomyces cerevisiae.

P2888

P304

6-13

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

P31

scholarly article

P356

10.1038/NSMB.1979

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

P433

1

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

P478

18

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

P50

P577

2010-12-26T00:00:00Z

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

P5875

49709925

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

P698

21186364

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

P932

4300845

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