Self-regulated Plk1 recruitment to kinetochores by the Plk1-PBIP1 interaction is critical for proper chromosome segregation. - Wikidata - awgldk - TriplyDB

Self-regulated Plk1 recruitment to kinetochores by the Plk1-PBIP1 interaction is critical for proper chromosome segregation.

Self-regulated Plk1 recruitment to kinetochores by the Plk1-PBIP1 interaction is critical for proper chromosome segregation.

http://www.wikidata.org/entity/Q34578828

about

Self-regulated mechanism of Plk1 localization to kinetochores: lessons from the Plk1-PBIP1 interaction Polo-like kinase is required for synaptonemal complex disassembly and phosphorylation in mouse spermatocytes Polo-like kinase 2-dependent phosphorylation of NPM/B23 on serine 4 triggers centriole duplication Tex14, a Plk1-regulated protein, is required for kinetochore-microtubule attachment and regulation of the spindle assembly checkpoint The decision to enter mitosis: feedback and redundancy in the mitotic entry network Identification of a novel Wnt5a-CK1ɛ-Dvl2-Plk1-mediated primary cilia disassembly pathway Maintaining Genome Stability in Defiance of Mitotic DNA Damage PLK-1 Targeted Inhibitors and Their Potential against Tumorigenesis Putting a bit into the polo-box domain of polo-like kinase 1 Polo-like kinase 1, on the rise from cell cycle regulation to prostate cancer development Molecular dynamics of PLK1 during mitosis Expression of constitutively active CDK1 stabilizes APC-Cdh1 substrates and potentiates premature spindle assembly and checkpoint function in G1 cells Kinetochore function is controlled by a phospho-dependent coexpansion of inner and outer components.Usp16 regulates kinetochore localization of Plk1 to promote proper chromosome alignment in mitosis.Cep169, a Novel Microtubule Plus-End-Tracking Centrosomal Protein, Binds to CDK5RAP2 and Regulates Microtubule Stability Multiple requirements of PLK1 during mouse oocyte maturation Group IVA Cytosolic Phospholipase A2 Regulates the G2-to-M Transition by Modulating the Activity of Tumor Suppressor SIRT2.Structural and functional analyses of minimal phosphopeptides targeting the polo-box domain of polo-like kinase 1 From Crystal Packing to Molecular Recognition: Prediction and Discovery of a Binding Site on the Surface of Polo-Like Kinase 1 Serendipitous alkylation of a Plk1 ligand uncovers a new binding channel Identification of High Affinity Polo-like Kinase 1 (Plk1) Polo-box Domain Binding Peptides Using Oxime-Based Diversification Exploring the Binding Nature of Pyrrolidine Pocket-Dependent Interactions in the Polo-Box Domain of Polo-Like Kinase 1 Structural basis for the inhibition of Polo-like kinase 1 Polo-like kinase and its inhibitors: Ready for the match to start?Chromosome congression is promoted by CENP-Q- and CENP-E-dependent pathways.Dynactin helps target Polo-like kinase 1 to kinetochores via its left-handed beta-helical p27 subunit Bod1 regulates protein phosphatase 2A at mitotic kinetochores Dbf4 regulates the Cdc5 Polo-like kinase through a distinct non-canonical binding interaction The chromosomal passenger complex activates Polo kinase at centromeres Investigation of tissue-specific expression and functions of MLF1-IP during development and in the immune system Design and synthesis of a cell-permeable, drug-like small molecule inhibitor targeting the polo-box domain of polo-like kinase 1 Meikin is a conserved regulator of meiosis-I-specific kinetochore function Decoding Polo-like kinase 1 signaling along the kinetochore-centromere axis Neighbor-directed histidine N (τ)-alkylation: A route to imidazolium-containing phosphopeptide macrocycles Connecting the microtubule attachment status of each kinetochore to cell cycle arrest through the spindle assembly checkpoint.Use of the novel Plk1 inhibitor ZK-thiazolidinone to elucidate functions of Plk1 in early and late stages of mitosis.Plk1 phosphorylates Sgt1 at the kinetochores to promote timely kinetochore-microtubule attachment.Deficiency in chromosome congression by the inhibition of Plk1 polo box domain-dependent recognition.Mechanisms underlying Plk1 polo-box domain-mediated biological processes and their physiological significance.The transforming parasite Theileria co-opts host cell mitotic and central spindles to persist in continuously dividing cells.

P2860

Q21203557-478137D6-744E-4C59-A83E-59FD879B3984 Q24294615-32FD0FB3-DCB9-49F9-806E-7D2735660C7A Q24305141-1918D242-8087-4F60-B065-F9821BCC7A43 Q24306949-687B3A5B-3FBE-45CF-AD6A-B75318237D80 Q24315132-A78B8C86-9FB9-48B0-80D4-52642857C09F Q24323675-584F4691-15F1-4724-856E-D96A51251A39 Q26738970-0C43EF81-66A6-4D1E-8005-25B38BA98AED Q26777811-89D6420C-F5EB-4EED-A8F2-AF82049EF78F Q26779135-C7FC607A-BF24-4736-863D-D6D547777BF7 Q26825016-F50BABB6-78A7-4580-8DFB-292562CC2509 Q27025174-FF8048FF-DA3B-424A-BF0E-A6540488F93C Q27306141-0AC8B435-59DC-4DCD-8F62-2C12215613E2 Q27309180-A28B99BF-541E-443E-AD6B-607138CB5E4B Q27310061-681FCC1F-A7B3-419E-B853-99128357BD1A Q27312376-0F45C88C-A3F6-468B-B481-84859A5D5284 Q27316964-D0D63E0B-F6C6-40A1-92BE-49C710CAE3E5 Q27320850-66486CFF-D96A-4687-9B8E-E40B0A73DFBB Q27656392-312A7AE7-17F5-441E-B278-6AA4F5CD1331 Q27667451-C1AE4753-1384-430E-AAE2-96A891B40724 Q27670838-B3DE461B-D521-42C0-A24C-96E67477D520 Q27676966-6D6F4322-43E8-41E1-8F35-4D12D80008FA Q27680590-860D2647-CC81-499E-B09B-44C2AAAC8C08 Q27685281-1EC99506-4E01-4D7C-A959-FFA83ED9FB21 Q28087433-A028FB0D-F53F-4DA0-B0D2-90341015C34F Q28116932-B75348D4-1B6B-4C30-BF77-43C2071002E5 Q28286541-6A8FD996-027E-47E6-B9F0-A9B27615648C Q28300849-EAEBF3D0-279F-4A78-956C-0E3EC0EAB821 Q28476633-0ECB21FC-92AA-4D84-8659-35F5D719A46C Q28479042-DB0CA101-4F77-4861-8809-C9098270A9A1 Q28510006-F4A76997-7952-4E3B-9B3D-9A40E094B237 Q28542938-F51DD7B1-ECE9-4EE1-8EED-0BE135F4D712 Q28593959-6E166C32-35CD-41E2-A57A-77AA13742E4F Q28833851-CCED8895-0FB4-449E-819F-76F6B920AF89 Q28834282-46E07995-B30C-4DA9-A551-143003B9F709 Q30300041-DABDD44E-06E4-44F6-903F-A9109C2E9B22 Q30480149-8F553019-1C72-4247-AE96-61ACCCCD092E Q30525261-E0F74DB2-031A-4107-A98D-FC2E5F917EE5 Q33387164-7B64D532-D039-444F-981B-9C8D722D80E4 Q33574269-9D29CDA7-AC08-4EC2-AF9A-6969E59D687F Q33712012-F0E82512-4AD5-42E3-AC40-0EA17CBE3E90

P2860

Self-regulated Plk1 recruitment to kinetochores by the Plk1-PBIP1 interaction is critical for proper chromosome segregation.

http://www.wikidata.org/entity/Q34578828

description

2006 nî lūn-bûn

@nan

2006 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2006年の論文

@ja

2006年論文

@yue

2006年論文

@zh-hant

2006年論文

@zh-hk

2006年論文

@zh-mo

2006年論文

@zh-tw

2006年论文

@wuu

name

Self-regulated Plk1 recruitmen ...... proper chromosome segregation.

@ast

Self-regulated Plk1 recruitmen ...... proper chromosome segregation.

@en

Self-regulated Plk1 recruitmen ...... proper chromosome segregation.

@nl

type

label

Self-regulated Plk1 recruitmen ...... proper chromosome segregation.

@ast

Self-regulated Plk1 recruitmen ...... proper chromosome segregation.

@en

Self-regulated Plk1 recruitmen ...... proper chromosome segregation.

@nl

prefLabel

Self-regulated Plk1 recruitmen ...... proper chromosome segregation.

@ast

Self-regulated Plk1 recruitmen ...... proper chromosome segregation.

@en

Self-regulated Plk1 recruitmen ...... proper chromosome segregation.

@nl

P1433

Q34578828-2626AB39-6BEA-43BE-99D9-457C64BE8890

P1476

Q34578828-66ABA365-8E18-4580-B6C7-6C44EA2A434E

P2093

Q34578828-171398AF-D5BA-4575-B203-1427FF1745C6

Q34578828-25175E84-095E-4752-8801-0DA6DA4261CE

Q34578828-2F786D92-E050-4D21-98E9-97C2CE2C9D8C

Q34578828-498A4C2E-A89E-479C-8191-6C8A26EE24AD

Q34578828-573D6CC0-5A37-4E42-A4DC-9090269FC703

Q34578828-6554D3B6-921A-4875-ACC4-A17343973BE3

Q34578828-7267DDE4-3939-4488-B3BC-C38211DB27EF

Q34578828-7D46F7C6-6383-479A-8DD5-9719503730E5

Q34578828-A413E9AC-8B14-4700-8B8F-AFEE90D06F81

Q34578828-B3D84891-7BC8-422D-B2C9-FE4073CA94F8

P304

Q34578828-8BFCFF51-0044-4889-91AE-552C8CD08228

P31

Q34578828-45BEE5EC-FDF9-48FA-8C5A-1CB62BCC1645

P356

Q34578828-5C247800-CCFD-40C5-AE05-77E2C1FBA732

P433

Q34578828-135B0B13-BD90-4A85-ABA4-475E08392F6D

P478

Q34578828-AC8823CC-75A0-4F74-9E9F-D4BE95EE268B

P577

Q34578828-11BF0EAE-0DF8-4CF7-84D9-F2163F570CAB

P5875

Q34578828-FE1A9FE4-D497-4899-BE67-98717B32DB70

P698

Q34578828-5E59263B-3162-466E-8ADD-DB74E31A1943

P921

Q34578828-5FA78B1F-6645-400A-9B7D-6D75791D0E78

P356

J.MOLCEL.2006.10.016

P1433

P1476

Self-regulated Plk1 recruitmen ...... proper chromosome segregation.

@en

P2093

Hongtao Yu

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

Jeong K Bang

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

Jung-Eun Park

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

Kyung S Lee

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

Li-Rong Yu

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

Nak-Kyun Soung

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

Sang-Moon Yun

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

Susan Garfield

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

Timothy D Veenstra

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

Yeon-Sun Seong

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

P304

409-422

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

P31

scholarly article

P356

10.1016/J.MOLCEL.2006.10.016

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

P433

3

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

P478

24

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

P577

2006-11-01T00:00:00Z

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

P5875

6714909

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

P698

17081991

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

P921