von Hippel-Lindau protein binds hyperphosphorylated large subunit of RNA polymerase II through a proline hydroxylation motif and targets it for ubiquitination - Wikidata - wikimedia - TriplyDB

von Hippel-Lindau protein binds hyperphosphorylated large subunit of RNA polymerase II through a proline hydroxylation motif and targets it for ubiquitination

von Hippel-Lindau protein binds hyperphosphorylated large subunit of RNA polymerase II through a proline hydroxylation motif and targets it for ubiquitination

http://www.wikidata.org/entity/Q24554216

about

Quantitative proteomics identifies the Myb-binding protein p160 as a novel target of the von Hippel-Lindau tumor suppressor Transcriptional repression of human immunodeficiency virus type 1 by AP-4 Oxygen-regulated beta(2)-adrenergic receptor hydroxylation by EGLN3 and ubiquitylation by pVHL Erythroid-specific 5-aminolevulinate synthase protein is stabilized by low oxygen and proteasomal inhibition Prolyl 4-hydroxylase The VHL tumor suppressor: master regulator of HIF HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1alpha in normoxia The structure and regulation of Cullin 2 based E3 ubiquitin ligases and their biological functions ELA1 and CUL3 are required along with ELC1 for RNA polymerase II polyubiquitylation and degradation in DNA-damaged yeast cells PHD2: from hypoxia regulation to disease progression The Nrf1 CNC-bZIP protein is regulated by the proteasome and activated by hypoxia Molecular mechanisms of action and therapeutic uses of pharmacological inhibitors of HIF-prolyl 4-hydroxylases for treatment of ischemic diseases Intermittent hypoxia regulates RNA polymerase II in hippocampus and prefrontal cortex Activation of the prolyl-hydroxylase oxygen-sensing signal cascade leads to AMPK activation in cardiomyocytes HIF hydroxylation and cellular oxygen sensing.Von Hippel-Lindau-coupled and transcription-coupled nucleotide excision repair-dependent degradation of RNA polymerase II in response to trabectedin.iTRAQ proteomic identification of pVHL-dependent and -independent targets of Egln1 prolyl hydroxylase knockdown in renal carcinoma cells.VHL deficiency augments anthracycline sensitivity of clear cell renal cell carcinomas by down-regulating ALDH2.Von Hippel-Lindau gene deletion and expression of hypoxia-inducible factor and ubiquitin in optic nerve hemangioma.The emerging role of the COP9 signalosome in cancer.Proteomic dissection of the von Hippel-Lindau (VHL) interactome.pVHL mediates K63-linked ubiquitination of nCLU.The hypoxia-inducible-factor hydroxylases bring fresh air into hypoxia signalling.Deficiency of a transmembrane prolyl 4-hydroxylase in the zebrafish leads to basement membrane defects and compromised kidney function VHL, the story of a tumour suppressor gene.The multifaceted von Hippel-Lindau tumour suppressor protein.Folliculin contributes to VHL tumor suppressing activity in renal cancer through regulation of autophagy.Ubiquitin pathway in VHL cancer syndrome.Clusterin is a secreted marker for a hypoxia-inducible factor-independent function of the von Hippel-Lindau tumor suppressor protein.Peroxisomal localization of hypoxia-inducible factors and hypoxia-inducible factor regulatory hydroxylases in primary rat hepatocytes exposed to hypoxia-reoxygenation.Oxygen sensing in cancer.The role of von Hippel-Lindau tumor suppressor protein and hypoxia in renal clear cell carcinoma.The Role of Elongin BC-Containing Ubiquitin Ligases.The VHL tumor suppressor in development and disease: functional studies in mice by conditional gene targeting.Manipulation of oxygen tensions for in vitro cell culture using a hypoxic workstation.The von Hippel-Lindau tumor suppressor protein and Egl-9-Type proline hydroxylases regulate the large subunit of RNA polymerase II in response to oxidative stress.Influence of the RNA-binding protein HuR in pVHL-regulated p53 expression in renal carcinoma cells Non-heme dioxygenases: cellular sensors and regulators jelly rolled into one?Hypoxia inducible factor prolyl 4-hydroxylase enzymes: center stage in the battle against hypoxia, metabolic compromise and oxidative stress.O(2)-sensing signal cascade: clamping of O(2) respiration, reduced ATP utilization, and inducible fumarate respiration.

P2860

Q21135547-0179FC1E-125C-485D-A928-186043657255 Q24307916-642B9F22-EF26-4F09-A66F-C032B00E82A8 Q24311838-BBCB743C-6A3A-49C0-986D-028249F505B1 Q24338581-7CFF9C97-72DE-477C-82F3-997388827DB4 Q24622617-0F1B7882-9161-451A-90B7-302660A92B6F Q24634592-D9756190-A959-4EF1-B01F-D7358FF1B468 Q24671941-35345557-C74A-44D0-AFD3-6FE707613FDA Q26746044-6F23F661-0854-4877-8424-84818A1A8E2B Q27934208-F23A613B-CB9F-47B8-B1FF-C34A81F96013 Q28069316-B001A28A-CE4C-4B1F-A1A5-D03C23FD4333 Q28256645-EE29A41D-C513-4B56-ABC9-2EAC377B6D5A Q28297656-14B83427-3FDD-4A16-962D-652E00072030 Q28575017-CF07F653-1824-4306-BA2B-A91C1238D967 Q28580371-14B4F860-3899-4C78-92A8-374AB01431F0 Q30164092-5712A3A3-741C-4502-A4DC-488DCE7F1F8D Q33377399-DD6AD843-3B11-4633-AEE5-1C289C0CF254 Q33401743-D8061C87-5693-4677-8421-3E9220968212 Q33826897-B1EC133F-C848-4648-A5F9-5F339B2A4C2A Q34123458-8998D8B2-94C0-4E37-825E-5A7226C0D8DC Q34147948-62CAD34E-889B-430B-A1C7-00185E659DC9 Q34218966-1B9EBB3A-4EC5-4E3C-BEBA-45AAADD31E6E Q34245192-EFFDEBBC-0D7A-4ADA-9F12-EB936DCD24D9 Q34360746-C429421F-AEE3-4552-94B5-6529A1E9832F Q34439080-D23E95BA-DE5E-4165-A31D-4FEF3EB552C6 Q34455226-3845029A-9C10-423E-8935-DB8D36F37E2D Q34660062-5EF985A1-15D1-4372-A074-ECC77859CC0C Q34905447-9A7EE1D0-AE29-4727-9570-9DA549703828 Q35082720-95A3A0CB-FB75-405E-9988-38F4DD99AE49 Q35087893-F9F2FB4A-3E78-498C-B1E6-0315B1AC7D69 Q35222144-C910D279-E47C-4697-BF9C-D5DDF98275B0 Q35565483-7EADCAA9-8AE2-4CC5-B66D-D0EEDAD23739 Q35794374-AAEA3E1B-5DA3-45DA-8046-F3C90D190BD8 Q35971082-3DF5BC33-E351-44E7-A4C9-A62D39ADCF7B Q36134573-6DC0D5A9-6853-44B1-AAAD-9D453D266CC0 Q36184777-2D0A061B-27D2-4E59-A74A-C953EB3189C2 Q36540303-EB409BE9-1A80-43C3-B982-7A9384CCD8F3 Q36549605-81BB6689-6714-4CBA-A3B0-C5B0CD8D4957 Q36736166-748BD45D-5503-46CB-851D-D48CBB0815ED Q36753387-574F4170-0FB4-4ECC-8F3E-1105F43020C9 Q36805298-E813458C-F49C-4419-BC48-5275517D96CF

P2860

von Hippel-Lindau protein binds hyperphosphorylated large subunit of RNA polymerase II through a proline hydroxylation motif and targets it for ubiquitination

http://www.wikidata.org/entity/Q24554216

description

2003 nî lūn-bûn

@nan

2003 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի մարտին հրատարակված գիտական հոդված

@hy

2003年の論文

@ja

2003年論文

@yue

2003年論文

@zh-hant

2003年論文

@zh-hk

2003年論文

@zh-mo

2003年論文

@zh-tw

2003年论文

@wuu

name

von Hippel-Lindau protein bind ...... targets it for ubiquitination

@ast

von Hippel-Lindau protein bind ...... targets it for ubiquitination

@en

von Hippel-Lindau protein bind ...... targets it for ubiquitination

@nl

type

label

von Hippel-Lindau protein bind ...... targets it for ubiquitination

@ast

von Hippel-Lindau protein bind ...... targets it for ubiquitination

@en

von Hippel-Lindau protein bind ...... targets it for ubiquitination

@nl

prefLabel

von Hippel-Lindau protein bind ...... targets it for ubiquitination

@ast

von Hippel-Lindau protein bind ...... targets it for ubiquitination

@en

von Hippel-Lindau protein bind ...... targets it for ubiquitination

@nl

P1433

Q24554216-C6DB4F31-CDCC-4C5B-A27B-6D1A6677530A

P1476

Q24554216-B101B9A5-071F-4A65-B693-C0B4030A4F5F

P2093

Q24554216-06363B3B-EE6C-4989-A458-EBEE34CA1659

Q24554216-14348DE7-7AD8-4E68-AD86-A2FE033F4369

Q24554216-2F510AF7-9928-4701-9DDC-7F6291CC7909

Q24554216-333E2CC0-ADC9-459B-8DAF-19A4B534586F

Q24554216-5FA922E8-B866-49C7-8E0B-A475AF748286

Q24554216-6D833C7F-CAD5-4A74-B6DC-E30CFFFBE019

Q24554216-85A39BBA-2E3C-46AA-A006-E16E15B6EEE9

Q24554216-9A5F0CBA-FBAF-4D6B-B50B-69D39DDCE586

P2860

Q24554216-16058462-7505-4E53-861D-2A12E04A5D7E

Q24554216-1C5898F2-F9B1-418D-B09C-6579465173BB

Q24554216-1EFA543F-D983-45DB-8D77-D705DFD6409F

Q24554216-20AA5395-71C2-4054-9B06-1FED7073B904

Q24554216-25F522DD-E2AA-4DA1-961C-B543E0A51CA3

Q24554216-29F75B00-1FB2-4368-BC74-51297E992EDE

Q24554216-3346E5B0-79E5-405B-B2A6-793B53E48AFB

Q24554216-3351B1AC-C1B9-4D24-985B-925051D96633

Q24554216-43D98D03-F65C-4875-9FFA-49378740FA0D

Q24554216-44291FAB-13EF-4A6E-B7CE-B5C2DD563FD9

P304

Q24554216-2C229E73-6CD2-43BB-AF8C-4786E42D8EF1

P31

Q24554216-0C889B41-81B9-42BC-A1E3-5887547D2EC5

P3181

Q24554216-2CFD313E-414C-4B25-AE6C-97D0CB00D44C

P356

Q24554216-9238471C-5658-4C1B-9B9C-130643810A30

P407

Q24554216-4532C2E3-ABD8-4B12-AF4D-DA6F40273385

P433

Q24554216-73FF005F-60AD-445C-9388-7C73CF1034D6

P478

Q24554216-3996B813-7EA6-4E19-BAC5-AC292A5DF76C

P50

Q24554216-7E244B55-6075-4823-82B9-A393839F65AB

P577

Q24554216-EE0A520C-DCBE-47CD-8280-652D6E7BE9AE

P5875

Q24554216-6E46D828-48C5-4228-9CE3-ED3FD9A589CC

P698

Q24554216-8BA22E65-E2B9-4BB0-ABFB-41E19B6DA626

P921

Q24554216-17D83320-10F7-438E-9F9D-315C927C657B

Q24554216-822EC244-0370-4396-B179-FA140802C725

P932

Q24554216-CCB22243-AFDD-4599-AE05-4E21EEB677C8

P3181

P356

PNAS.0436037100

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

von Hippel-Lindau protein bind ...... targets it for ubiquitination

@en

P2093

Anna V Kuznetsova

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

James A Nash

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

Jaroslaw Meller

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

Maria F Czyzyk-Krzeska

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

Monika L Ignacak

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

Phillip O Schnell

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

Ronald C Conaway

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

Yolanda Sanchez

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

P2860

HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing

C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation

A conserved family of prolyl-4-hydroxylases that modify HIF

Ubiquitination of a novel deubiquitinating enzyme requires direct binding to von Hippel-Lindau tumor suppressor protein

Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling

Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL

Inhibition of transcription elongation by the VHL tumor suppressor protein

Binding of the von Hippel-Lindau tumor suppressor protein to Elongin B and C

HIF-1alpha binding to VHL is regulated by stimulus-sensitive proline hydroxylation

The von Hippel-Lindau tumor-suppressor gene product forms a stable complex with human CUL-2, a member of the Cdc53 family of proteins

P304

2706-11

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

P31

scholarly article

P3181

1425019

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

P356

10.1073/PNAS.0436037100

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

P407

P433

5

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

P478

100

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

P50

Joan W. Conaway

P577

2003-03-04T00:00:00Z

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

P5875

10884050

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

P698

12604794

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

P921

protein ubiquitination

proline hydroxylation

P932

151405

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