Function and regulation of protein neddylation. 'Protein modifications: beyond the usual suspects' review series - Wikidata - wikimedia - TriplyDB

Function and regulation of protein neddylation. 'Protein modifications: beyond the usual suspects' review series

Function and regulation of protein neddylation. 'Protein modifications: beyond the usual suspects' review series

http://www.wikidata.org/entity/Q36946992

about

Identification of druggable cancer driver genes amplified across TCGA datasets The NEDD8 modification pathway in plants CSN complex controls the stability of selected synaptic proteins via a torsinA-dependent process Regulation of nucleolar signalling to p53 through NEDDylation of L11 Control of cell growth by the SCF and APC/C ubiquitin ligases Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways Posttranslational modifications of proteins in the pathobiology of medically relevant fungi Inhibition of NEDD8-conjugation pathway by novel molecules: potential approaches to anticancer therapy 60th residues of ubiquitin and Nedd8 are located out of E2-binding surfaces, but are important for K48 ubiquitin-linkage Polyubiquitin binding and cross-reactivity in the USP domain deubiquitinase USP21 Structural mechanism of ubiquitin and NEDD8 deamidation catalyzed by bacterial effectors that induce macrophage-specific apoptosis.Structural and enzymatic characterization of a host-specificity determinant fromSalmonella New suppressors of THO mutations identify Thp3 (Ypr045c)-Csn12 as a protein complex involved in transcription elongation.Systematic approaches to identify E3 ligase substrates Protein stability: a crystallographer's perspective Ubiquitylation, neddylation and the DNA damage response Myeloma overexpressed 2 (Myeov2) regulates L11 subnuclear localization through Nedd8 modification A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles The ubiquitin E1 enzyme Ube1 mediates NEDD8 activation under diverse stress conditions NEDDylation is essential for Kaposi's sarcoma-associated herpesvirus latency and lytic reactivation and represents a novel anti-KSHV target Tbata modulates thymic stromal cell proliferation and thymus function Interaction of an intracellular pentraxin with a BTB-Kelch protein is associated with ubiquitylation, aggregation and neuronal apoptosis Inactivation of SAG/RBX2 E3 ubiquitin ligase suppresses KrasG12D-driven lung tumorigenesis Dissection of DNA damage responses using multiconditional genetic interaction maps Endothelial deletion of Sag/Rbx2/Roc2 E3 ubiquitin ligase causes embryonic lethality and blocks tumor angiogenesis.MLN4924 protects against bleomycin-induced pulmonary fibrosis by inhibiting the early inflammatory process Pathogenic bacteria target NEDD8-conjugated cullins to hijack host-cell signaling pathways Noise cancellation: viral fine tuning of the cellular environment for its own genome replication.Therapeutic Effects of a NEDD8-Activating Enzyme Inhibitor, Pevonedistat, on Sclerodermatous Graft-versus-Host Disease in Mice.Histone deacetylase inhibitor (HDACI) mechanisms of action: emerging insights.In vivo RNAi screen reveals neddylation genes as novel regulators of Hedgehog signaling VACM-1/cul5 expression in vascular tissue in vivo is induced by water deprivation and its expression in vitro regulates aquaporin-1 concentrations.Protein neddylation: beyond cullin-RING ligases.The molecular determinants of NEDD8 specific recognition by human SENP8.The NEDD8 Conjugation Pathway and Its Relevance in Cancer Biology and Therapy.A novel RNAi lethality rescue screen to identify regulators of adipogenesis.p53 post-translational modification: deregulated in tumorigenesis Small RING Finger Proteins RBX1 and RBX2 of SCF E3 Ubiquitin Ligases: The Role in Cancer and as Cancer Targets Dynamics of cullin-RING ubiquitin ligase network revealed by systematic quantitative proteomics.Covalent NEDD8 conjugation increases RCAN1 protein stability and potentiates its inhibitory action on calcineurin.

P2860

Q21090621-68970FE4-EF32-4ABC-92C2-EF3D2C966C76 Q21129204-F93047A3-A0D0-4207-8742-1F524EDF9F75 Q24307876-4E22B055-2733-4F76-AAFF-228EB40345E3 Q24310534-7F424B63-1905-4ED1-8F8D-3B29F52D4B78 Q24647543-D920069F-8515-480B-A25D-8B83A5880D86 Q24647626-CF7AD33C-24F8-4203-A814-EA9CB882FFA8 Q26824233-97AA6BCA-40D0-40AF-BE34-1C59CB715E67 Q27003218-B916B85D-ADCE-4BCD-BC62-E25CCA5683F6 Q27657571-333725DA-B4F9-436A-AE79-DB3930282003 Q27667261-080F6419-918F-40C6-A284-7DE2008E974E Q27675204-504B6374-DDDC-4939-8F93-EA3A90F5AEF1 Q27681760-734C20EB-9091-477F-A237-A34FFD5586AE Q27939470-2D5E479B-900C-474A-A87D-39EEC3050139 Q28068398-0F0AB28D-E3CB-4498-B14F-129A701A5086 Q28068775-8130079E-9BFC-46F8-B0B3-04123F2E63CE Q28087342-BD21B721-9B59-4B0C-9FC4-CE2E804EB09E Q28116360-6554C796-50C4-4E87-8500-C4281E3652F2 Q28247080-B68D1967-3FF5-4CF9-85D1-BF5B6F13A0F1 Q28260754-9B8E73E8-0191-49A8-9AAA-CABF4B05CB74 Q28544735-7189B5A4-D257-4B8B-AEC8-980B906A964C Q28585690-4BEC1264-D7A9-4781-A4F3-7080C0B5BF03 Q28591483-C29BA52A-8E76-45F3-A61F-AF7501AA97D4 Q30569769-DB3A2D90-4CF3-4972-8439-9E1E12E5230F Q30663150-3222B728-D0D8-4CBB-AF12-6EEB65363946 Q33594656-033DEA31-E9DB-4AF8-A69A-BDFC30E6F271 Q33623144-B8275AFA-9B4F-4889-84F8-3D9BA1C32FA0 Q33716987-CFB9EED5-DD5F-4832-B7AC-ED77B3A8FDB3 Q33780955-0E1A0305-E876-4655-8D27-B6C7EBC925C0 Q33792598-DE4CFD90-F893-4E6A-93B9-382262F7F779 Q33983255-7326FB11-FC0B-403F-BBC8-066DB7449577 Q34023306-6DF7F905-5080-4507-BD85-85E542A8E90A Q34031947-7E51F4B9-B7F2-4D89-A5ED-A2B7D798DE90 Q34042816-1F4F15F7-E330-4D88-B88B-CAAF57C80894 Q34081793-83A47C4D-FD96-4441-84AA-B215F7B47BFF Q34202686-6D52BC03-9201-46E0-94A4-E49924841329 Q34297060-BF1F475D-ACD0-4366-8201-0F083E210AA9 Q34300569-61E9B02A-3626-4921-BC7F-5569FD2BB977 Q34318259-77F83204-F7A8-4887-A7AE-DC1FC460BA6D Q34433677-257FD52D-F58E-476D-B0D7-B41F6DB1C8AB Q34464956-AE934071-F855-48BC-9F7E-5765DD417B06

P2860

Function and regulation of protein neddylation. 'Protein modifications: beyond the usual suspects' review series

http://www.wikidata.org/entity/Q36946992

description

2008 nî lūn-bûn

@nan

2008年の論文

@ja

2008年論文

@yue

2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

2008年论文

@zh

2008年论文

@zh-cn

name

Function and regulation of pro ...... usual suspects' review series

@en

type

label

Function and regulation of pro ...... usual suspects' review series

@en

prefLabel

Function and regulation of pro ...... usual suspects' review series

@en

P1433

Q36946992-FC59B303-2057-4D51-96B3-4B28129F8CFB

P1476

Q36946992-26642A2D-B659-4B29-A02B-26EDA061EC47

P2093

Q36946992-867DE541-EA8B-4890-B31D-355BAC035A72

Q36946992-8DD4933C-79AD-4741-8837-7AD8BDBBD61E

P2860

Q36946992-04BA4545-3D21-464E-A1A3-BA21F0E69347

Q36946992-063B170D-97B6-4544-A20E-CD434E2572B5

Q36946992-066E6A80-D0F5-4E2F-876E-92BFA22D9C92

Q36946992-14594282-FC94-43D4-AAF5-6B669015E704

Q36946992-175B9E06-4F3F-4ECA-A05B-82A3BA22390A

Q36946992-18250E63-402E-46B2-A4B8-B20D73D13AF9

Q36946992-187A5B57-44FD-4775-9211-ECCF807A766F

Q36946992-1AACF842-0497-4AD5-A945-715E4C2F8C6C

Q36946992-1F6D9454-0893-42DA-A945-DD5C9AC63DD3

Q36946992-20790F04-C4A6-4102-963B-FF2F79E12AE4

P304

Q36946992-E703A5AA-FF70-415F-9B4F-0E53D3FEDDC4

P31

Q36946992-D8355A90-432C-4BA3-9F6C-DA02BBD26E7C

Q36946992-aad50913-069b-4031-b2da-9af0c1d45213

P356

Q36946992-A3D376B5-1A17-407E-8B71-DEB0898FDA68

P433

Q36946992-B1FC3F68-6F72-4C7E-970B-5772E5406488

P478

Q36946992-A5EDD418-D813-4F4A-B9F5-5EFB32E62546

P577

Q36946992-0536B5B8-C39F-4419-90E8-722C1F2B5969

P5875

Q36946992-84AF0B32-9259-442D-B7C4-CA6501785BB3

P698

Q36946992-D82760C3-FC9C-4974-A06B-BB45D7AC7A11

P932

Q36946992-31C28654-7E02-4515-8EDB-6CF751A6F7D5

P356

P1433

P1476

Function and regulation of pro ...... usual suspects' review series

@en

P2093

Gwénaël Rabut

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

Matthias Peter

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

P2860

Cullin-RING ubiquitin ligases: global regulation and activation cycles

ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity

Identification of a novel isopeptidase with dual specificity for ubiquitin- and NEDD8-conjugated proteins

The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction

Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex

A unique E1-E2 interaction required for optimal conjugation of the ubiquitin-like protein NEDD8

The conserved protein DCN-1/Dcn1p is required for cullin neddylation in C. elegans and S. cerevisiae

Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for the assembly of the multisubunit cullin-dependent ubiquitin ligases

Ribosomal proteins are targets for the NEDD8 pathway

FBXO11 promotes the Neddylation of p53 and inhibits its transcriptional activity

P304

969-976

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

P31

scholarly article

P356

10.1038/EMBOR.2008.183

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

P433

10

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

P478

9

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

P577

2008-09-19T00:00:00Z

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

P5875

23267730

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

P698

18802447

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

P932

2572130

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