Pairs of dipeptides synergistically activate the binding of substrate by ubiquitin ligase through dissociation of its autoinhibitory domain. - Wikidata - wikimedia - TriplyDB

Pairs of dipeptides synergistically activate the binding of substrate by ubiquitin ligase through dissociation of its autoinhibitory domain.

Pairs of dipeptides synergistically activate the binding of substrate by ubiquitin ligase through dissociation of its autoinhibitory domain.

http://www.wikidata.org/entity/Q34392119

about

Structure of a RING E3 trapped in action reveals ligation mechanism for the ubiquitin-like protein NEDD8 Autoregulation of Parkin activity through its ubiquitin-like domain Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation A family of mammalian E3 ubiquitin ligases that contain the UBR box motif and recognize N-degrons.The N-end rule pathway Discovery of cellular regulation by protein degradation Structural basis for autoinhibition and phosphorylation-dependent activation of c-Cbl Female lethality and apoptosis of spermatocytes in mice lacking the UBR2 ubiquitin ligase of the N-end rule pathway Harnessing natural diversity to probe metabolic pathways Structure of a Glomulin-RBX1-CUL1 Complex: Inhibition of a RING E3 Ligase through Masking of Its E2-Binding Surface Structure of HHARI, a RING-IBR-RING Ubiquitin Ligase: Autoinhibition of an Ariadne-Family E3 and Insights into Ligation Mechanism Ubr1 and Ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins.Amino acids induce peptide uptake via accelerated degradation of CUP9, the transcriptional repressor of the PTR2 peptide transporter.Degradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase Ubr1.Biochemical and genetic studies of UBR3, a ubiquitin ligase with a function in olfactory and other sensory systems The substrate recognition domains of the N-end rule pathway.The UBR-box and its relationship to binuclear RING-like treble clef zinc fingers Genomewide screen reveals a wide regulatory network for di/tripeptide utilization in Saccharomyces cerevisiae.Sent to destroy: the ubiquitin proteasome system regulates cell signaling and protein quality control in cardiovascular development and disease.Ubiquitin ligases of the N-end rule pathway: assessment of mutations in UBR1 that cause the Johanson-Blizzard syndrome The N-end rule pathway and regulation by proteolysis Sexually dimorphic effect of in vitro fertilization (IVF) on adult mouse fat and liver metabolomes Aminoacyl-transferases and the N-end rule pathway of prokaryotic/eukaryotic specificity in a human pathogen Impaired neurogenesis and cardiovascular development in mice lacking the E3 ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway.Expression and biochemical characterization of the human enzyme N-terminal asparagine amidohydrolase.Alternative ubiquitin activation/conjugation cascades interact with N-end rule ubiquitin ligases to control degradation of RGS proteins.Crystal structures of leucyl/phenylalanyl-tRNA-protein transferase and its complex with an aminoacyl-tRNA analog.Absence of the Yeast Hsp31 Chaperones of the DJ-1 Superfamily Perturbs Cytoplasmic Protein Quality Control in Late Growth Phase.Itch WW Domains Inhibit Its E3 Ubiquitin Ligase Activity by Blocking E2-E3 Ligase Trans-thiolation.Pharmacological Modulation of the N-End Rule Pathway and Its Therapeutic Implications.The N-end rule pathway is a sensor of heme.Degradation elements coincide with cofactor binding sites in a short-lived transcription factor.Regulation of peptide import through phosphorylation of Ubr1, the ubiquitin ligase of the N-end rule pathway Two proteolytic pathways regulate DNA repair by cotargeting the Mgt1 alkylguanine transferase Specificity in the actions of the UBR1 ubiquitin ligase in the degradation of nuclear receptors.Quorum sensing controls hyphal initiation in Candida albicans through Ubr1-mediated protein degradation.Policing Parkin with a UblD.SILAC-Based Quantitative Proteomic Analysis Unveils Arsenite-Induced Perturbation of Multiple Pathways in Human Skin Fibroblast Cells.Mobilization of LINE-1 retrotransposons is restricted by Tex19.1 in mouse embryonic stem cells.The N-end rule pathway is mediated by a complex of the RING-type Ubr1 and HECT-type Ufd4 ubiquitin ligases.

P2860

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P2860

Pairs of dipeptides synergistically activate the binding of substrate by ubiquitin ligase through dissociation of its autoinhibitory domain.

http://www.wikidata.org/entity/Q34392119

description

2002 nî lūn-bûn

@nan

2002 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年論文

@yue

2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

name

Pairs of dipeptides synergisti ...... of its autoinhibitory domain.

@ast

Pairs of dipeptides synergisti ...... of its autoinhibitory domain.

@en

Pairs of dipeptides synergisti ...... of its autoinhibitory domain.

@nl

type

label

Pairs of dipeptides synergisti ...... of its autoinhibitory domain.

@ast

Pairs of dipeptides synergisti ...... of its autoinhibitory domain.

@en

Pairs of dipeptides synergisti ...... of its autoinhibitory domain.

@nl

prefLabel

Pairs of dipeptides synergisti ...... of its autoinhibitory domain.

@ast

Pairs of dipeptides synergisti ...... of its autoinhibitory domain.

@en

Pairs of dipeptides synergisti ...... of its autoinhibitory domain.

@nl

P1433

Q34392119-E108D681-83FD-4250-BF22-39BFE831BBE4

P1476

Q34392119-4C5AE8F2-22FA-44E6-890B-652704633C26

P2093

Q34392119-34F1D6E3-7066-487F-BF57-E9DFF2A5D2E4

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P2860

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Q34392119-0D61A0E5-CE35-4D3B-A3D7-B94E85565ED0

Q34392119-2CC89793-AC62-486D-B8BC-C881049BFAE0

Q34392119-2D2417EB-5790-402A-B4E4-46038B40D29B

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Q34392119-992CE763-46E8-4DF4-87B0-FAB4186C0BD0

P31

Q34392119-6BC09388-EBE5-40FC-BCF2-BC608011AF32

P356

Q34392119-71F9E7A4-0280-4823-BCB2-C8D2D81573D3

P407

Q34392119-AA40DFC1-BA30-4A43-8EB6-EA67A4A65559

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Q34392119-C79B0F10-E756-452D-846F-9AA985504B26

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Q34392119-34E841F1-5983-44F3-9A8A-FE62316E3C28

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Q34392119-2D1A9928-31FC-460A-836F-62EA0D0A40A9

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Q34392119-755F509C-47FA-40B4-9D14-4963FA4FD39C

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Q34392119-E8C5C548-5EE2-4B5A-8A4C-E994DBE611ED

P932

Q34392119-BD0E65E4-90AE-48A3-B30B-481A2752A882

P356

P1433

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

P1476

Pairs of dipeptides synergisti ...... of its autoinhibitory domain.

@en

P2093

Alexander Varshavsky

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

Fangyong Du

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

Federico Navarro-Garcia

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

Takafumi Tasaki

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

Zanxian Xia

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

P2860

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

The N-end rule: functions, mysteries, uses

The mouse and human genes encoding the recognition component of the N-end rule pathway

Crystal structures of c-Src reveal features of its autoinhibitory mechanism

Mechanisms underlying ubiquitination

The N-end rule pathway controls the import of peptides through degradation of a transcriptional repressor

Peptides accelerate their uptake by activating a ubiquitin-dependent proteolytic pathway.

Physical association of ubiquitin ligases and the 26S proteasome.

Yeast N-terminal amidase. A new enzyme and component of the N-end rule pathway.

The E2-E3 interaction in the N-end rule pathway: the RING-H2 finger of E3 is required for the synthesis of multiubiquitin chain.

P304

14110-14115

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

P31

scholarly article

P356

10.1073/PNAS.172527399

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P407

P433

22

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P478

99

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P577

2002-10-21T00:00:00Z

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P5875

11071618

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P698

12391316

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P932

137845

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