Synthetic biology approach to reconstituting the ubiquitylation cascade in bacteria. - Wikidata - wikimedia - TriplyDB

Synthetic biology approach to reconstituting the ubiquitylation cascade in bacteria.

Synthetic biology approach to reconstituting the ubiquitylation cascade in bacteria.

http://www.wikidata.org/entity/Q40514576

about

The Ubiquitin System and Jasmonate Signaling A bacterial genetic selection system for ubiquitylation cascade discovery A comparative analysis of the ubiquitination kinetics of multiple degrons to identify an ideal targeting sequence for a proteasome reporter The challenge of producing ubiquitinated proteins for structural studies Ubiquitin binding by the CUE domain promotes endosomal localization of the Rab5 GEF Vps9.Spatiotemporal regulation of the ubiquitinated cargo-binding activity of Rabex-5 in the endocytic pathway.Structure-based in silico identification of ubiquitin-binding domains provides insights into the ALIX-V:ubiquitin complex and retrovirus budding Measuring activity in the ubiquitin-proteasome system: from large scale discoveries to single cells analysis Enzymatic production of mono-ubiquitinated proteins for structural studies: The example of the Josephin domain of ataxin-3.Chemistry and biology of the ubiquitin signal.Ubiquitylation-dependent oligomerization regulates activity of Nedd4 ligases.Biological and Physicochemical Functions of Ubiquitylation Revealed by Synthetic Chemistry Approaches.Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism.An assay for 26S proteasome activity based on fluorescence anisotropy measurements of dye-labeled protein substrates Purification and crystallization of mono-ubiquitylated ubiquitin receptor Rpn10.UbiGate: a synthetic biology toolbox to analyse ubiquitination.Excessive UBE3A dosage impairs retinoic acid signaling and synaptic plasticity in autism spectrum disorders.Reconstitution of the plant ubiquitination cascade in bacteria using a synthetic biology approach.A versatile plasmid system for reconstitution and analysis of mammalian ubiquitination cascades in yeast.

P2860

Q26748467-93D11953-AA4D-41BE-803D-1CDF24FFCB58 Q27728163-83D52AC6-D5DC-49B0-9ECE-70B0A19924B3 Q28301510-3125DBE1-DB1B-4C9E-B9D2-9C689B139F74 Q33883901-428C170A-400B-4731-B610-3C36C4E3CB58 Q35679268-8904701D-2847-41FF-BF8A-9EB6B422297C Q36418897-11948A20-0463-41A2-89A5-99C7422D7401 Q36628891-01373326-6335-4195-829E-98F60821C1A1 Q37136216-C6C852B9-6B68-4F1C-9717-367DD6174D23 Q37313663-FB23EAD6-584E-48F9-BCEA-7C43A893F255 Q38018581-C4D82973-7E6B-4BA0-9BA3-9744099A355C Q39030641-EF1C3180-DA7B-48FB-8486-5ADF9C990F53 Q39336897-73040025-FEE7-48A8-8B59-6D42EEFF897D Q41429616-08DB168D-F242-46B3-B84C-97C196D3B439 Q41729079-729A9A27-B939-4DCC-8BFF-0BAD8AB29EE2 Q41780704-B5ED43DD-293C-4B45-ABC5-AB97AAB7DDCC Q47342192-BB479C97-2462-42CD-AC30-B5D49735C428 Q47998222-A664A153-C6C2-47BE-A9EB-6C8A9897D24F Q50437900-1CD28B4F-2525-4B68-BE7A-DDE4BE9E945D Q52371879-5F44A8F9-35F8-4B4A-B52A-6130038B7267

P2860

Synthetic biology approach to reconstituting the ubiquitylation cascade in bacteria.

http://www.wikidata.org/entity/Q40514576

description

2011 nî lūn-bûn

@nan

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

2011年论文

@zh

2011年论文

@zh-cn

name

Synthetic biology approach to reconstituting the ubiquitylation cascade in bacteria.

@en

type

label

Synthetic biology approach to reconstituting the ubiquitylation cascade in bacteria.

@en

prefLabel

Synthetic biology approach to reconstituting the ubiquitylation cascade in bacteria.

@en

P1433

Q40514576-2F8EBF56-680E-4540-9451-973847138C28

P1476

Q40514576-FBBFCDC8-935C-406B-96F0-D7AA982EC5A0

P2093

Q40514576-0A5B074D-3BC4-413A-B986-A38C9C63BC77

Q40514576-4506239E-958C-41A6-870E-F1B38CF20989

Q40514576-73922341-9BD6-452A-A94E-E3F3C07F6461

Q40514576-7489830F-9AF6-49E5-B09C-B750C4508449

Q40514576-869004A9-1353-4724-A2F3-6EE0742CF252

Q40514576-B00EE5ED-FE4E-4D06-A0CE-7265A63C9CE3

Q40514576-B82370E6-C377-4B1A-8B49-4EE0577FEBC8

Q40514576-C1390739-777E-4A7B-885D-16324EC91243

Q40514576-C5FE64B7-9D52-4712-87FC-D907BACDDC6B

Q40514576-C916CD75-9EB8-47BA-8443-56DCC7D6201F

P2860

Q40514576-005A556F-7D71-4D2F-8973-11799595DCCD

Q40514576-086773A8-2414-4A14-B0C3-4E3D8396EB42

Q40514576-0E92DDA0-E491-45E6-8751-64732EA47BEC

Q40514576-21C3F5CC-79A8-4D56-917D-CB2BBBE5954A

Q40514576-22797FF7-5BBC-4412-A006-4A09D5C1338D

Q40514576-283121A9-3825-48ED-8E80-E3284B384D1B

Q40514576-2BCD46D5-BF2F-4B7C-913A-ECC4A818566D

Q40514576-3108A503-B568-42B4-AD8E-FAFC7FFDF3EA

Q40514576-3113ED8C-DADB-4467-99AA-3C1A826BF6FD

Q40514576-32601E93-163B-4A5C-A1B0-228AB871B703

P304

Q40514576-8DC8BB4B-1FC3-4299-B560-C7EA1FDE4861

P31

Q40514576-B6CF588F-AE0E-416F-A60C-FF3E47F83EAA

P356

Q40514576-1969F9F9-3190-47C9-AEF6-5CBE13B99A2A

P407

Q40514576-4FDF3315-0835-471B-B508-E22C78F71EEC

P433

Q40514576-AA7A4360-C6D9-41FA-993D-4D86F0A2E5FC

P478

Q40514576-BFEF08B6-7F1D-416C-A2F1-7E73615DC12D

P50

Q40514576-D374EF81-4B7C-49CA-8EAB-841C1C0DD0F8

Q40514576-EDB2AC43-564E-4B22-98ED-3C7D56B1A57A

P577

Q40514576-8B872725-2193-4629-8963-398DA6CDA7C0

P5875

Q40514576-00D38477-47E7-42B2-BB34-D49FD587966D

P698

Q40514576-C813C96E-05E4-41A9-8BE6-DD31268871EF

P921

Q40514576-4F195AC0-F966-449B-8F7F-3DDA4AF111E6

Q40514576-D0DEAB2C-2587-47F4-8D18-2EDA078030DD

P932

Q40514576-F0808834-38B4-4B1B-88E2-BA2F3290AC5B

P356

P1433

The EMBO Journal

P1476

Synthetic biology approach to reconstituting the ubiquitylation cascade in bacteria

@en

P2093

Brian A Davis

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

Bruce F Horazdovsky

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

Einat Laudon

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

Gali Prag

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

Ilan Attali

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

Khatereh Motamedchaboki

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

Mikhail Kolot

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

Neta Tanner

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

Oded Kleifeld

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

Olga Levin-Kravets

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

P2860

Genome-wide and functional annotation of human E3 ubiquitin ligases identifies MULAN, a mitochondrial E3 that regulates the organelle's dynamics and signaling

Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair

RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination

U box proteins as a new family of ubiquitin-protein ligases

Structural basis for Rab GTPase activation by VPS9 domain exchange factors

Crystal structure of the ubiquitin binding domains of rabex-5 reveals two modes of interaction with ubiquitin

Monoubiquitinylation regulates endosomal localization of Lst2, a negative regulator of EGF receptor signaling

A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase

Proximity-induced activation of human Cdc34 through heterologous dimerization.

Proposed role of ATP in protein breakdown: conjugation of protein with multiple chains of the polypeptide of ATP-dependent proteolysis

P304

378-390

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

P31

scholarly article

P356

10.1038/EMBOJ.2011.397

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

P407

P433

2

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

P478

31

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

P50

Michael H Glickman

P577

2011-11-11T00:00:00Z

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

P5875

51789596

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

P698

22081111

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

P921

synthetic biology

P932

3261559

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