Active site remodelling accompanies thioester bond formation in the SUMO E1 - Wikidata - wikimedia - TriplyDB

Active site remodelling accompanies thioester bond formation in the SUMO E1

Active site remodelling accompanies thioester bond formation in the SUMO E1

http://www.wikidata.org/entity/Q24299970

about

Isoform-specific monobody inhibitors of small ubiquitin-related modifiers engineered using structure-guided library design K11-linked ubiquitin chains as novel regulators of cell division Advances in the development of SUMO specific protease (SENP) inhibitors Crystal Structure of UBA2ufd-Ubc9: Insights into E1-E2 Interactions in Sumo Pathways Noncanonical E2 recruitment by the autophagy E1 revealed by Atg7–Atg3 and Atg7–Atg10 structures Atg8 Transfer from Atg7 to Atg3: A Distinctive E1-E2 Architecture and Mechanism in the Autophagy Pathway Insights into noncanonical E1 enzyme activation from the structure of autophagic E1 Atg7 with Atg8 Determinants of Small Ubiquitin-like Modifier 1 (SUMO1) Protein Specificity, E3 Ligase, and SUMO-RanGAP1 Binding Activities of Nucleoporin RanBP2 Structure of a Ubiquitin E1-E2 Complex: Insights to E1-E2 Thioester Transfer Structural and Functional Investigation of the Intermolecular Interaction between NRPS Adenylation and Carrier Protein Domains Recognition of SUMO-modified PCNA requires tandem receptor motifs in Srs2 Structure of PA1221, a Nonribosomal Peptide Synthetase Containing Adenylation and Peptidyl Carrier Protein Domains Structure of the ubiquitin-activating enzyme loaded with two ubiquitin molecules Expression, purification, and crystal structure of N-terminal domains of human ubiquitin-activating enzyme (E1)A cascading activity-based probe sequentially targets E1-E2-E3 ubiquitin enzymes Role of the Zn(2+) motif of E1 in SUMO adenylation The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition.Largazole and its derivatives selectively inhibit ubiquitin activating enzyme (e1)Perilous journey: a tour of the ubiquitin-proteasome system A Chemical and Enzymatic Approach to Study Site-Specific Sumoylation Probes of ubiquitin E3 ligases enable systematic dissection of parkin activation Small-molecule activation of SERCA2a SUMOylation for the treatment of heart failure.Structural and functional insights to ubiquitin-like protein conjugation.Protein neddylation: beyond cullin-RING ligases.Elevated global SUMOylation in Ubc9 transgenic mice protects their brains against focal cerebral ischemic damage.Twists and turns in ubiquitin-like protein conjugation cascades.Mechanism of E1-E2 interaction for the inhibition of Ubl adenylation Neuronal SUMOylation: mechanisms, physiology, and roles in neuronal dysfunction.The dynamics and mechanism of SUMO chain deconjugation by SUMO-specific proteases.Development of FRET assay into quantitative and high-throughput screening technology platforms for protein-protein interactions.Macromolecular juggling by ubiquitylation enzymes.SUMO-mimicking peptides inhibiting protein SUMOylation.Mechanistic studies on activation of ubiquitin and di-ubiquitin-like protein, FAT10, by ubiquitin-like modifier activating enzyme 6, Uba6 Small ubiquitin-like modifier (SUMO) modification mediates function of the inhibitory domains of developmental regulators FOXC1 and FOXC2 Designed Small-Molecule Inhibitors of the Anthranilyl-CoA Synthetase PqsA Block Quinolone Biosynthesis in Pseudomonas aeruginosa An in vitro Förster resonance energy transfer-based high-throughput screening assay for inhibitors of protein-protein interactions in SUMOylation pathway.Stable analogues of OSB-AMP: potent inhibitors of MenE, the o-succinylbenzoate-CoA synthetase from bacterial menaquinone biosynthesis Using protein motion to read, write, and erase ubiquitin signals.Specificity of the E1-E2-E3 enzymatic cascade for ubiquitin C-terminal sequences identified by phage display Streamlined expressed protein ligation using split inteins.

P2860

14f4e6d5200f05d15ee6bd75d34d6edbf7a79890 266c351720db6b59877b7453916435da52bd5caa 46addb05770e159df5376830963774e2d0318214 47b1fe886870aa42db7d763b635203b83c05ad94 6b3b4d70fbd18a34e53cd0ffec0a9e277263fd2d 6e73c77708c0d01142d6a32c88e8b80873a070c9 90914d6b22a5009473d516cc048727448b829605 c443b6a25f5be8797c8e38ca064d66f248a6e847 d56cd25a0dd725597a793e4078410cd5248decd5 e34a5e2a9e700a7333ba5025a9105382203f2f53 e362eb3e3d136dc3827d7c65ea09ba1d55a579a9 f385733333a37f0f43c5b89d2e1461cf7011dcb3

P248

Q24594140-022FC536-BF9F-47FF-A065-292FF809A03B Q26851677-DCD047E7-EE93-44C8-88E5-20F1BA25358E Q26864235-43103E05-1593-4525-BA73-CD6817F1952A Q27666500-F1F64704-793C-438E-9E9A-4D9060D55B36 Q27675051-FC32E9BA-7139-4F29-9B68-865A32890CCD Q27675398-8295C513-D8A7-4BDD-AEE8-8CE22B77EF6E Q27675408-BEC8D820-DDBD-4AA7-85F8-90AAF510C599 Q27676384-5A49B847-249E-4205-9685-F93C9E607C6C Q27676404-128B5567-27E5-482A-A84F-CE26C8DA3B08 Q27677481-1BB8B905-C90B-44E4-BF86-517381E3AC60 Q27677554-017E27DE-0202-4BEE-905C-67C23F2A1DC7 Q27678231-664DD60A-CDD0-4139-93B6-D1969CD497CC Q27690199-33A94B3C-4DAF-40D3-9D44-5EA4211E19A2 Q27695600-CE3A3C04-1957-4A7F-A1D2-DE50BF0103C8 Q27704870-A932DBDD-DA2F-4560-951F-D37D8E67414F Q27865252-86248954-949F-4B34-86FE-E2FA926C1C37 Q27865256-EE9C109B-E75C-4809-B60C-4F41EC083337 Q28258201-C8305AC0-039A-4760-99AC-F441CD3817BB Q28306492-D34B4C9B-24E5-4F52-98DA-4B682ECE8D7A Q28551317-32A3B658-2322-4307-B2F5-0FC6908BA737 Q28830194-74D8FC3B-F2A8-4E1A-8DEB-C858EE7F8DE4 Q30654383-E3674243-D58C-424D-9BB3-A8968B25B16F Q33987001-0A294179-8A83-4C12-88E9-33440B11436C Q34042816-DADFB5BE-2AC4-4BFF-850F-3BCA331DCA57 Q34053347-A60F54CE-A016-434E-8FD8-9001E9026E3A Q34225698-E0047399-DA5F-4445-87DB-98572FC0DCD9 Q34236443-091CC273-A30D-40A7-B967-7420CEC38CD1 Q34295237-A13F48A0-E1B9-4B78-B865-3FF9E819F0F3 Q34695640-6E668CFC-93E9-4519-8F4F-4404B9C93908 Q34751430-C5CFE4BE-CC46-4D8E-A9D0-C68CBEAE0BF9 Q34782977-058B9BC0-94B6-4A34-9B1C-2150E7317B8C Q35440501-AAA2C439-AC80-4780-B241-A88B0D803ACA Q35939802-67578639-50CD-4FC0-B8E5-0546F9DADF2E Q36003002-5B365DE5-F31C-4BEE-B50E-7C8DADE85480 Q36141081-8662B081-DB4D-4FD2-9C8D-1CB18B9D53F8 Q36166518-5BA242AA-93D7-4C30-AA0E-D63019EB51EF Q36218220-6A7D093D-E2F3-4691-805B-F2A222CEF41B Q36283663-28F089CF-DA30-4C1F-A744-47957C190507 Q36298709-8215F178-08AC-4EF2-B990-504AD83EC786 Q36530093-24E5B962-9C15-4F4C-8C19-E78A48847249

P2860

Active site remodelling accompanies thioester bond formation in the SUMO E1

http://www.wikidata.org/entity/Q24299970

description

2010 nî lūn-bûn

@nan

2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Active site remodelling accompanies thioester bond formation in the SUMO E1

@ast

Active site remodelling accompanies thioester bond formation in the SUMO E1

@en

Active site remodelling accompanies thioester bond formation in the SUMO E1

@en-gb

Active site remodelling accompanies thioester bond formation in the SUMO E1

@nl

type

label

Active site remodelling accompanies thioester bond formation in the SUMO E1

@ast

Active site remodelling accompanies thioester bond formation in the SUMO E1

@en

Active site remodelling accompanies thioester bond formation in the SUMO E1

@en-gb

Active site remodelling accompanies thioester bond formation in the SUMO E1

@nl

prefLabel

Active site remodelling accompanies thioester bond formation in the SUMO E1

@ast

Active site remodelling accompanies thioester bond formation in the SUMO E1

@en

Active site remodelling accompanies thioester bond formation in the SUMO E1

@en-gb

Active site remodelling accompanies thioester bond formation in the SUMO E1

@nl

P1433

Q24299970-F13A464D-D02E-4AD2-871A-D8AFEA7F1114

P1476

Q24299970-C69FED8E-F042-438E-A0C5-6910BF0F85BE

P2093

Q24299970-12A1202D-9C0C-4B81-886E-8B7B3CEAB77B

Q24299970-40CD345E-0893-4677-821D-EEFC9447095A

Q24299970-808B1E92-AD47-4E23-BE50-8254D3919EE4

Q24299970-C9B4F99D-E1E2-4DC1-AD7E-E61CF8956165

Q24299970-E8A5E0F9-7586-4E81-AF20-CC48BFDB443B

P2860

Q24299970-08F71245-AF56-4C35-ABF1-5AD9B60208F9

Q24299970-12B7767F-94FB-4435-BEC7-5BD6A1050422

Q24299970-14DCED52-686D-44C4-8A01-9925A29039CC

Q24299970-1CEDF3E0-6626-4B0B-9809-2E52DDC6247D

Q24299970-30F6AB44-F831-49EA-8B16-0EE4E3DD5961

Q24299970-3E3304F0-1C92-4CA2-8724-0065FEF77E81

Q24299970-4ACC9FED-97B5-4F3B-8703-293C38B3E416

Q24299970-4EC66441-C562-4565-A9DF-0A04931948F3

Q24299970-6327E823-0D59-44FA-AC54-FAF0DB104C3C

Q24299970-6375EB7D-0E63-4B2D-B785-49133CC525F2

P2888

Q24299970-3A4BDF6A-FE79-49B9-81DD-B241FED02D4B

P304

Q24299970-13FC7273-A199-4F76-883B-5CCFAC858554

P31

Q24299970-DB5F5127-74C3-4E0C-8332-E59922C3AD0A

P3181

Q24299970-2567CC22-AF46-4356-8375-C57C23EBF66A

P356

Q24299970-666C6864-4FD5-4605-934A-B2FA337EDAD7

P407

Q24299970-75F5B25B-E4CF-420E-A4E0-3D9E1A08BF22

P433

Q24299970-87477215-5B70-4830-8E31-6A958C437BFD

P478

Q24299970-CE67EF3B-CEDB-489E-965A-D01BFF421EDB

P577

Q24299970-2F5D5E10-3EEE-4ABC-A0C2-0587AD7D5774

P5875

Q24299970-C8944581-344B-45A3-A8FE-108CF314EE3F

P6179

Q24299970-0053C213-ABBA-480D-B01C-ADB27FB94C3A

P698

Q24299970-D31FCB7C-3C19-451E-90F0-5708F8CB4D43

P921

Q24299970-35625EF7-B924-4EBF-BA5F-ED8911EBF428

Q24299970-48AE9284-7C79-4AF2-A89D-82179C56AE57

Q24299970-4C113B3B-8226-4B60-931A-0B00BB0642F3

P932

Q24299970-78701D5A-F7EF-4EA7-8DAD-063DB4FF0F67

P3181

P356

P1433

P1476

Active site remodelling accompanies thioester bond formation in the SUMO E1.

@en

P2093

Allan D Capili

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

Christopher D Lima

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

Derek S Tan

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

Shaun K Olsen

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

Xuequan Lu

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

P2860

Conformational flexibility underlies ubiquitin ligation mediated by the WWP1 HECT domain E3 ligase

Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1

Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast

Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex

Basis for a ubiquitin-like protein thioester switch toggling E1–E2 affinity

The structure of the APPBP1-UBA3-NEDD8-ATP complex reveals the basis for selective ubiquitin-like protein activation by an E1

Structural insights into E1-catalyzed ubiquitin activation and transfer to conjugating enzymes

P2888

P304

906-12

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

P31

scholarly article

P3181

3943404

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

P356

10.1038/NATURE08765

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

P407

P433

7283

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

P478

463

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

P577

2010-02-18T00:00:00Z

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

P5875

41466460

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

P6179

1001908526

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

P698

20164921

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

P921

protein heterodimerization activity

Ubiquitin like modifier activating enzyme 2

SUMO1 activating enzyme subunit 1

P932

2866016

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