about
Adenylylation control by intra- or intermolecular active-site obstruction in Fic proteinsFic domain-catalyzed adenylylation: Insight provided by the structural analysis of the type IV secretion system effector BepAStructure of the Legionella effector AnkX reveals the mechanism of phosphocholine transfer by the FIC domainConserved Inhibitory Mechanism and Competent ATP Binding Mode for Adenylyltransferases with Fic FoldCrystal Structure of the Escherichia coli Fic Toxin-Like Protein in Complex with Its Cognate AntitoxinRho GTPase Recognition by C3 Exoenzyme Based on C3-RhoA Complex Structure.Expression of Histophilus somni IbpA DR2 protective antigen in the diatom Thalassiosira pseudonana.Comparative analysis of Histophilus somni immunoglobulin-binding protein A (IbpA) with other fic domain-containing enzymes reveals differences in substrate and nucleotide specificities.AMPylation: Something Old is New AgainInhibiting AMPylation: a novel screen to identify the first small molecule inhibitors of protein AMPylation.Crystal structure of the human, FIC-domain containing protein HYPE and implications for its functions.novPTMenzy: a database for enzymes involved in novel post-translational modifications.A chemical reporter for protein AMPylation.In silico identification of AMPylating enzymes and study of their divergent evolution.Global Profiling of Huntingtin-associated protein E (HYPE)-Mediated AMPylation through a Chemical Proteomic Approach.Intrinsic regulation of FIC-domain AMP-transferases by oligomerization and automodification.Doc toxin is a kinase that inactivates elongation factor TuExploring adenylylation and phosphocholination as post-translational modifications.Probing adenylation: using a fluorescently labelled ATP probe to directly label and immunoprecipitate VopS substrates.Structure and function of Fic proteins.HypE-specific nanobodies as tools to modulate HypE-mediated target AMPylation.rAMPing Up Stress Signaling: Protein AMPylation in Metazoans.Protein expression, characterization, crystallization and preliminary X-ray crystallographic analysis of a Fic protein from Clostridium difficileA Novel Fic (Filamentation Induced by cAMP) Protein from Clostridium difficile Reveals an Inhibitory Motif-independent Adenylylation/AMPylation Mechanism.FICD acts bifunctionally to AMPylate and de-AMPylate the endoplasmic reticulum chaperone BiP.A novel link between Fic (filamentation induced by cAMP)-mediated adenylylation/AMPylation and the unfolded protein responseKey enzymes enabling the growth of Arthrobacter sp. strain JBH1 with nitroglycerin as the sole source of carbon and nitrogen.The Fic protein Doc uses an inverted substrate to phosphorylate and inactivate EF-TuFic Proteins of Campylobacter fetus subsp. venerealis Form a Network of Functional Toxin-Antitoxin Systems.Enzyme mechanisms: What's up 'Doc'?Enzymes Involved in AMPylation and deAMPylation.Substrate Recognition of MARTX Ras/Rap1-Specific Endopeptidase.YopT domain of the PfhB2 toxin from Pasteurella multocida: protein expression, characterization, crystallization and crystallographic analysis.A New Chemical Handle for Protein AMPylation at the Host-Pathogen Interface
P2860
Q24302658-D0090990-F790-4CF9-A3DC-55A4A1753AD6Q27666512-47FBA099-FE1E-4F9B-A864-1A0BB57F6893Q27677280-87329FD5-0269-444F-A412-D907F19F848EQ27678499-787C13BA-0C33-4300-98F7-8923941FD189Q28554287-0065D01F-DB19-4EC5-B950-CAD3570F6481Q30375572-5D9AFB16-13A9-4491-BC38-3B8EE60F43BFQ33841510-12BFA875-E230-4483-AAF3-1363BEFA2FB7Q33973430-78A19C97-7866-476E-968B-28FBA2BB0B29Q34629458-4B1D07A3-3547-418C-9A21-BBA5DF5CFA24Q35052423-A69E3348-59BB-4A7D-9EBF-979677F6F6D4Q35126437-97A17058-83F3-4BEF-9B4B-374716608AA2Q35554912-11A0D4B4-ABA5-4CA5-AE87-D476FB7FA636Q35635498-86E95F78-6F7A-4870-BA48-B7609BB95181Q35678963-78220895-C362-43D2-AB65-6E9EE0E55838Q35851894-752F3B35-0C27-4AE2-8064-48F976FFD6CCQ36563109-A07C244E-14A7-45D3-A9C6-B6401A743CF0Q37635836-8DD345E3-A2ED-4D9F-9339-8641F44DF8BEQ38156707-76712101-544B-4A58-9CC9-9E7050AD62ABQ38459352-81CC4A90-33DE-40C4-8FF8-ACD14A2BE41DQ38572149-65DD61BF-BDB5-4EA5-A7FF-7D00A343DCBDQ38910073-1A281445-8CBD-4D0F-89E0-210062CAB082Q39256380-8C2390D2-610D-4AD2-BA18-82C6CEC02698Q40514610-83DCFD06-1678-4AF0-96DD-63E7BC5B4DA4Q40715444-E8B07EA5-2802-4300-A40B-C3E7C4E8E4ABQ41029065-C2D130F8-2FB8-41FC-BE35-DCDF71F1C589Q41561104-64618F10-6B8D-4ECD-8371-46FC55831C6BQ41960802-CE77470D-EA4F-4151-BE84-88EE68B38679Q42050878-71E4E18F-C0D8-4ECA-939A-7D34B35BB413Q42736188-2E4F14AE-B004-4923-B687-1DE978F5BCD5Q44413942-E6AE5D3B-84E3-4DC8-8F53-18137313A9DAQ47936599-209B491C-155E-4976-A6AC-E92EB56C6695Q48212809-7B508FE4-E744-4CC0-86B2-5B7780C96A0FQ54263681-C749ABB8-9906-46B9-B800-D31F8598E140Q58231183-839C4CF9-682C-46EE-AF63-E3A70D77BA73
P2860
description
2010 nî lūn-bûn
@nan
2010 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի օգոստոսին 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
Structural basis of Fic-mediated adenylylation
@ast
Structural basis of Fic-mediated adenylylation
@en
Structural basis of Fic-mediated adenylylation
@nl
type
label
Structural basis of Fic-mediated adenylylation
@ast
Structural basis of Fic-mediated adenylylation
@en
Structural basis of Fic-mediated adenylylation
@nl
prefLabel
Structural basis of Fic-mediated adenylylation
@ast
Structural basis of Fic-mediated adenylylation
@en
Structural basis of Fic-mediated adenylylation
@nl
P2093
P2860
P3181
P356
P1476
Structural basis of Fic-mediated adenylylation
@en
P2093
Carolyn A Worby
Jack E Dixon
Junyu Xiao
Seema Mattoo
P2860
P2888
P304
P3181
P356
10.1038/NSMB.1867
P577
2010-08-01T00:00:00Z
P5875
P6179
1030381079