Rifamycin antibiotic resistance by ADP-ribosylation: Structure and diversity of Arr - Wikidata - wikimedia - TriplyDB

Rifamycin antibiotic resistance by ADP-ribosylation: Structure and diversity of Arr

Rifamycin antibiotic resistance by ADP-ribosylation: Structure and diversity of Arr

http://www.wikidata.org/entity/Q27650104

about

The Mycobacterium tuberculosis drugome and its polypharmacological implications Use of Mycobacterium smegmatis deficient in ADP-ribosyltransferase as surrogate for Mycobacterium tuberculosis in drug testing and mutation analysis Origins and evolution of antibiotic resistance Wide variation in antibiotic resistance proteins identified by functional metagenomic screening of a soil DNA library.Identification of novel components of NAD-utilizing metabolic pathways and prediction of their biochemical functions.New Insights in to the Intrinsic and Acquired Drug Resistance Mechanisms in Mycobacteria Rifabutin Is Active against Mycobacterium abscessus Complex.Catalytic and non-catalytic roles for the mono-ADP-ribosyltransferase Arr in the mycobacterial DNA damage response.ADP-ribosylation of arginine.Multidrug efflux pumps from Enterobacteriaceae, Vibrio cholerae and Staphylococcus aureus bacterial food pathogens The natural history of ADP-ribosyltransferases and the ADP-ribosylation system.The initial state of the human gut microbiome determines its reshaping by antibiotics.Casein Kinase 2 (CK2)-mediated Phosphorylation of Hsp90β as a Novel Mechanism of Rifampin-induced MDR1 Expression Antimicrobial susceptibility testing, drug resistance mechanisms, and therapy of infections with nontuberculous mycobacteria.Characterization of a rifampin-inactivating glycosyltransferase from a screen of environmental actinomycetes.Study of the rifampin monoresistance mechanism in Mycobacterium tuberculosis.Structural basis of rifampin inactivation by rifampin phosphotransferase.Rifampin phosphotransferase is an unusual antibiotic resistance kinase A temporal proteome dynamics study reveals the molecular basis of induced phenotypic resistance in Mycobacterium smegmatis at sub-lethal rifampicin concentrations Pyrazinamide: the importance of uncovering the mechanisms of action in mycobacteria.Control of Multidrug-Resistant Gene Flow in the Environment Through Bacteriophage Intervention.Intrinsic rifamycin resistance of Mycobacterium abscessus is mediated by ADP-ribosyltransferase MAB_0591.The Structure of the Antibiotic Deactivating, N-hydroxylating Rifampicin Monooxygenase.Going Beyond Common Drug Metabolizing Enzymes: Case Studies of Biotransformation Involving Aldehyde Oxidase, γ-Glutamyl Transpeptidase, Cathepsin B, Flavin-Containing Monooxygenase, and ADP-Ribosyltransferase.Species specific interactions of Arr with RplK mediate stringent response in bacteria.Arr-cb Is a Rifampin Resistance Determinant Found Active or Cryptic in Clostridium bolteae Strains.Insights into the biogenesis, function, and regulation of ADP-ribosylation.Disruption of SCO5461 gene coding for a mono-ADP-ribosyltransferase enzyme produces a conditional pleiotropic phenotype affecting morphological differentiation and antibiotic production in Streptomyces coelicolor.Tetracycline-Inactivating Enzymes.Redetermination of rifampicin pentahydrate revealing a zwitterionic form of the antibiotic Integrative metagenomic and biochemical studies on rifamycin ADP-ribosyltransferases discovered in the sediment microbiome

P2860

Q28476004-F307273D-CB42-4A9F-B12F-63B9F7B20AEB Q28546190-212876FA-0D6B-4E4A-B488-E5B6B646BF48 Q29617791-BBEB0647-1E0F-4276-B50D-072F630F177F Q30411789-6A69FDEC-5D6A-40D2-9858-53BCE117FE6F Q31049613-B85347C0-DD82-4C29-BF8D-FE8BDE171415 Q33600161-3D1A4DD6-2548-4BDB-85B2-3212C3B0D170 Q33726686-D01B8451-F934-420B-9EC3-8B53355530C4 Q33971121-D73E5698-59C9-4C90-B66F-B87B4BB07350 Q34023226-7451BA50-826F-4402-8E41-8E9B4B73001A Q35131669-52130C9A-FCF1-4E71-ABB5-0EA2A901FE19 Q35207356-15333EAB-B6A2-46F2-B6A3-19D81BF6CC36 Q35770426-C9C69A93-B1E9-433C-A370-014C5749F2A9 Q35860589-15D87904-E400-4938-9BA3-444777E0BE64 Q36156072-AA561904-97D5-412A-A874-23771BBA14DD Q36276927-F4F03DF7-B947-4559-AF73-071EECA0543C Q36558506-9F99DFCE-0BF7-4D9C-9033-2AA35C54D0B3 Q36802479-E6E1A70C-FB7F-492F-9247-645119CF5B40 Q36834702-12F4BA2B-8EDA-4BBD-9737-F1C547BE1B21 Q37682241-5E849547-C086-4E5D-9502-C6615CC0270E Q38368943-598A7B2E-1C64-4206-B164-AFFB7AC251BF Q38976992-EDF561DF-B5EE-47E9-8191-B7A8782D90B2 Q39080590-C9C33538-EE94-4D31-B966-F2D7DB3EA52B Q42281328-0F5D0B59-0EEE-40C9-96B6-16B9B7CED536 Q46554332-501B2885-F435-4C79-882A-50A97D51E6BF Q47222956-3AC75962-E286-4F20-8318-3CA4E8D64FF8 Q49637022-1505D274-016F-4262-B658-AE875F0E8BAC Q50001563-A0ECE437-056A-4D74-A735-273F1DDD843C Q52627070-DA3464A5-5508-4C02-9208-3288F2498112 Q55082798-930F074C-4E6E-4EFF-9B37-907297F805B6 Q57587264-A0BA9B6D-0D20-4420-8C8C-49D89A382BCA Q58782968-E503BF20-2F60-4E34-8A73-C7FBA1C28846

P2860

Rifamycin antibiotic resistance by ADP-ribosylation: Structure and diversity of Arr

http://www.wikidata.org/entity/Q27650104

description

2008 nî lūn-bûn

@nan

2008 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի մարտին հրատարակված գիտական հոդված

@hy

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

name

Rifamycin antibiotic resistance by ADP-ribosylation: Structure and diversity of Arr

@ast

Rifamycin antibiotic resistance by ADP-ribosylation: Structure and diversity of Arr

@en

Rifamycin antibiotic resistance by ADP-ribosylation: Structure and diversity of Arr

@nl

type

label

Rifamycin antibiotic resistance by ADP-ribosylation: Structure and diversity of Arr

@ast

Rifamycin antibiotic resistance by ADP-ribosylation: Structure and diversity of Arr

@en

Rifamycin antibiotic resistance by ADP-ribosylation: Structure and diversity of Arr

@nl

prefLabel

Rifamycin antibiotic resistance by ADP-ribosylation: Structure and diversity of Arr

@ast

Rifamycin antibiotic resistance by ADP-ribosylation: Structure and diversity of Arr

@en

Rifamycin antibiotic resistance by ADP-ribosylation: Structure and diversity of Arr

@nl

P1433

Q27650104-AA674C61-FCBA-4D9B-8837-E097A61A817C

P1476

Q27650104-F57E8947-6A8D-49E7-8259-D739AB42AF7F

P2093

Q27650104-2FADACF8-603D-4160-BEB1-514C615FF315

Q27650104-364D48DE-52AD-4F7E-AB28-F8A4AE1E5AC2

Q27650104-6DDF8624-E637-4ED7-867B-C6F0D796E96D

Q27650104-7B941C1E-B08D-43AA-B9AE-423821703FA0

Q27650104-8B0F4267-F520-410B-85C2-35CE0BCBBE1E

Q27650104-CEFD1D17-A52C-4B7D-AFBB-A14DE99E4CF9

P2860

Q27650104-083D5E15-CDD9-4E0B-A7EB-D94BB05785D0

Q27650104-1839187E-32AF-4FE3-9136-4EBEC9324180

Q27650104-1D083FD3-7D6B-4801-BCCD-D0921BC06E11

Q27650104-1EA44EA5-FDF0-47C8-9829-A871702C7A9E

Q27650104-2A41B303-7477-4A25-9B55-0FE0236C94D5

Q27650104-2B8AE0C3-75E4-485C-8B74-2759D1145EBE

Q27650104-2F2FD60A-1221-4423-A163-A652E24E2FD2

Q27650104-3105B441-0C37-4752-8425-50BF805FCA78

Q27650104-423A3D01-0C87-4D5C-94E9-DDCB23F1D776

Q27650104-4AD9F404-0B0A-4342-8803-AF9F9CDB2F56

P304

Q27650104-8202469E-DED7-4E1D-A789-6FAFE935AF10

P31

Q27650104-F4AA690A-C063-40CB-90B6-F4EAB21C6AF7

P3181

Q27650104-6C730DB0-6DEF-4B10-A2F9-848A77FAF9E1

P356

Q27650104-A938A4B4-FC78-43A4-A1A8-7CB7FB288E54

P407

Q27650104-3F42BF3E-535B-4741-A8C7-C9DF9824D37F

P433

Q27650104-2C70B033-0736-466A-9E77-034652D89291

P478

Q27650104-DECC20AA-C72F-4943-9E7D-56C9A17B721F

P50

Q27650104-C5511854-2A37-43EE-A305-4B152FA20A2E

Q27650104-F2E00E33-9488-4CD3-8026-712A11345024

P577

Q27650104-A5EF606F-FC80-4C78-976D-C2DEA6FA5E26

P5875

Q27650104-31938B80-2C7D-4361-B478-D28EC8A0E177

P698

Q27650104-7F8F7093-1E6A-4AE1-9C0D-D86B1885127A

P921

Q27650104-2E18B3C9-ADD2-43EC-8D94-E2FED0BC1C16

P932

Q27650104-691DB828-4EAF-46C1-BD9B-44A4ED4FEDF3

P3181

P356

PNAS.0711939105

P1433

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

P1476

Rifamycin antibiotic resistance by ADP-ribosylation: Structure and diversity of Arr

@en

P2093

Donald W Hughes

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

Emma Griffiths

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

Jennifer Baysarowich

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

Kalinka Koteva

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

Kun Zhang

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

Linda Ejim

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

P2860

In silico characterization of the family of PARP-like poly(ADP-ribosyl)transferases (pARTs)

Crystal structure of an aminoglycoside 6'-N-acetyltransferase: defining the GCN5-related N-acetyltransferase superfamily fold

Crystal structure and novel recognition motif of rho ADP-ribosylating C3 exoenzyme from Clostridium botulinum: structural insights for recognition specificity and catalysis

Structural mechanism for rifampicin inhibition of bacterial rna polymerase

Structure of the ecto-ADP-ribosyl transferase ART2.2 from rat

Crystal structure and site-directed mutagenesis of enzymatic components from Clostridium perfringens iota-toxin

The three-dimensional crystal structure of cholera toxin

The crystal structure of pertussis toxin

Crystal structure of diphtheria toxin bound to nicotinamide adenine dinucleotide

Crystal structure of the catalytic domain of Pseudomonas exotoxin A complexed with a nicotinamide adenine dinucleotide analog: implications for the activation process and for ADP ribosylation

P304

4886-91

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

P31

scholarly article

P3181

2147196

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

P356

10.1073/PNAS.0711939105

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

P407

P433

12

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

P478

105

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

P50

Gerard D. Wright

P577

2008-03-25T00:00:00Z

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

P5875

5503614

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

P698

18349144

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

P921

antibiotic resistance

P932

2290778

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