Redox regulation by reversible protein S-thiolation in bacteria - Test2 - elhamkhani - TriplyDB

Redox regulation by reversible protein S-thiolation in bacteria

Redox regulation by reversible protein S-thiolation in bacteria

http://www.wikidata.org/entity/Q28083854

about

Adaptation in Bacillus cereus: From Stress to Disease Biological and Chemical Adaptation to Endogenous Hydrogen Peroxide Production in Streptococcus pneumoniae D39 Real-Time Imaging of the Bacillithiol Redox Potential in the Human Pathogen Staphylococcus aureus Using a Genetically Encoded Bacilliredoxin-Fused Redox Biosensor Ecology of cold environments: new insights of bacterial metabolic adaptation through an integrated genomic-phenomic approach Glutathionylation of Yersinia pestis LcrV and Its Effects on Plague Pathogenesis European contribution to the study of ROS: A summary of the findings and prospects for the future from the COST action BM1203 (EU-ROS).Regulatory potential of post-translational modifications in bacteria.Myrosinase-dependent and -independent formation and control of isothiocyanate products of glucosinolate hydrolysis Conferring specificity in redox pathways by enzymatic thiol/disulfide exchange reactions.Measurement and meaning of cellular thiol:disufhide redox status.Activity of the Pore-Forming Virulence Factor Listeriolysin O Is Reversibly Inhibited by Naturally Occurring S-Glutathionylation.The Role of Bacillithiol in Gram-Positive Firmicutes.Neutrophil-generated oxidative stress and protein damage in Staphylococcus aureus.Investigation on the antimicrobial activities of gingers (Etlingera coccinea (Blume) S.Sakai & Nagam and Etlingera sessilanthera R.M.Sm.) endemic to Borneo.Repurposing Thiram and Disulfiram as Antibacterial Agents for Multidrug-Resistant Staphylococcus aureus Infections.The glyceraldehyde-3-phosphate dehydrogenase GapDH of Corynebacterium diphtheriae is redox-controlled by protein S-mycothiolation under oxidative stress.Purification and Characterization of an ATPase GsiA from Salmonella enterica Monitoring global protein thiol-oxidation and protein S-mycothiolation in Mycobacterium smegmatis under hypochlorite stress.Differential regulation of riboflavin supply genes in Vibrio cholerae.Adenosine Monophosphate Binding Stabilizes the KTN Domain of the Shewanella denitrificans Kef Potassium Efflux System.Allicin-inspired pyridyl disulfides as antimicrobial agents for multidrug-resistant Staphylococcus aureus.Protein Posttranslational Modifications: Roles in Aging and Age-Related Disease.Hydrogen Sulfide and Reactive Sulfur Species Impact Proteome S-Sulfhydration and Global Virulence Regulation in Staphylococcus aureus.The versatile low-molecular-weight thiols: Beyond cell protection.A two-step evolutionary process establishes a non-native vitamin B6 pathway in Bacillus subtilis.Redox Probing for Chemical Information of Oxidative Stress.Protein S-Bacillithiolation Functions in Thiol Protection and Redox Regulation of the Glyceraldehyde-3-Phosphate Dehydrogenase Gap in Staphylococcus aureus Under Hypochlorite Stress.Protein CoAlation and antioxidant function of Coenzyme A in prokaryotic cells.Host-pathogen redox dynamics modulate Mycobacterium tuberculosis pathogenesis.Sensory-Neuropathy-Causing Mutations in ATL3 Cause Aberrant ER Membrane Tethering.The enzyme activity of histone deacetylase 8 is modulated by a redox-switch Redox regulation by reversible protein S-thiolation in Gram-positive bacteria Thioredoxin Profiling of Multiple Thioredoxin-Like Proteins in Reduce, Induce, Thrive: Bacterial Redox Sensing during Pathogenesis Complete genome sequence of sp. PAMC21323 isolated from Antarctica and its metabolic potential to detoxify pollutants

P2860

Q28079646-F714C982-FB4C-480C-873E-343268112A3C Q28818040-6C669958-FA98-4203-A67B-5BD560A61AD8 Q30355543-D593BB8C-7187-4A00-8CCF-814CA762F068 Q33678319-11CDB849-221F-4E89-BDE6-7CD58A58F0BF Q33691879-D31C08F9-1A9D-4380-87DF-09AF8F10E475 Q33761211-DF80F411-2E46-4C63-914C-5E04B16B0C3C Q35659128-30B04204-CEEB-4662-AFA1-1AD842C4EB88 Q36123258-8E50FD8D-DC81-496E-8F72-B908A3947823 Q38634845-761721B5-09D3-4E65-8269-553B7902ECCA Q38676671-2F7E4313-F66F-411D-ACF5-63B9399E184F Q38718753-7C490260-59C7-4D61-A4B1-E0B3718A6687 Q38744009-EF59BE9F-978C-48CD-8371-CA6BF9266103 Q38847411-8F031A81-3F6D-4E87-9AEF-096727931B94 Q38961433-F3FAD2B6-13BB-4877-9FE6-737E3C7F6F72 Q40148525-3C95B24F-3DCC-47DD-8D0B-F3255CD58E23 Q40973989-97C59432-8AA3-45F5-918E-E68CB8F49DDE Q41038304-C9D6379D-136C-48BD-8916-CF5F4506F6D6 Q41891132-6B0CCECA-FDE6-4617-9766-2E849B38E6B9 Q42154475-DDB4556C-8426-4A75-8FC8-D1DF29575A7C Q42379820-AA67F005-97AA-47DF-86BB-665E840FB1CE Q45072648-CEC76C3C-BC54-45A3-8386-C46D5D5556B8 Q46064843-F68034BF-EB37-4F65-A65B-377440CAEEA7 Q46315067-90970E02-39A9-4390-A6D5-6D8F3D2F16CB Q46646737-9C61AD2A-FF36-4DA7-BB65-9807A66ABD62 Q47658955-89E1C54E-4BA7-4EBC-80ED-68BB3ACA26D4 Q47840287-4E2BD38E-525D-4D2C-82D5-48651EE258E0 Q50085241-7890C9E6-A125-495E-8D54-5362603C2AA4 Q52601655-774C5167-9761-495E-A6E8-618FF6158C5F Q55022151-EA101C01-B906-4B8F-B8F5-3F4261AA1083 Q55396745-5EF3B206-0194-451C-980E-BA28A0D0F86E Q57191113-095170E3-836A-48B1-978E-24E06EE1DBDE Q57300944-EE9461F7-7325-48FB-8631-841E6BC11149 Q58122118-FDA9185C-75F5-4D39-9956-1B1C1C4CF66C Q58790706-63DC6B24-7279-49DC-91E2-09FA3EFAED1F Q59130289-27BA5FD2-79DF-4195-9B98-5490512B6677

P2860

Redox regulation by reversible protein S-thiolation in bacteria

http://www.wikidata.org/entity/Q28083854

description

2015 nî lūn-bûn

@nan

2015 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2015 թվականի մարտին հրատարակված գիտական հոդված

@hy

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

name

Redox regulation by reversible protein S-thiolation in bacteria

@ast

Redox regulation by reversible protein S-thiolation in bacteria

@en

Redox regulation by reversible protein S-thiolation in bacteria

@nl

type

label

Redox regulation by reversible protein S-thiolation in bacteria

@ast

Redox regulation by reversible protein S-thiolation in bacteria

@en

Redox regulation by reversible protein S-thiolation in bacteria

@nl

prefLabel

Redox regulation by reversible protein S-thiolation in bacteria

@ast

Redox regulation by reversible protein S-thiolation in bacteria

@en

Redox regulation by reversible protein S-thiolation in bacteria

@nl

P1433

Q28083854-4F498536-FA9A-418A-8F03-41DABBE9966D

P1476

Q28083854-93D9C645-ACAF-465B-B9D8-1356D0C6DE66

P2093

Q28083854-6B6010BE-EA13-4FDB-802F-E7B99D4165DF

Q28083854-B05FC9AA-8B79-4D4A-B4D8-7255125FE9C9

P2860

Q28083854-0155E7A7-216B-43E0-BFAE-8EA6AB0D7C69

Q28083854-02EDDF15-7624-44F7-8B52-BE053BF63633

Q28083854-03105608-19AC-4691-8615-17056D0F2AE5

Q28083854-04B9DD97-CB4A-438C-A191-03E39508D244

Q28083854-04BFB9D0-A581-40A4-ADFD-BEA0B0ED89A4

Q28083854-0609DE01-F21D-489D-A523-72DFA6A943A9

Q28083854-062F8D43-667D-45B8-9710-0484C250918D

Q28083854-065CD560-15E1-4581-8B00-77E60BD73316

Q28083854-0CA444DE-6036-4E6E-85FD-78E179DF7AA5

Q28083854-0CCA0A56-5704-451E-82E3-A02ADBB91864

P304

Q28083854-54429330-8004-4556-90F3-68CCDB340DD8

P31

Q28083854-A675700B-3BFB-4A25-9E80-FA4C90C9476E

P3181

Q28083854-019548DA-5E74-43D1-A918-52DA3A383065

P356

Q28083854-28EA2C1E-2EA0-4C67-B0EC-991BBA709986

P407

Q28083854-75319142-AD05-42BD-8378-ED4A2EE5F5C2

P478

Q28083854-52CE0AAC-CE83-4BEB-9540-2812B6FE9FC5

P50

Q28083854-B36BDEF9-30CE-474B-80CE-FFE01D25D455

P577

Q28083854-1846CC2A-AA87-477E-963F-A0BF1B388AD3

P5875

Q28083854-D6F81DB4-FE20-478F-AD19-E48425F29878

P698

Q28083854-3AD4718E-9C50-42E6-9E32-4BBF1A40F65C

P932

Q28083854-883E15A4-A86F-4806-80C3-9CDE00DCCFBE

P3181

P356

FMICB.2015.00187

P1433

Frontiers in Microbiology

P1476

Redox regulation by reversible protein S-thiolation in bacteria

@en

P2093

Martina Rossius

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

Vu Van Loi

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

P2860

Biosynthesis and functions of bacillithiol, a major low-molecular-weight thiol in Bacilli

Bacillithiol is an antioxidant thiol produced in Bacilli

Spx-RNA polymerase interaction and global transcriptional control during oxidative stress

Biosynthesis and functions of mycothiol, the unique protective thiol of Actinobacteria

Listeria monocytogenes - from saprophyte to intracellular pathogen

Oxidative stress inactivates cobalamin-independent methionine synthase (MetE) in Escherichia coli

Protein-thiol oxidation and cell death: regulatory role of glutaredoxins

Bacterial responses to reactive chlorine species

Advances in the function and regulation of hydrogenase in the cyanobacterium Synechocystis PCC6803

Crystal structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558

P304

187

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

P31

scholarly article

P3181

3149984

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

P356

10.3389/FMICB.2015.00187

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

P407

P478

6

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

P50

Haike Antelmann

P577

2015-03-16T00:00:00Z

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

P5875

272679075

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

P698

25852656

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

P932

4360819

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