Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase - Test2 - elhamkhani - TriplyDB

Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase

Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase

http://www.wikidata.org/entity/Q27617878

about

Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-phosphate-dependent heme protein Cofactor mobility determines reaction outcome in the IMPDH and GMPR (β-α)8 barrel enzymes Bateman domains and adenosine derivatives form a binding contract CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations IMP dehydrogenase: structure, mechanism, and inhibition.IMP dehydrogenase type 1 associates with polyribosomes translating rhodopsin mRNA Intrasteric control of AMPK via the gamma1 subunit AMP allosteric regulatory site A regulatory role of the Bateman domain of IMP dehydrogenase in adenylate nucleotide biosynthesis Mutations in the inosine monophosphate dehydrogenase 1 gene (IMPDH1) cause the RP10 form of autosomal dominant retinitis pigmentosa.Identification of novel Mt-Guab2 inhibitor series active against M. tuberculosis Different characteristics and nucleotide binding properties of inosine monophosphate dehydrogenase (IMPDH) isoforms Crystal structure of Tritrichomonas foetus inosine monophosphate dehydrogenase in complex with the inhibitor ribavirin monophosphate reveals a catalysis-dependent ion-binding site Essential but not vulnerable: indazole sulfonamides targeting inosine monophosphate dehydrogenase as potential leads against Mycobacterium tuberculosis Biochemical and Structural Characterization of a Novel Family of Cystathionine β-Synthase Domain Proteins Fused to a Zn Ribbon-Like Domain Bacillus anthracis Inosine 5′-Monophosphate Dehydrogenase in Action: The First Bacterial Series of Structures of Phosphate Ion-, Substrate-, and Product-Bound Complexes Single Cystathionine -Synthase Domain-Containing Proteins Modulate Development by Regulating the Thioredoxin System in Arabidopsis Structure ofPseudomonas aeruginosainosine 5′-monophosphate dehydrogenase Increased riboflavin production by manipulation of inosine 5'-monophosphate dehydrogenase in Ashbya gossypii CBS domains: structure, function, and pathology in human proteins Triazole-linked inhibitors of inosine monophosphate dehydrogenase from human and Mycobacterium tuberculosis Two classes of bacterial IMPDHs according to their quaternary structures and catalytic properties Proteomic analysis of carbon concentrating chemolithotrophic bacteria Serratia sp. for sequestration of carbon dioxide The antibiotic potential of prokaryotic IMP dehydrogenase inhibitors Structural determinants of inhibitor selectivity in prokaryotic IMP dehydrogenases.Genetic complementation in apicomplexan parasites A cytoplasmic domain mutation in ClC-Kb affects long-distance communication across the membrane Purification, crystallization and preliminary crystallographic analysis of protein MJ1225 from Methanocaldococcus jannaschii, a putative archaeal homologue of gamma-AMPK IMP dehydrogenase from the protozoan parasite Toxoplasma gondii.The role of IMP dehydrogenase 2 in Inauhzin-induced ribosomal stress.Regulation of the muscle-specific AMP-activated protein kinase alpha2beta2gamma3 complexes by AMP and implications of the mutations in the gamma3-subunit for the AMP dependence of the enzyme.Regulation of the phototrophic iron oxidation (pio) genes in Rhodopseudomonas palustris TIE-1 is mediated by the global regulator, FixK.Binding of ATP to the CBS domains in the C-terminal region of CLC-1.A sensor for intracellular ionic strength.A novel cofactor-binding mode in bacterial IMP dehydrogenases explains inhibitor selectivity.A two-holed story: structural secrets about ClC proteins become unraveled?Guanine nucleotide binding to the Bateman domain mediates the allosteric inhibition of eukaryotic IMP dehydrogenases.Identification of Pathogenicity-Related Genes in Biofilm-Defective Acidovorax citrulli by Transposon Tn5 Mutagenesis The muscle chloride channel ClC-1 is not directly regulated by intracellular ATP Protein surface analysis for function annotation in high-throughput structural genomics pipeline.The CBS subdomain of inosine 5'-monophosphate dehydrogenase regulates purine nucleotide turnover.

P2860

Q24291509-64C7B685-8F08-4427-90F1-EA97FE771CDB Q24294954-E1E85E3F-947A-44C2-AD75-BFFD1DC84C6F Q24614437-513400C4-200F-437B-8DCB-2A3E7F5DB3C2 Q24614590-094AAFD6-59A8-4FDA-96A9-019BA0B138B4 Q24642299-21FC0A3D-9072-4A29-809A-D1AE112E111D Q24643480-1260DC8C-A424-497B-B2A0-D5A01964F503 Q24645338-D4C412F4-0CF8-447A-B31B-23CA2004DE76 Q24655404-AA510B98-58E5-4EB7-BE9D-459E0C2EE0F9 Q24655474-73F962BA-CCDB-457B-9468-26A814ACD1E0 Q27306024-A86B85F9-8D68-49BA-8936-553C02C8C635 Q27332315-148FD5A2-D810-492E-8608-BEE601474CB6 Q27639659-ACB692CC-D15A-4824-8B53-B1F088B756D9 Q27644255-5E9785F8-023D-44D6-ADD8-E38EBB4AA0FC Q27649089-C2AA11C6-77F3-4569-AC97-ABD7950EBC6D Q27670715-3835CCA8-A546-4717-8EB3-4360FEA3E583 Q27675186-1B6FBFC4-955C-4E3B-AF69-03C715DFB934 Q27676976-9593E0B4-0FC5-4BD6-BAF5-EB98A7E15BE5 Q27701531-70265EB1-3331-496B-AD92-AB3A9A8749A8 Q28280884-8DA50ED4-33C1-45AF-9B2D-8B80E210C720 Q28486568-7DB92A33-0C92-4A0D-9E60-9BAA1047D02D Q28543579-B2AA702F-78F0-4DD3-B530-EC79D836C919 Q28657907-C048613E-5303-439E-A640-73D7C9903929 Q30356398-34A8DE91-649C-4D7D-B2B6-55F0422A19D6 Q30430133-D3F729D4-02F4-4B6D-9D06-B480532DE8CB Q30701283-82CAACFC-7502-4A39-BD36-EB0901EABA54 Q30845345-305E34B6-A1CE-4F51-AE30-7E60CB4B808E Q33490081-13491A78-1324-4BBD-88DA-CF14480F2699 Q33836711-041130DF-B9BD-445F-A1C1-B09BDD202F25 Q34404155-F3CB32B3-37EF-446E-94A8-B056C57D0258 Q34630778-EE14BB6B-82AD-44EB-8910-A25150F5B4EA Q34632437-2F031095-F4A0-43DC-9048-7153AC0C2D68 Q34744998-851E2DD8-C3EC-410F-A1E9-740F99CCB86F Q34771039-494EB8A7-4757-4B57-81BF-89C40BF2578F Q35126722-A917F17A-818D-4767-8BA0-1E018A72269D Q35894413-EC5D7E00-AA15-436E-A037-2091DB2E9C91 Q36320750-3DB012B2-655F-4EF9-809D-628687F7292E Q36403911-57F9BE92-F294-4A08-BB5B-01A8CD80E1B8 Q36404795-A65D1F7D-F60F-442D-ABDB-55FDDE259F1D Q36476631-692F8289-5262-4C6D-998C-E4A5BD145F30 Q36517922-6AFCE36D-85BB-4DC7-B4B0-BB77450291A8

P2860

Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase

http://www.wikidata.org/entity/Q27617878

description

1999 nî lūn-bûn

@nan

1999 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

1999 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

1999年の論文

@ja

1999年論文

@yue

1999年論文

@zh-hant

1999年論文

@zh-hk

1999年論文

@zh-mo

1999年論文

@zh-tw

1999年论文

@wuu

name

Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase

@ast

Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase

@en

Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase

@nl

type

label

Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase

@ast

Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase

@en

Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase

@nl

prefLabel

Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase

@ast

Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase

@en

Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase

@nl

P1433

Q27617878-7DA729C8-EE04-4C42-9559-579CE4ED692F

P1476

Q27617878-784D3AF7-BBB4-4613-8FCD-4CAB66C458B0

P2093

Q27617878-2DAF4296-B8BC-4A7B-A1A0-A8659694B778

Q27617878-342011E0-7857-45C0-8261-22EBFBF724E1

Q27617878-43407F73-A900-4D28-BC59-341716DF0EDA

Q27617878-BF436467-6768-4500-867B-2378E113CD4E

Q27617878-DA13A280-4125-41B2-87AB-0E24C33E3B9F

Q27617878-E64ED550-C471-4BFC-9C03-891D12F5AF79

Q27617878-FBBF3FC5-B7A8-4689-B303-FB8C796E64F2

Q27617878-FF21CC90-5849-413A-8D5B-0073CAEDC2D5

P304

Q27617878-0AC1F587-AEAF-4EA3-9C3E-6DE81F7E5B11

P31

Q27617878-2170D226-5C8D-4AF9-8B0D-6D34CEF02B74

P3181

Q27617878-8CC10DE3-CD56-4D6B-9327-6A4F92F8B563

P356

Q27617878-D19D4D02-2871-454D-8A7A-AE8585D96264

P407

Q27617878-BD2D4783-04CE-433B-BB16-AC6FE8560EA6

P433

Q27617878-3B2E1D02-F0E9-46CC-822E-C5C3CEE685D5

P478

Q27617878-8F813479-5392-4D91-9617-8AADF4FE7F9B

P577

Q27617878-22DDF5A2-0008-42E2-A330-3AEB284A590F

P5875

Q27617878-9864C58A-53E7-4714-A7C9-1215D466F590

P698

Q27617878-59D615DE-A718-4DAD-874E-403B8623163A

P921

Q27617878-6D9808F3-1580-450C-BFC4-3D08C232A020

P3181

P356

P1433

P1476

Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase

@en

P2093

A Joachimiak

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

D Beno

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

E Huberman

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

E M Westbrook

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

F J Rotella

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

F R Collart

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

G Evans

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

R Zhang

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

P304

4691-700

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

P31

scholarly article

P3181

247894

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

P356

10.1021/BI982858V

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

P407

P433

15

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

P478

38

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

P577

1999-04-13T00:00:00Z

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

P5875

13098376

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

P698

10200156

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

P921

crystal structure