Design of O -Acetylserine Sulfhydrylase Inhibitors by Mimicking Nature - Test2 - elhamkhani - TriplyDB

Design of O -Acetylserine Sulfhydrylase Inhibitors by Mimicking Nature

Design of O -Acetylserine Sulfhydrylase Inhibitors by Mimicking Nature

http://www.wikidata.org/entity/Q27658287

about

Moonlighting O-acetylserine sulfhydrylase: New functions for an old protein Structure ofLeishmania majorcysteine synthase The narrow active-site cleft of O-acetylserine sulfhydrylase from Leishmania donovani allows complex formation with serine acetyltransferases with a range of C-terminal sequences From protein structure to function via single crystal optical spectroscopy Identification of natural inhibitors of Entamoeba histolytica cysteine synthase from microbial secondary metabolites Comparative thermodynamic studies on substrate and product binding of O-acetylserine sulfhydrylase reveals two different ligand recognition modes Isozyme-specific ligands for O-acetylserine sulfhydrylase, a novel antibiotic target Targeting cystalysin, a virulence factor of treponema denticola-supported periodontitis.Three-stage assembly of the cysteine synthase complex from Escherichia coli Identification of a target cell permissive factor required for contact-dependent growth inhibition (CDI).Structural insight into the interaction of O-acetylserine sulfhydrylase with competitive, peptidic inhibitors by saturation transfer difference-NMR.Unraveling the essential role of CysK in CDI toxin activation.Computational Insights into the Mechanism of Inhibition of OASS-A by a Small Molecule Inhibitor.Chemogenomics of pyridoxal 5'-phosphate dependent enzymes.Activation of an anti-bacterial toxin by the biosynthetic enzyme CysK: mechanism of binding, interaction specificity and competition with cysteine synthase.Ergot alkaloids: From witchcraft till in silico analysis. Multi-receptor analysis of ergotamine metabolites.ATP binding to human serine racemase is cooperative and modulated by glycine.Modulation of Escherichia coli serine acetyltransferase catalytic activity in the cysteine synthase complex.Cyclopropane-1,2-dicarboxylic acids as new tools for the biophysical investigation of O-acetylserine sulfhydrylases by fluorimetric methods and saturation transfer difference (STD) NMR.Regulation of human serine racemase activity and dynamics by halides, ATP and malonate Design and synthesis of trans-2-substituted-cyclopropane-1-carboxylic acids as the first non-natural small molecule inhibitors of O-acetylserine sulfhydrylase Refining the structure-activity relationships of 2-phenylcyclopropane carboxylic acids as inhibitors of O-acetylserine sulfhydrylase isoforms Inhibition of O-acetylserine sulfhydrylase by fluoroalanine derivatives Discovery of novel fragments inhibiting O-acetylserine sulphhydrylase by combining scaffold hopping and ligand-based drug design

P2860

Q27026625-695A8D84-09DC-4C83-9C73-B9A83BC8893D Q27670578-2F17A320-1960-4316-9812-2712DA191CAA Q27681897-F111CA88-867C-4149-B143-220D24354340 Q28084584-0FFB5E04-432B-4DAC-AE95-D0506F7BE1CC Q30387417-05F72853-828C-464F-B5C8-9B09070B5137 Q33919255-C1F863E7-33F4-43E5-865C-D9192F1E46E5 Q35027753-A2A4C5AE-8004-4F94-A915-1B9E4EA12055 Q35116929-4F257D49-4D3B-4B2E-8D94-03CCC1E1FE16 Q35763233-1A1F9A3C-00F1-46F6-9D9F-F8DD9031059B Q35835231-B23C1F54-7D58-478B-99E4-65A1241692F8 Q35987690-32147359-8C84-499C-9731-F8035C44355F Q37258599-E476FB9B-EBF4-4C8F-9F60-D3E9DCC075E5 Q39535345-BE988AF9-75AF-434C-A791-A6E168A76805 Q39674260-72CF9852-BE54-46C1-88F3-A526D37E555A Q41460284-42074D17-1221-4A78-B76E-81F943B9AC4F Q41680386-0E3ED300-D9AB-4A03-8216-FCAFB6FBCDF6 Q44066212-C5DE6E55-1125-4ED0-89F6-436FBD16AF22 Q46666237-07B0F4B5-3D60-470E-A33B-5554B9BB4248 Q49962224-9FB86AE1-2295-4014-A5B8-2F0265FC375C Q53407738-864AB71A-5079-45DB-A794-C186B7F87DE7 Q53408060-D51A625B-06DB-4BF3-B17E-D1E5EC31D759 Q58539530-47FC87DE-E377-4CF7-95FB-4FBE6D80CC6E Q58700160-F8250A90-CB10-4F1B-93D7-285AF98055D4 Q58732049-3FA158AC-1E82-43BE-B864-4014354244F8

P2860

Design of O -Acetylserine Sulfhydrylase Inhibitors by Mimicking Nature

http://www.wikidata.org/entity/Q27658287

description

2010 nî lūn-bûn

@nan

2010 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հունվարին 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

Design of O -Acetylserine Sulfhydrylase Inhibitors by Mimicking Nature

@ast

Design of O -Acetylserine Sulfhydrylase Inhibitors by Mimicking Nature

@en

Design of O -Acetylserine Sulfhydrylase Inhibitors by Mimicking Nature

@nl

type

label

Design of O -Acetylserine Sulfhydrylase Inhibitors by Mimicking Nature

@ast

Design of O -Acetylserine Sulfhydrylase Inhibitors by Mimicking Nature

@en

Design of O -Acetylserine Sulfhydrylase Inhibitors by Mimicking Nature

@nl

prefLabel

Design of O -Acetylserine Sulfhydrylase Inhibitors by Mimicking Nature

@ast

Design of O -Acetylserine Sulfhydrylase Inhibitors by Mimicking Nature

@en

Design of O -Acetylserine Sulfhydrylase Inhibitors by Mimicking Nature

@nl

P1433

Q27658287-9EFA5164-CAF6-4244-BE6E-87C194E3B4F0

P1476

Q27658287-F003F30D-D89B-4F27-8B90-55178EE81C51

P2093

Q27658287-22770C27-FBC1-4E86-BA37-0622A49D9091

Q27658287-2978BEA2-789A-47FC-8C18-1FD22638C628

Q27658287-2BEDA115-D1C0-4700-A1F7-F39C4D302BD9

Q27658287-7D3E1440-7D0A-4698-AFE6-FE7AEC7C2A13

Q27658287-8BE60F3C-19AA-493F-91F3-D4BA8662CFA6

Q27658287-9DE1CCE8-1EA4-42C7-AF20-B7B36E42B705

Q27658287-B95DEB36-E41A-4CCA-A383-CA4A4A7832CC

Q27658287-FA289881-C2DB-48D4-A0F0-0A6C1292CD9C

P2860

Q27658287-02DC3D1D-144B-4C45-8B89-B2F24297C82E

Q27658287-02E0892F-2E06-4A24-962B-2A6726B0B0F3

Q27658287-055DB1F1-9149-47FA-BDBC-06EF482526A5

Q27658287-0A3631E0-F6C6-40DF-9277-B243B89E7F60

Q27658287-0AC91E28-09C7-4F72-96C7-1D3C6D2AC866

Q27658287-0B86A0FF-0EBE-4EE4-A790-4F8BCA8E1C16

Q27658287-0C025CC4-198F-4516-BF49-981A0D17BBE8

Q27658287-0C5E1B00-1C37-48AA-82C2-56E1019D9156

Q27658287-0DCDC2D5-23FD-4F12-8A75-B203E29463C1

Q27658287-10021873-1C66-4F0F-8404-085D48D8792E

P304

Q27658287-B2F73B0F-CAEB-4F02-A3D6-5F6E1181621B

P31

Q27658287-A63F9B49-8CA6-421B-9F96-113321555F73

P356

Q27658287-222E52B8-4273-4D25-8A6C-33E8CEF88473

P407

Q27658287-CF005ACE-F783-4989-A1A5-37ACFDEBD82E

P433

Q27658287-F210AAD4-9411-4D1C-B318-CDA0A041184E

P478

Q27658287-15747CDF-523D-493B-B8B2-664DE7D722B4

P50

Q27658287-6B98E4C7-ED7D-43EE-AB06-55A68E321777

Q27658287-C1F1A484-8090-436A-9378-F2CDD8413D39

Q27658287-DEE13D31-B8E7-49F7-B4AD-89C71506F71B

Q27658287-E9AF8061-46BC-4AE3-A026-98454906B746

P577

Q27658287-83726CF2-E867-473E-86A6-5323553EA636

P5875

Q27658287-08CCFEF8-328D-4109-9074-363FF9CB07DB

P698

Q27658287-723E8783-E325-4607-AAB5-9BF92C38425A

P921

Q27658287-172581B5-6541-4381-B625-B157658307C0

P932

Q27658287-BFBB2937-8EAB-4050-A580-591FFAF615F1

P356

P1433

Journal of Medicinal Chemistry

P1476

Design of O -Acetylserine Sulfhydrylase Inhibitors by Mimicking Nature

@en

P2093

Alessio Amadasi

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

Alexander S Bayden

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

Barbara Campanini

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

Enea Salsi

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

Paul F Cook

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

Pietro Cozzini

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

Steven L Roderick

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

Tetyana Dodatko

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

P2860

A global view of Staphylococcus aureus whole genome expression upon internalization in human epithelial cells

Multidrug resistance in bacteria

Ligand binding induces a large conformational change in O-acetylserine sulfhydrylase from Salmonella typhimurium

Structural Basis for Interaction of O-Acetylserine Sulfhydrylase and Serine Acetyltransferase in the Arabidopsis Cysteine Synthase Complex

Structural insights into catalysis and inhibition of O-acetylserine sulfhydrylase from Mycobacterium tuberculosis. Crystal structures of the enzyme alpha-aminoacrylate intermediate and an enzyme-inhibitor complex

Cysteine synthase (CysM) of Mycobacterium tuberculosis is an O-phosphoserine sulfhydrylase: evidence for an alternative cysteine biosynthesis pathway in mycobacteria

The C-terminal of CysM from Mycobacterium tuberculosis protects the aminoacrylate intermediate and is involved in sulfur donor selectivity

Three-dimensional structure of O-acetylserine sulfhydrylase from Salmonella typhimurium

Coot: model-building tools for molecular graphics

Refinement of macromolecular structures by the maximum-likelihood method

P304

345-56

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

P31

scholarly article

P356

10.1021/JM901325E

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

P407

P433

1

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

P478

53

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

P50

Andrea Mozzarelli

Stefano Bettati

Glen E. Kellogg

Francesca Spyrakis

P577

2010-01-14T00:00:00Z

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

P5875

40022343

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

P698

19928859

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

P921

P932

2804909

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