Structural studies examining the substrate specificity profiles of PC-PLCBc protein variants - Wikidata - wikimedia - TriplyDB

Structural studies examining the substrate specificity profiles of PC-PLCBc protein variants

Structural studies examining the substrate specificity profiles of PC-PLCBc protein variants

http://www.wikidata.org/entity/Q27643912

about

Plant multifunctional nuclease TBN1 with unexpected phospholipase activity: structural study and reaction-mechanism analysis Requirements for transitional endoplasmic reticulum site structure and function in Saccharomyces cerevisiae A quantitative continuous enzyme assay of intramolecularly quenched fluorogenic phospholipase substrates for molecular imaging.Recent research progress with phospholipase C from Bacillus cereus.Design and synthesis of phospholipase C and A2-activatable near-infrared fluorescent smart probes.The Legionella pneumophila Dot/Icm-secreted effector PlcC/CegC1 together with PlcA and PlcB promotes virulence and belongs to a novel zinc metallophospholipase C family present in bacteria and fungi.In vitro analysis of the Staphylococcus aureus lipoteichoic acid synthase enzyme using fluorescently labeled lipids.

P2860

Q27683939-E812A092-9D20-4B55-A768-2A81D3BE669B Q30494268-68E8AD1A-133E-45DA-B4A9-82E67E2BF62C Q36482220-689D4765-3E15-4614-9E52-65368289CFB3 Q38599549-682536A5-FAC4-444C-9680-4D8585AA1A07 Q39832315-86E4F792-8387-45F1-AE9E-174583DB0BF9 Q39959076-9AF3EFF7-3213-4AEA-A546-2CA63344F5EB Q41957315-654907BC-C805-4881-9E4E-D4806490AB13

P2860

Structural studies examining the substrate specificity profiles of PC-PLCBc protein variants

http://www.wikidata.org/entity/Q27643912

description

2007 nî lūn-bûn

@nan

2007 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2007年の論文

@ja

2007年論文

@yue

2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

@wuu

name

Structural studies examining t ...... s of PC-PLCBc protein variants

@ast

Structural studies examining t ...... s of PC-PLCBc protein variants

@en

Structural studies examining t ...... s of PC-PLCBc protein variants

@nl

type

label

Structural studies examining t ...... s of PC-PLCBc protein variants

@ast

Structural studies examining t ...... s of PC-PLCBc protein variants

@en

Structural studies examining t ...... s of PC-PLCBc protein variants

@nl

prefLabel

Structural studies examining t ...... s of PC-PLCBc protein variants

@ast

Structural studies examining t ...... s of PC-PLCBc protein variants

@en

Structural studies examining t ...... s of PC-PLCBc protein variants

@nl

P1433

Q27643912-0A245051-A4FB-4262-BB8A-6BA56FED783A

P1476

Q27643912-196EFA07-88D6-49FE-8B49-FA2C46FE63AE

P2093

Q27643912-05081E78-28A0-4FE9-AC2F-A4B0A38796A6

Q27643912-32F01D94-B667-40DC-B0D7-07B7626C0F73

Q27643912-E2CBFE21-E177-45BC-B103-245F573900E7

Q27643912-F4F4E67A-EC12-479A-B9CF-993ADA0661B7

P2860

Q27643912-07119328-83D9-4A9D-88B3-917159175186

Q27643912-0766D015-36EC-4F2A-8684-C46A13805BB1

Q27643912-251B3AAE-E0F6-4D50-9CAC-039BA32DA6BF

Q27643912-3061DB74-65A7-43A3-9FEB-E6648EC043F9

Q27643912-36AC33D4-3824-43FE-BB3E-B1146FEAC6C0

Q27643912-48A58B44-CE8A-4F75-AD61-8C96B56ECBE7

Q27643912-6191E467-9DBD-4773-ACF7-5C905A4BA93B

Q27643912-70C480BD-BA72-4AF0-A7B3-3873F25676E8

Q27643912-723E1192-E376-4239-ACCF-C1847F894BE5

Q27643912-73E9C793-884E-4755-B6DC-B118C8FD87B8

P304

Q27643912-5CBEF2C8-11D8-4F3A-99B3-799A14908C3F

P31

Q27643912-4C4BA607-7493-44C0-BF5C-2834B1F64814

P356

Q27643912-8EEE654A-8554-4474-A355-8D0AB50EBF13

P407

Q27643912-FD675C2A-8B22-486C-A702-557A7EED2B85

P433

Q27643912-EFAD280E-136F-4FDA-AF25-C3BC121599DD

P478

Q27643912-CA64E64C-66ED-4DC9-9756-45C486FFEC57

P577

Q27643912-C6928F2E-3CA1-41C7-8EB6-02F867F47E71

P5875

Q27643912-DD5A2479-DE41-454F-B5EC-A303E5BAFCFB

P698

Q27643912-BF155BA0-8E7B-4181-8BFC-3C3DD32577DB

P921

Q27643912-8822776B-2258-4424-8F81-E2A6407A01F4

P932

Q27643912-496D4B6A-377E-4F06-8C9E-0DD3B9CDAF6B

P356

J.ABB.2007.01.023

P1433

Archives of Biochemistry and Biophysics

P1476

Structural studies examining t ...... s of PC-PLCBc protein variants

@en

P2093

Aaron P Benfield

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

Lauren T Phillips

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

Nina M Goodey

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

Stephen F Martin

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

P2860

Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

High-resolution (1.5 A) crystal structure of phospholipase C from Bacillus cereus

The CCP4 suite: programs for protein crystallography

Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein

Cation-pi interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp

Altering substrate specificity of phosphatidylcholine-preferring phospholipase C of Bacillus cereus by random mutagenesis of the headgroup binding site.

Weakly polar interactions in proteins.

Cation-pi bonding and amino-aromatic interactions in the biomolecular recognition of substituted ammonium ligands.

P304

41-7

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

P31

scholarly article

P356

10.1016/J.ABB.2007.01.023

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

P407

P433

1

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

P478

460

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

P577

2007-04-01T00:00:00Z

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

P5875

6482774

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

P698

17324372

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

P921

P932

1905842

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