Structure of a Calcium-dependent 11R-Lipoxygenase Suggests a Mechanism for Ca2+ Regulation - Wikidata - wikimedia - TriplyDB

Structure of a Calcium-dependent 11R-Lipoxygenase Suggests a Mechanism for Ca2+ Regulation

Structure of a Calcium-dependent 11R-Lipoxygenase Suggests a Mechanism for Ca2+ Regulation

http://www.wikidata.org/entity/Q27678989

about

The structure of human 15-lipoxygenase-2 with a substrate mimic A polycystin-centric view of cyst formation and disease: the polycystins revisited Structure and interaction with phospholipids of a prokaryotic lipoxygenase from Pseudomonas aeruginosa The structural basis for specificity in lipoxygenase catalysis.Crystal structure of a lipoxygenase in complex with substrate: the arachidonic acid-binding site of 8R-lipoxygenase.The Arabidopsis PLAT domain protein1 is critically involved in abiotic stress tolerance.A Catalase-related Hemoprotein in Coral Is Specialized for Synthesis of Short-chain Aldehydes: DISCOVERY OF P450-TYPE HYDROPEROXIDE LYASE ACTIVITY IN A CATALASE.Structural and Functional Analysis of Calcium Ion Mediated Binding of 5-Lipoxygenase to Nanodiscs Identification and Characterization of a New Protein Isoform of Human 5-Lipoxygenase Locating a lipid at the portal to the lipoxygenase active site Identification of the Substrate Access Portal of 5-Lipoxygenase The Polycystin-1, Lipoxygenase, and α-Toxin Domain Regulates Polycystin-1 Trafficking.5-Lipoxygenase-activating protein rescues activity of 5-lipoxygenase mutations that delay nuclear membrane association and disrupt product formation Industrial potential of lipoxygenases.Crystallization and preliminary crystallographic analysis of manganese lipoxygenase Crystal Structure of Manganese Lipoxygenase of the Rice Blast Fungus Magnaporthe oryzae.Hydrogen-deuterium exchange reveals long-range dynamical allostery in soybean lipoxygenase.Structural Dynamics of 15-Lipoxygenase-2 via Hydrogen-Deuterium Exchange.n-Hexanal and (Z)-3-hexenal are generated from arachidonic acid and linolenic acid by a lipoxygenase in Marchantia polymorpha L.

P2860

Q24329199-496A8460-3D5E-4EA9-8966-7F4A46513E3F Q26800974-809BCA9D-A453-4D95-87ED-1B37292F5D09 Q27679822-F7D0BA5C-BBD8-4614-B1CB-D1689B27232C Q30153264-00C478DA-C9EA-47E9-9D2C-9C6EC51BC275 Q30366916-21D897C6-939A-4732-AEC7-E7CCA7A06107 Q34514434-A7A206B3-714E-493C-9E07-AF935C39AD69 Q35671387-DCF4A2C5-ABE9-4EB9-AE2C-E1DF3446C047 Q35968860-FAE2F858-39E6-405E-808A-83D55854FB54 Q36195133-AE495301-71B2-44C2-91BF-D16CBD69192F Q36439481-F37E1137-D4B6-43DD-858D-20032924D797 Q36648981-DCD2185D-8DA8-48A9-B44D-79C13E8C6EEE Q36746031-AFA66A39-35ED-45C1-83D2-2B13C144A901 Q36812054-CD1DAE57-5F7A-47B6-A4C3-9E305DF9A0FD Q38340154-2E24A01A-05F6-47AB-A7E8-15CA1CEB1603 Q38618953-847BF64E-1540-4207-8E1A-56EE04E0D138 Q39971521-25712230-6C14-4F12-8205-D1C32CC196C1 Q46731869-5440DE62-C789-4C6E-89FC-9B2DA68C6F49 Q47951198-AF71D754-6A99-4733-8665-35B6BCF40380 Q50208787-E95A3C5C-80F6-4EF3-B736-0A34A92BE321

P2860

Structure of a Calcium-dependent 11R-Lipoxygenase Suggests a Mechanism for Ca2+ Regulation

http://www.wikidata.org/entity/Q27678989

description

2012 nî lūn-bûn

@nan

2012 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

name

Structure of a Calcium-depende ...... Mechanism for Ca2+ Regulation

@ast

Structure of a Calcium-depende ...... Mechanism for Ca2+ Regulation

@en

Structure of a Calcium-depende ...... Mechanism for Ca2+ Regulation

@nl

type

label

Structure of a Calcium-depende ...... Mechanism for Ca2+ Regulation

@ast

Structure of a Calcium-depende ...... Mechanism for Ca2+ Regulation

@en

Structure of a Calcium-depende ...... Mechanism for Ca2+ Regulation

@nl

prefLabel

Structure of a Calcium-depende ...... Mechanism for Ca2+ Regulation

@ast

Structure of a Calcium-depende ...... Mechanism for Ca2+ Regulation

@en

Structure of a Calcium-depende ...... Mechanism for Ca2+ Regulation

@nl

P1433

Q27678989-FCBFDE3A-C355-42A9-BEBC-AAB1480950E0

P1476

Q27678989-296CBA65-A1AE-443D-91DA-A0F29E1BFF6A

P2093

Q27678989-30A60ACB-657B-451B-BC34-1010B97A346F

Q27678989-3231F5E0-EF56-411B-9426-8F2E90990CE4

Q27678989-9C3FBED8-B5FD-4929-90C8-76CA713FC7C5

Q27678989-DC3EB27C-C247-426D-98F3-250612A3B15C

Q27678989-E4DF2822-54E4-4C72-9962-A1BF35B88FD3

P2860

Q27678989-01F3F8E8-385B-4C37-B344-E4D2DBFB95C7

Q27678989-0FA0E56F-69A8-4595-9FB0-D0E95F59A9C8

Q27678989-120F7F90-1527-41CB-94C5-CC7B11FD4082

Q27678989-148ED384-2D17-4E15-8CFB-A071C0E77669

Q27678989-14943002-BE61-4F9B-8D94-D6ADDA83E3E2

Q27678989-1519A6E7-D289-45B5-AC5D-2061D948D2DE

Q27678989-18E9BEE5-6DD8-4325-89D4-0CCAB70CAAC9

Q27678989-1BEAD68F-C56A-482C-BEDB-81925EC0F721

Q27678989-1E98FBA0-E7C4-43AB-8D0C-BB4E7663FEC0

Q27678989-24F36B32-9D23-4676-9760-A3B97FDC22D5

P304

Q27678989-5B2FD4BA-8C6A-4C28-83BD-6D3725B97247

P31

Q27678989-D84BC957-0291-469E-924C-5C47A93C4913

P3181

Q27678989-619771D0-F4E7-4E8A-BE87-2BDF97294549

P356

Q27678989-DC47D87C-0AB6-457F-AFF6-3AB41111C13D

P407

Q27678989-A05430E0-852F-427F-A5DF-8BC1C60EEFFC

P433

Q27678989-7F00390C-752F-4D95-95BB-96CA3EA42DA5

P478

Q27678989-BFDC2EF9-F03F-4317-8045-9D9F87F6AC31

P50

Q27678989-0CB2423B-685E-4061-BBF8-F18EC27F6DC5

P577

Q27678989-06561439-486D-4500-AC2B-3A1EA7A05C66

P5875

Q27678989-61980224-37EC-4809-BB15-66465FF77BDB

P698

Q27678989-0ED75FD5-99BE-4ADC-8CBC-9F792411F05F

P921

Q27678989-809DAA37-EEC3-4E42-8480-810EDF473BEA

P932

Q27678989-B986458A-503F-43EB-9EF4-0A0335F70178

P3181

P356

JBC.M112.343285

P1433

Journal of Biological Chemistry

P1476

Structure of a calcium-depende ...... mechanism for Ca2+ regulation

@en

P2093

Ivar Järving

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

Marcia E Newcomer

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

Nathaniel C Gilbert

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

Nigulas Samel

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

Reet Järving

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

P2860

Identification of amino acid determinants of the positional specificity of mouse 8S-lipoxygenase and human 15S-lipoxygenase-2

A primary determinant for lipoxygenase positional specificity

The structure of human 5-lipoxygenase

MolProbity: all-atom structure validation for macromolecular crystallography

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Multiple sequence alignment with the Clustal series of programs

Characterisation of the calcium-binding C-terminal domain of Clostridium perfringens alpha-toxin

The 1.85 Å Structure of an 8 R -Lipoxygenase Suggests a General Model for Lipoxygenase Product Specificity

Conformational flexibility in mammalian 15S-lipoxygenase: Reinterpretation of the crystallographic data

Determination of protein structures--a series of fortunate events.

P304

22377-22386

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

P31

scholarly article

P3181

5070670

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

P356

10.1074/JBC.M112.343285

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

P407

P433

26

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

P478

287

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

P50

P577

2012-05-09T00:00:00Z

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

P5875

224933280

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

P698

22573333

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

P921

P932

3381197

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