Structural basis for Ca2+-independence and activation by homodimerization of tomato subtilase 3 - Wikidata - awgldk - TriplyDB

Structural basis for Ca2+-independence and activation by homodimerization of tomato subtilase 3

Structural basis for Ca2+-independence and activation by homodimerization of tomato subtilase 3

http://www.wikidata.org/entity/Q27657677

about

Parasitic plants of the genus Cuscuta and their interaction with susceptible and resistant host plants Regulation of an intracellular subtilisin protease activity by a short propeptide sequence through an original combined dual mechanism The malaria parasite egress protease SUB1 is a calcium-dependent redox switch subtilisin Functional insight into the C-terminal extension of halolysin SptA from haloarchaeon Natrinema sp. J7 Phylogenetic analyses reveal molecular signatures associated with functional divergence among Subtilisin like Serine Proteases are linked to lifestyle transitions in Hypocreales Characterization of a New S8 serine Protease from Marine Sedimentary Photobacterium sp. A5-7 and the Function of Its Protease-Associated Domain Arabidopsis PECTIN METHYLESTERASE17 is co-expressed with and processed by SBT3.5, a subtilisin-like serine protease.A subtilisin-like protein from soybean contains an embedded, cryptic signal that activates defense-related genes.Functional analysis of the cucumisin propeptide as a potent inhibitor of its mature enzyme.A plant alternative to animal caspases: subtilisin-like proteases Plant phytaspases and animal caspases: structurally unrelated death proteases with a common role and specificity.Improved detection of remote homologues using cascade PSI-BLAST: influence of neighbouring protein families on sequence coverage.Horizontal transfer of a subtilisin gene from plants into an ancestor of the plant pathogenic fungal genus Colletotrichum Genome-wide and molecular evolution analysis of the subtilase gene family in Vitis vinifera Insights into the maturation of hyperthermophilic pyrolysin and the roles of its N-terminal propeptide and long C-terminal extension.Regulation of Clostridium difficile spore germination by the CspA pseudoprotease domain A Clostridium difficile-Specific, Gel-Forming Protein Required for Optimal Spore Germination The subtilisin-like protease SBT3 contributes to insect resistance in tomato.Trafficking and proteolytic processing of RNF13, a model PA-TM-RING family endosomal membrane ubiquitin ligase.Subtilases - versatile tools for protein turnover, plant development, and interactions with the environment.Small signaling peptides in Arabidopsis development: how cells communicate over a short distance.Plasmodium berghei PIMMS2 promotes ookinete invasion of the Anopheles gambiae mosquito midgut.From structure to function - a family portrait of plant subtilases.Subtilisin-like proteases in plant defence: the past, the present and beyond.The asparagine-rich protein NRP interacts with the Verticillium effector PevD1 and regulates the subcellular localization of cryptochrome 2.Isolation and Characterization of a Thionin Proprotein-processing Enzyme from Barley.Structural features of plant subtilases.Functional Characterization of Propeptides in Plant Subtilases as Intramolecular Chaperones and Inhibitors of the Mature Protease.New insights into the evolution and structure of Colletotrichum plant-like subtilisins (CPLSs).Self-processing of a barley subtilase expressed in E. coli.How vacuolar sorting receptor proteins interact with their cargo proteins: crystal structures of apo and cargo-bound forms of the protease-associated domain from an Arabidopsis vacuolar sorting receptor.Tumour-associated mutations of PA-TM-RING ubiquitin ligases RNF167/RNF13 identify the PA domain as a determinant for endosomal localization.Structural basis of cucumisin protease activity regulation by its propeptide.Native and Biotechnologically Engineered Plant Proteases with Industrial Applications Identification, gene cloning and expression of serine proteases in the extracellular medium of Nicotiana tabacum cells

P2860

Q27027723-0AF5600A-DC3C-400D-83E7-322A34059B32 Q27666916-983C5F5F-743B-484B-B717-81ACBC47EC85 Q27683602-EE7369B7-735E-4CD1-A6D1-E4FA744C03B6 Q28476631-D72F783A-0055-49CF-9F52-80630FC1F34D Q28597208-2E635D22-B155-4F81-874B-BDC7F1E65E1B Q28818791-62914FB6-3CAD-451D-90A8-98C3F0A40DFD Q30360583-0742F3C6-06D4-477C-AF9E-E01ADC67A68A Q34093280-2DE30194-E71A-49B9-B1F9-9C5BE57DD715 Q34144534-4CE352FA-5343-48C0-A22D-432D884339F7 Q34183085-97C940D3-4554-4992-A8D5-C91AE50991C2 Q34241603-EDA211CD-80DC-4487-A8F7-8B29871FFC0B Q34598734-A967D167-995E-44EE-AE0D-0EF3C8C44797 Q34648716-4FC29A92-31A9-4FDE-8B5A-700C2B14EA47 Q35228324-D8B2A341-F316-40F3-B4B6-773E951AA2E4 Q36018091-5D637FA2-9A79-4681-B9E7-E12932BB9575 Q36520610-C6A7E821-6F53-4AD5-8041-DBEE1B483B17 Q37590711-5F3A14DE-0AB5-4692-ACF5-76D61746D181 Q37635516-14CB4D19-EDAF-458E-8071-BD15375D4774 Q37809581-3A304ABF-D073-408D-804D-E3A80D7529E0 Q37944286-A02D18F2-4737-40F3-8608-F8D47635188E Q38038977-FD41C325-B6F3-4024-A807-43AAB59D90BD Q38755598-6E9B18FB-530D-44BB-85BF-E6EAD568D526 Q39280575-4A4DA24B-DA65-4C8C-9D50-A0515EBEDFE5 Q39317801-0ED234FC-8715-41FF-B3F4-9B372AA4191A Q40165064-342F523F-F177-4760-9014-9F363C511EC8 Q40899612-017D0E03-83D5-4453-8CF9-0FB226A9B5DF Q41001082-537BC12B-51C9-46DC-9AB3-8C67F8294C5D Q41049557-B3F5199E-BB6E-43AA-936B-CA3F0B2277C1 Q41933259-7F362175-06D8-41AD-AD27-62E408866D61 Q42848929-60F44A60-65F3-4120-A40F-FAA472751621 Q44660751-5C1C9037-C867-4ECD-80E4-4B7BCCFDBEDA Q46124826-25B7A88E-8F0C-4B65-8BB9-C286A826D3AB Q51167127-644BE1C7-B4E7-448B-91F8-6A0F2E2A1A65 Q56093590-B5F1038C-976B-4D45-8B93-F45C455797D5 Q57800549-294E8774-85F5-492A-A7E9-E8B23317654C

P2860

Structural basis for Ca2+-independence and activation by homodimerization of tomato subtilase 3

http://www.wikidata.org/entity/Q27657677

description

2009 nî lūn-bûn

@nan

2009 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

Structural basis for Ca2+-inde ...... rization of tomato subtilase 3

@ast

Structural basis for Ca2+-inde ...... rization of tomato subtilase 3

@en

Structural basis for Ca2+-inde ...... rization of tomato subtilase 3

@nl

type

label

Structural basis for Ca2+-inde ...... rization of tomato subtilase 3

@ast

Structural basis for Ca2+-inde ...... rization of tomato subtilase 3

@en

Structural basis for Ca2+-inde ...... rization of tomato subtilase 3

@nl

prefLabel

Structural basis for Ca2+-inde ...... rization of tomato subtilase 3

@ast

Structural basis for Ca2+-inde ...... rization of tomato subtilase 3

@en

Structural basis for Ca2+-inde ...... rization of tomato subtilase 3

@nl

P1433

Q27657677-F54F889A-E41F-4856-9DB8-8F498840E6F1

P1476

Q27657677-A5586056-D0D1-4EE4-9960-5B25EFF7289C

P2093

Q27657677-35380359-7183-47F3-8EE6-F567AA04D69D

Q27657677-393539FF-12B3-4556-B7FE-5C863048339B

Q27657677-900B5FF8-8B4F-441C-9544-A78716EB9F6C

Q27657677-C1B6E91D-87E1-4DE0-8B39-07C927DA02E1

Q27657677-CE55C327-B7D9-47A1-A791-78FFABBD5F8E

Q27657677-ECFFD5F4-3416-4A51-840E-B793135A2345

P2860

Q27657677-00BECB93-B663-4F2C-9698-E19729F951CD

Q27657677-05F9D642-0029-4F0E-A07B-F9118740DFA7

Q27657677-08777F5B-4167-4E70-9202-F45F214EAF56

Q27657677-0B79E7FD-A4CB-4DA6-B32F-B35722BB0A7E

Q27657677-10AFD6C6-94D3-43EA-A965-75410B305705

Q27657677-13A5850C-0690-4E3B-95CD-56B460E6FF50

Q27657677-178BCA51-83AB-4F37-BB72-3B8DB68300FD

Q27657677-21F5D58D-04CB-4E2F-BC0B-8F74825AA2FC

Q27657677-26E092A8-F083-418B-9306-C0F07D79A89F

Q27657677-35988D41-CB0D-48A8-B1D5-77AE4F932EA6

P304

Q27657677-1A8C8499-E468-4B75-8216-3997A8DDC8B1

P31

Q27657677-C071D464-C48D-4891-8220-CD52B291B559

P3181

Q27657677-F97150B2-566B-4CC0-B9A2-DAED0728970B

P356

Q27657677-37F168A6-B1B0-40DD-8AD6-8CF107DDB754

P407

Q27657677-2ADBE99B-7EFB-4812-BD94-972470242E66

P433

Q27657677-AA1840AC-9680-4404-903B-4FD16C30B0DB

P478

Q27657677-CDF8D756-FF11-47E3-9953-E62FB53D25AF

P50

Q27657677-382926D1-8235-4592-84EE-DC305C443265

Q27657677-92A15602-A5B6-4E63-8E74-AB3A0473D26E

P577

Q27657677-98056655-E261-4DED-A9D1-3964BCFF50E7

P5875

Q27657677-E3E2FB9C-005C-4377-9B38-18E53EF75A1A

P698

Q27657677-F761EDDD-81E1-4CFA-A947-115EDD259F7A

P932

Q27657677-81A10F2E-83BA-4D3B-A9BE-00BC2FC4306E

P3181

P356

PNAS.0907587106

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Structural basis for Ca2+-inde ...... rization of tomato subtilase 3

@en

P2093

Anna Cedzich

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

Franziska Huttenlocher

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

Markus Kaiser

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

Patrick Hauske

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

Robert Huber

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

Rolf Rose

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

P2860

Differential localization and identification of a critical aspartate suggest non-redundant proteolytic functions of the presenilin homologues SPPL2b and SPPL3

Three-dimensional structure of a transglutaminase: human blood coagulation factor XIII

Inferring hypotheses on functional relationships of genes: Analysis of the Arabidopsis thaliana subtilase gene family.

Crystal structure of the ectodomain of human transferrin receptor

Calcium-mediated thermostability in the subtilisin superfamily: the crystal structure of Bacillus Ak.1 protease at 1.8 A resolution

The crystal structure of the proprotein processing proteinase furin explains its stringent specificity

Differential P1 arginine and lysine recognition in the prototypical proprotein convertase Kex2

Model for substrate interactions in C5a peptidase from Streptococcus pyogenes: A 1.9 A crystal structure of the active form of ScpA

Large increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfolding

Calcium-independent subtilisin by design

P304

17223-8

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

P31

scholarly article

P3181

2918162

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

P356

10.1073/PNAS.0907587106

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

P407

P433

40

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

P478

106

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

P50

Christian Ottmann

Andreas Schaller

P577

2009-10-06T00:00:00Z

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

P5875

26871277

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

P698

19805099

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

P932

2749846

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