Characterization of a novel zinc metalloprotease involved in degrading targeting peptides in mitochondria and chloroplasts. - Test2 - elhamkhani - TriplyDB

Characterization of a novel zinc metalloprotease involved in degrading targeting peptides in mitochondria and chloroplasts.

Characterization of a novel zinc metalloprotease involved in degrading targeting peptides in mitochondria and chloroplasts.

http://www.wikidata.org/entity/Q44655469

about

Chloroplast Proteases: Updates on Proteolysis within and across Suborganellar Compartments Killing Me Softly: Connotations to Unfolded Protein Response and Oxidative Stress in Alzheimer's Disease Molecular Basis of Substrate Recognition and Degradation by Human Presequence Protease Role of the novel metallopeptidase Mop112 and saccharolysin for the complete degradation of proteins residing in different subcompartments of mitochondria.A role for falcilysin in transit peptide degradation in the Plasmodium falciparum apicoplast Engineering membrane protein overproduction in Escherichia coli.Cloning, expression and characterization of insulin-degrading enzyme from tomato (Solanum lycopersicum).Light has a specific role in modulating Arabidopsis gene expression at low temperature.Differential protein acetylation assists import of excess SOD2 into mitochondria and mediates SOD2 aggregation associated with cardiac hypertrophy in the murine SOD2-tg heart.The stromal processing peptidase of chloroplasts is essential in Arabidopsis, with knockout mutations causing embryo arrest after the 16-cell stage The closed structure of presequence protease PreP forms a unique 10,000 Angstroms3 chamber for proteolysis.Protein degradation within mitochondria: versatile activities of AAA proteases and other peptidases.Amyloid-Beta interaction with mitochondria Identification of human presequence protease (hPreP) agonists for the treatment of Alzheimer's disease.A proteomic analysis of the chromoplasts isolated from sweet orange fruits [Citrus sinensis (L.) Osbeck].A Putative Chloroplast Thylakoid Metalloprotease VIRESCENT3 Regulates Chloroplast Development in Arabidopsis thaliana.Two novel mitochondrial and chloroplastic targeting-peptide-degrading peptidasomes in A. thaliana, AtPreP1 and AtPreP2.Organellar oligopeptidase (OOP) provides a complementary pathway for targeting peptide degradation in mitochondria and chloroplasts.Mitochondrial accumulation of APP and Abeta: significance for Alzheimer disease pathogenesis.A novel mitochondrial and chloroplast peptidasome, PreP.Proteolytic system of plant mitochondria.Mitochondrial quality control: a matter of life and death for neurons.Mitochondrial protein homeostasis.The versatility of the mitochondrial presequence processing machinery: cleavage, quality control and turnover.INTERMEDIATE CLEAVAGE PEPTIDASE55 Modifies Enzyme Amino Termini and Alters Protein Stability in Arabidopsis Mitochondria.Proteolytic processing of an Arabidopsis membrane-bound NAC transcription factor is triggered by cold-induced changes in membrane fluidity.Proteomic analysis of salicylic acid-induced resistance to Magnaporthe oryzae in susceptible and resistant rice.Refining the definition of plant mitochondrial presequences through analysis of sorting signals, N-terminal modifications, and cleavage motifs.An antimicrobial origin of transit peptides accounts for early endosymbiotic events.Functional requirement for human pitrilysin metallopeptidase 1 arginine 183, mutated in amyloidogenic neuropathy.Catalysis, subcellular localization, expression and evolution of the targeting peptides degrading protease, AtPreP2.Colorimetric in situ assay of membrane-bound enzyme based on lipid bilayer inhibition of ion transport.In VitroComparative Kinetic Analysis of the Chloroplast Toc GTPases Divalent metal ions in plant mitochondria and their role in interactions with proteins and oxidative stress-induced damage to respiratory function Cellular Fractionation and Nanoscopic X-Ray Fluorescence Imaging Analyses Reveal Changes of Zinc Distribution in Leaf Cells of Iron-Deficient Plants

P2860

Q26747073-006F28B0-BF27-4A21-84D9-810AF0B45EF7 Q26765824-A6AFEA81-1969-4860-AF59-073B218018A3 Q27684349-9462393A-BDEF-4A35-ACC4-7C06B466BFD9 Q27933424-02BB02A5-5182-4C37-A14E-1585ADBAAF3D Q30042129-8F39EF7F-CEF1-4480-804E-3DDBF3F07C39 Q30841537-FEBB0D99-4E40-4955-A4DD-D1B08E8D2F1D Q33311567-F7C534C7-AEB8-4B70-B3ED-6BC1B701E598 Q33317057-61D8A6F2-A883-49C6-8727-1F6F4A5A27C3 Q33842677-09CA54D6-5148-44F9-83DF-BF8DBF78F1C6 Q33999136-70498880-17FE-4B72-838D-C8983F3C83EB Q34511800-EB730D81-F5D2-4056-B5F6-0B2E32193DD2 Q34636507-5F385FC8-5DF2-4270-BCB2-BEF25B46550D Q34725635-271DFC17-6707-4018-BFA5-5F656421DA8B Q35240665-3E13B0D5-2AD0-433D-BDC9-60B87A826B8F Q35570080-64847FAA-5112-4B12-8198-550F47FF22AA Q36573958-87649CD2-732E-4AF3-8CB9-8B955B722E2B Q36642771-07B64774-016C-418F-8A03-E72E32E550ED Q37218415-143CD169-2D06-4507-AFC2-2E32C1817952 Q37590902-8BC92642-BD58-418F-8E98-8E605892EEB8 Q37945294-8CBE19D9-1280-4026-BA21-635DE02C5BB7 Q37956411-5927B32E-B4F4-49AF-B5EC-BFFD2C7860B6 Q37987023-DA7C687F-47E6-408E-968C-92475338C1EB Q38076092-031035C9-7E9D-40E3-9646-9CE1BAED8680 Q38946441-1DF9243C-2A7C-456C-B88A-A88591001214 Q41089770-B85734E6-C010-4CBD-ABBC-45536763FE03 Q43161821-E62C7B27-A2AD-44F7-AB9A-EB26C17679F7 Q43717468-AB770087-0D5A-4A60-9CA6-814C04C74B46 Q45993903-799500EB-E110-43E4-8F42-DD898B2DE4DF Q49051343-D435D3E9-1706-4547-BE75-D06915D673EB Q49565161-3838617F-818C-41C1-B373-7E1BFA7EB3B5 Q50771628-254A4398-187B-435A-9B93-54985E189E8E Q55260356-2908C9A5-D675-4CC5-BAE6-EE3F0F4D12EA Q57951188-C8E9EB75-ABBE-4D20-A3B6-0D536C51B752 Q58064251-B2573B40-F4DC-4658-BC17-B7A3CBF6D7A0 Q58801868-59E03A6C-1143-4370-B0C4-CFB3ECCFAC0A

P2860

Characterization of a novel zinc metalloprotease involved in degrading targeting peptides in mitochondria and chloroplasts.

http://www.wikidata.org/entity/Q44655469

description

2003 nî lūn-bûn

@nan

2003年の論文

@ja

2003年学术文章

@wuu

2003年学术文章

@zh

2003年学术文章

@zh-cn

2003年学术文章

@zh-hans

2003年学术文章

@zh-my

2003年学术文章

@zh-sg

2003年學術文章

@yue

2003年學術文章

@zh-hant

name

Characterization of a novel zi ...... mitochondria and chloroplasts.

@en

Characterization of a novel zi ...... mitochondria and chloroplasts.

@nl

type

label

Characterization of a novel zi ...... mitochondria and chloroplasts.

@en

Characterization of a novel zi ...... mitochondria and chloroplasts.

@nl

prefLabel

Characterization of a novel zi ...... mitochondria and chloroplasts.

@en

Characterization of a novel zi ...... mitochondria and chloroplasts.

@nl

P1433

Q44655469-53C8BA14-0E86-41CC-B230-A37614103EA4

P1476

Q44655469-8316D504-59B7-4C87-98DC-736EACB53713

P2093

Q44655469-5B5C6822-CB36-4630-AAF2-FEC9B135A7B9

Q44655469-7924048C-80A3-4E37-AD29-E38F2C18F0C9

Q44655469-83E7A636-C590-495A-9C21-C027720ECB50

Q44655469-87674C93-4279-412C-A979-D4BDBD95FEDE

Q44655469-EC700444-09FE-40B4-8EB5-E9B3541DB6C9

Q44655469-FCC0A2E5-2734-426A-BFED-37FC6F9A8A0C

Q44655469-FEAE3A40-E4C9-4C18-ADCB-01495BEE4A12

P2860

Q44655469-0FE4F4B3-FFC7-4478-8030-D15C41CC1771

Q44655469-2257EC20-2D84-4BBE-A77E-7D0D32AD6525

Q44655469-4F6FB9C1-8068-4AAD-94DB-0D6BF640BA89

Q44655469-5B707E45-D587-43E4-94EC-1304FF932E61

Q44655469-A2F034A3-8669-44F5-AB03-5AA56799A6E6

P304

Q44655469-9AB36C1D-E39F-4C1B-9A4F-727EEBAB9E69

P31

Q44655469-255524AB-9A8D-49E5-AC56-0D670C664494

P356

Q44655469-CD0EA9E1-1765-4B69-9AE4-3A4B197C0FBA

P433

Q44655469-0707181D-5921-4E79-9BB0-2D6BC7DFF033

P478

Q44655469-80D99399-EA75-4584-B0E9-44E7AE1CE27F

P577

Q44655469-B1C8D4AD-BBFB-4186-B66E-4EA6603D5924

P698

Q44655469-16D4C986-B245-4A83-8B1E-02E641ADFF0E

P921

Q44655469-E2765DE1-43C0-41FE-A9E3-4A6D2F875C58

P356

J.1365-313X.2003.01904.X

P1433

The Plant Journal

P1476

Characterization of a novel zi ...... mitochondria and chloroplasts.

@en

P2093

AnnaCarin Eriksson

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

Annelie Ståhl

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

Barry D Bruce

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

Elzbieta Glaser

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

Per Moberg

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

Sarah J Wright

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

Shashi Bhushan

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

P2860

Homologues of insulinase, a new superfamily of metalloendopeptidases.

Dual targeting to mitochondria and chloroplasts.

Identification of glutamate-169 as the third zinc-binding residue in proteinase III, a member of the family of insulin-degrading enzymes.

Rapid degradation of the presequence of the f1beta precursor of the ATP synthase inside mitochondria.

Evidence for a novel ATP-dependent membrane-associated protease in spinach leaf mitochondria.

P304

616-628

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

P31

scholarly article

P356

10.1046/J.1365-313X.2003.01904.X

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

P433

5

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

P478

36

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

P577

2003-12-01T00:00:00Z

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

P698

14617063

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

P921