Crystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber - Test2 - elhamkhani - TriplyDB

Crystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber

Crystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber

http://www.wikidata.org/entity/Q27664441

about

Mutations to a glycine loop in the catalytic site of human Lon changes its protease, peptidase and ATPase activities Cross Talk of Proteostasis and Mitostasis in Cellular Homeodynamics, Ageing, and Disease Multitasking in the mitochondrion by the ATP-dependent Lon protease Evolution and significance of the Lon gene family in Arabidopsis organelle biogenesis and energy metabolism A Self-compartmentalizing Hexamer Serine Protease from Pyrococcus Horikoshii: SUBSTRATE SELECTION ACHIEVED THROUGH MULTIMERIZATION Structure of an Rrp6–RNA exosome complex bound to poly(A) RNA Structures of an ATP-independent Lon-like protease and its complexes with covalent inhibitors The N-terminal substrate-recognition domain of a LonC protease exhibits structural and functional similarity to cytosolic chaperones Mitochondrial Lon protease in human disease and aging: Including an etiologic classification of Lon-related diseases and disorders The N-terminal domain plays a crucial role in the structure of a full-length human mitochondrial Lon protease.Multifunctional Mitochondrial AAA Proteases Dynamic and static components power unfolding in topologically closed rings of a AAA+ proteolytic machine.A Lon-like protease with no ATP-powered unfolding activity The LonB protease controls membrane lipids composition and is essential for viability in the extremophilic haloarchaeon Haloferax volcanii.Mitochondrial Lon protease at the crossroads of oxidative stress, ageing and cancer.Distinct quaternary structures of the AAA+ Lon protease control substrate degradation.Archaeal membrane-associated proteases: insights on Haloferax volcanii and other haloarchaea.Proteomic Insights into Sulfur Metabolism in the Hydrogen-Producing Hyperthermophilic Archaeon Thermococcus onnurineus NA1.Gates of enzymes.A mutation in the N domain of Escherichia coli lon stabilizes dodecamers and selectively alters degradation of model substrates.Archaeal proteasomes and sampylation.Marching to the beat of the ring: polypeptide translocation by AAA+ proteases.The multifaceted role of Lon proteolysis in seedling establishment and maintenance of plant organelle function: living from protein destruction.Post-translation modification in Archaea: lessons from Haloferax volcanii and other haloarchaea.Mini review: ATP-dependent proteases in bacteria.The Roles of β-Oxidation and Cofactor Homeostasis in Peroxisome Distribution and Function in Arabidopsis thaliana.Assessing heterogeneity in oligomeric AAA+ machines.Roles of the N domain of the AAA+ Lon protease in substrate recognition, allosteric regulation and chaperone activity.Structural basis for the ATP-independent proteolytic activity of LonB proteases and reclassification of their AAA+ modules.Regulatory circuits of the AAA+ disaggregase Hsp104.Lon protease affects the RdxA nitroreductase activity and metronidazole susceptibility in Helicobacter pylori.Role of an N-terminal extension in stability and catalytic activity of a hyperthermostable α/β hydrolase fold esterase.Mitochondrial LON protease-dependent degradation of cytochrome c oxidase subunits under hypoxia and myocardial ischemia.A Phosphorylation Switch on Lon Protease Regulates Bacterial Type III Secretion System in Host.Defining the crucial domain and amino acid residues in bacterial Lon protease for DNA binding and processing of DNA-interacting substrates.A redox switch shapes the Lon protease exit pore to facultatively regulate proteolysis Multiple domains of bacterial and human Lon proteases define substrate selectivity

P2860

Q24337020-A426BDB3-0367-4215-95F5-207387198B19 Q26765684-7626571D-57AB-4DA4-9B57-AFB11B38F998 Q27003208-FC79F4C1-76D3-4513-B1B9-BEEDB9175FE7 Q27003925-686459E9-A84C-4CA4-A28C-96B7C9BD5F1D Q27677875-C213D091-1FDD-4F56-B23E-FCE31C709C82 Q27684742-B9F27D3A-9260-4D2F-B243-53DDE93D5261 Q27685291-31A9A1A2-55C1-4474-AF0F-FA9B971AA47E Q27685452-E4BDB71B-1855-4D1D-8FCA-6B651AF9CBF7 Q28071866-10DD8E5E-C41D-49F0-8170-82C40299F30F Q30812118-DD64E228-CE93-492A-8759-4F8176126900 Q33710845-2617D0F2-3B15-4BDB-9BA1-C50BB4FCC16D Q34273097-A80FC87E-0592-4187-AFED-C60F031289C9 Q34336038-1C5F294B-A9E0-420D-9FB5-8FEC39253426 Q34398073-4DA5972E-BDE0-4D95-86A9-094761698844 Q34493828-3266D34A-F161-4E8B-94BA-379C382C4F91 Q34651849-405A9E51-2604-40C0-BFEC-407E7F104B41 Q35129642-08F3159B-0F46-4B31-A108-09A7DD1B442E Q35722710-91F628C8-E05F-4E3A-A659-9DBBC32F088D Q37098498-539BEE51-34D5-4D50-B208-D3D4989FF5E6 Q37469756-89D81C87-B9B8-4E01-BB47-7A66E0995355 Q37606188-CC0FCDC1-ABBD-4310-BB59-40AC5150FE67 Q37625067-228BF58C-710B-430B-A354-A9DD8DD2A1DD Q37949008-1360CB09-1A76-484D-94F6-D693C35856F5 Q38061206-E0B12A55-1D59-473B-958C-DAA260A33EA0 Q38772212-848A7FD8-5B1D-4D88-AA38-CFF5F98B7ACC Q38823505-7BDEB80A-D7F4-4F0E-9F69-E153DEB5D7C8 Q38964718-9B6DDE3F-659A-4AB6-BAE3-A70598BC8F9B Q39217558-EB3A1B0F-DA7C-4818-91CB-12E5E3C49B27 Q40475660-E71B4410-F9D8-49D4-BF70-8DB0BB49B2DD Q42733235-9B419D72-14E6-4F92-BB96-BD3FFB58F2BD Q43757938-F991ED79-8DCA-4667-BA13-12F7CB889300 Q47716456-11949D71-5006-45B7-85FE-582FC1DB271B Q47910121-F01B9D5D-A231-42BB-9429-E607E77332DA Q49193031-18D88383-3B47-49FF-94E1-045438029ACF Q50959628-40D53FC2-F0EE-4961-B708-1488F5FCA054 Q57893547-FADF1180-D9D7-4CCB-9D4D-A42DA364C566 Q58770991-AC35A67F-3984-42BD-97B2-983F3A55BD3E

P2860

Crystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber

http://www.wikidata.org/entity/Q27664441

description

2010 nî lūn-bûn

@nan

2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հոտեմբերին 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

Crystal structure of Lon prote ...... equestered degradation chamber

@ast

Crystal structure of Lon prote ...... equestered degradation chamber

@en

Crystal structure of Lon prote ...... equestered degradation chamber

@nl

type

label

Crystal structure of Lon prote ...... equestered degradation chamber

@ast

Crystal structure of Lon prote ...... equestered degradation chamber

@en

Crystal structure of Lon prote ...... equestered degradation chamber

@nl

prefLabel

Crystal structure of Lon prote ...... equestered degradation chamber

@ast

Crystal structure of Lon prote ...... equestered degradation chamber

@en

Crystal structure of Lon prote ...... equestered degradation chamber

@nl

P1433

Q27664441-C8A4B3D9-48E4-4E35-8998-948C96339901

P1476

Q27664441-E8066247-9E70-455E-935A-C4FDACA51CA0

P2093

Q27664441-0C1264C3-DD59-44C8-ACD5-D8742C5F3F45

Q27664441-28BA0C4B-C826-4C2C-A50F-10E6C4468B97

Q27664441-4AC17477-0FBE-4B76-8937-B2B9C2CEE530

Q27664441-5370FCE1-D0C8-4D09-B0D7-C6247E8E66A7

Q27664441-8E8DA31D-1253-42B6-8B2A-08D8BD0A75D1

Q27664441-8EB7E4AF-557D-4576-98D5-23107408FF98

Q27664441-9162E7C4-CEA7-44B7-93CD-641B3FFD7AD1

Q27664441-9F3FC65C-0DDB-486D-8135-E0E45708A493

Q27664441-A02A9D46-9E20-4F5D-BC9C-07CDC3FD150B

Q27664441-B72D524E-6EE5-445C-9A9C-4B57D59F4CB1

P2860

Q27664441-043D9D72-EE0B-40B3-B6B5-1D5A494BA639

Q27664441-073F7282-907B-4A2A-BB2C-36996D77074E

Q27664441-078DB490-1C48-4F53-BFBB-9F1349BEA48B

Q27664441-08DFA593-0130-45B8-8B0E-41ECE7FBE58C

Q27664441-183E07A3-BBF1-4859-9C2D-04BD42C0805D

Q27664441-1FC37D67-845D-4253-B621-2BC6A42CA62D

Q27664441-2AA982AA-1629-457C-8265-B0A008373BDE

Q27664441-2B118CA8-DAC6-4CD3-9959-5BA7204733CE

Q27664441-35B72C8E-0C72-4A0F-9293-A90DF09E856B

Q27664441-38E027A9-D857-402B-ACEC-1664C1BFBC59

P304

Q27664441-51A4AF03-D595-4F7F-8F51-D718B8EEFCC5

P31

Q27664441-5257F2DD-5E8A-4346-B5AC-99C954FDAB4A

P3181

Q27664441-841BFDC4-673E-496E-BEBA-FCB6CC349858

P356

Q27664441-2767358A-66AD-40D8-9B60-714EC5E289B8

P407

Q27664441-53B29222-F149-4709-9D88-F13FE0891BB9

P433

Q27664441-2DC31A71-05D4-47DF-9A74-3EF477AB0658

P478

Q27664441-17223960-F7FA-40F3-907F-740CFF41D146

P577

Q27664441-96BDBBFB-D087-461E-8244-0EA5C89143D1

P5875

Q27664441-BEDDC0EA-A11B-458C-9B5C-8324B624D438

P698

Q27664441-2C99898E-E972-4DD6-B4C7-5300D26CBF4F

P921

Q27664441-1E6E2BA3-710F-43D5-998B-D2F6E1D6EA87

P932

Q27664441-0DA6349E-C70D-4E36-88EA-7EB4E823F09D

P3181

P356

P1433

The EMBO Journal

P1476

Crystal structure of Lon prote ...... equestered degradation chamber

@en

P2093

Chang Ro Lee

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

Gian Marco De Donatis

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

Hyun Sook Lee

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

Jung-Hyun Lee

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

Kae Kyoung Kwon

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

Michael R Maurizi

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

Sang Jin Kim

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

Sun-Shin Cha

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

Sung Gyun Kang

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

Yeon-Gil Kim

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

P2860

The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system

Single-turnover kinetic experiments confirm the existence of high- and low-affinity ATPase sites in Escherichia coli Lon protease

The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site

Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine.

The crystal structure of apo-FtsH reveals domain movements necessary for substrate unfolding and translocation.

Crystal structures of Bacillus subtilis Lon protease

Acyldepsipeptide antibiotics induce the formation of a structured axial channel in ClpP: A model for the ClpX/ClpA-bound state of ClpP.

Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution

Structure of 20S proteasome from yeast at 2.4 A resolution

Crystal structure of heat shock locus V (HslV) from Escherichia coli

P304

3520-30

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

P31

scholarly article

P3181

3491558

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

P356

10.1038/EMBOJ.2010.226

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

P407

P433

20

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

P478

29

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

P577

2010-10-20T00:00:00Z

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

P5875

46220731

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

P698

20834233

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

P921

crystal structure

P932

2964173

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