The closed structure of presequence protease PreP forms a unique 10,000 Angstroms3 chamber for proteolysis.
about
Structure of substrate-free human insulin-degrading enzyme (IDE) and biophysical analysis of ATP-induced conformational switch of IDEKilling Me Softly: Connotations to Unfolded Protein Response and Oxidative Stress in Alzheimer's DiseaseMolecular Basis for the Recognition and Cleavages of IGF-II, TGF-α, and Amylin by Human Insulin-Degrading EnzymeCrystal and Solution Structures of a Prokaryotic M16B Peptidase: an Open and Shut CaseConformational states and recognition of amyloidogenic peptides of human insulin-degrading enzymeMolecular Basis of Substrate Recognition and Degradation by Human Presequence ProteaseA role for falcilysin in transit peptide degradation in the Plasmodium falciparum apicoplastDecreased proteolytic activity of the mitochondrial amyloid-β degrading enzyme, PreP peptidasome, in Alzheimer's disease brain mitochondriaCell-permeable, small-molecule activators of the insulin-degrading enzyme.Mechanism of oxidative inactivation of human presequence protease by hydrogen peroxideProtein degradation within mitochondria: versatile activities of AAA proteases and other peptidases.Proteolytically inactive insulin-degrading enzyme inhibits amyloid formation yielding non-neurotoxic aβ peptide aggregatesAmyloid beta-degrading cryptidases: insulin degrading enzyme, presequence peptidase, and neprilysin.Identification of human presequence protease (hPreP) agonists for the treatment of Alzheimer's disease.Mitochondrial biogenesis and function in Arabidopsis.Two novel mitochondrial and chloroplastic targeting-peptide-degrading peptidasomes in A. thaliana, AtPreP1 and AtPreP2.In vitro oxidative inactivation of human presequence protease (hPreP).Evolution of peptidase diversity.Crystal Structure and Function of PqqF Protein in the Pyrroloquinoline Quinone Biosynthetic Pathway.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.Protein disulfide engineering.Quantitative analysis of protein turnover in plants.The versatility of the mitochondrial presequence processing machinery: cleavage, quality control and turnover.Structure, function, and regulation of insulin-degrading enzyme.Protein-protein docking and analysis reveal that two homologous bacterial adenylyl cyclase toxins interact with calmodulin differently.Divergent evolution of the M3A family of metallopeptidases in plants.A multi-step peptidolytic cascade for amino acid recovery in chloroplasts.Functional requirement for human pitrilysin metallopeptidase 1 arginine 183, mutated in amyloidogenic neuropathy.FusC, a member of the M16 protease family acquired by bacteria for iron piracy against plants
P2860
Q24317274-2052DAA7-BE14-4EF9-B057-1E8012EDD352Q26765824-BA17A8E6-437E-4B76-9D56-E329A1C7EB70Q27658095-18A5C2E7-0379-4648-9E09-8F141D6EE340Q27658164-8790E471-3EFC-4C4C-ADD0-60337B8499DAQ27679412-D8D4773E-5E26-4473-9060-802F48875A34Q27684349-88F45CE9-D169-4B4F-8166-1C14228439E9Q30042129-5598CE69-DCBA-4F20-A0CA-71185E329E42Q34199931-7E786A66-5594-4119-BF57-30D0837D70C2Q34319474-AF20D582-6E81-4669-9A41-BF4F127091C5Q34439464-75856719-4DBC-44F8-AFF9-DD414EACE9E6Q34636507-C3919FD9-C8A3-45FF-8FF2-5037FDF5CBC8Q34672360-D3B88A16-4669-495C-AA1A-0B36DE9F9861Q34777829-D631298F-7729-42B8-9580-83B89A1D7A7CQ35240665-A023CEF8-4058-4389-903F-819D23FC821CQ35625774-D3E94582-034D-4C92-B791-7A800FD6CDACQ36642771-6A8DEA4A-A434-47C4-AA66-215D2CA14379Q36660696-F70F9423-D773-45F4-BBC7-CB994259AEC0Q36949406-EA73A604-635C-4933-95ED-4CA3EDB41EA9Q37117280-E2988197-B882-4348-A50F-763B426A3B3EQ37218415-42318596-2A92-4BC7-9A62-3C0DFEBC2F53Q37590902-5F642577-E317-424F-BDC2-4A27D04DD3D2Q37945294-F16F58A2-44BB-4527-8C9E-0FB063647F0CQ37956411-13983EB1-62C9-4667-A90C-A458365ACAEDQ37987023-275E39E8-A7F3-4EEB-B61C-734A0CB61FE7Q38167555-65C6FDE1-EFA8-4CAF-9F5D-F9347D5B958CQ38170027-246C9F96-39EB-4B55-9098-FA716EF0B6EBQ38946441-B1AD7CC1-D96C-4569-850B-C766E0484A61Q40782441-BFE75A3C-DFA4-4C70-B469-9F85215B30F1Q42423418-BB5207FE-A6CD-4828-A197-8347EDEC1DD0Q46560310-6BCAE651-3855-4B21-AB7C-E047FB8108DEQ48053318-033D6C21-1494-4D48-8FCA-FB9CAC590622Q49565161-B3287468-5CC7-4ACD-969C-E074262CC03BQ57751848-84015A01-426A-41D1-BACD-9295004E1F47
P2860
The closed structure of presequence protease PreP forms a unique 10,000 Angstroms3 chamber for proteolysis.
description
2006 nî lūn-bûn
@nan
2006 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
The closed structure of preseq ...... roms3 chamber for proteolysis.
@ast
The closed structure of preseq ...... roms3 chamber for proteolysis.
@en
The closed structure of preseq ...... roms3 chamber for proteolysis.
@nl
type
label
The closed structure of preseq ...... roms3 chamber for proteolysis.
@ast
The closed structure of preseq ...... roms3 chamber for proteolysis.
@en
The closed structure of preseq ...... roms3 chamber for proteolysis.
@nl
prefLabel
The closed structure of preseq ...... roms3 chamber for proteolysis.
@ast
The closed structure of preseq ...... roms3 chamber for proteolysis.
@en
The closed structure of preseq ...... roms3 chamber for proteolysis.
@nl
P2093
P2860
P356
P1433
P1476
The closed structure of preseq ...... roms3 chamber for proteolysis.
@en
P2093
Anne Frohn
Annelie Ståhl
B Martin Hallberg
Elzbieta Glaser
Kenneth A Johnson
Therese Eneqvist
P2860
P304
P356
10.1038/SJ.EMBOJ.7601080
P407
P577
2006-04-06T00:00:00Z