Investigation of a peptide responsible for amyloid fibril formation of beta 2-microglobulin by achromobacter protease I.
about
Prediction of "hot spots" of aggregation in disease-linked polypeptidesAggregation properties of a short peptide that mediates amyloid fibril formation in model proteins unrelated to disease.Hexafluoroisopropanol induces amyloid fibrils of islet amyloid polypeptide by enhancing both hydrophobic and electrostatic interactions.Prediction of amyloidogenic and disordered regions in protein chainsDestruction of amyloid fibrils of a beta2-microglobulin fragment by laser beam irradiation.Molecular dynamics simulations to gain insights into the stability and morphologies of K3 oligomers from beta2-microglobulin.Amyloidogenic regions and interaction surfaces overlap in globular proteins related to conformational diseases.Antimicrobial protegrin-1 forms ion channels: molecular dynamic simulation, atomic force microscopy, and electrical conductance studiesStacked sets of parallel, in-register beta-strands of beta2-microglobulin in amyloid fibrils revealed by site-directed spin labeling and chemical labeling.Polymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape.In vitro amyloidogenic peptides of galectin-7: possible mechanism of amyloidogenesis of primary localized cutaneous amyloidosisInsufficiently dehydrated hydrogen bonds as determinants of protein interactionsA systematic screen of beta(2)-microglobulin and insulin for amyloid-like segmentsC-terminal sequence of amyloid-resistant type F apolipoprotein A-II inhibits amyloid fibril formation of apolipoprotein A-II in mice.Structural defects and the diagnosis of amyloidogenic propensity3D structure of amyloid protofilaments of beta2-microglobulin fragment probed by solid-state NMR.Structure and aggregation mechanism of beta(2)-microglobulin (83-99) peptides studied by molecular dynamics simulations.The beta-strand-loop-beta-strand conformation is marginally populated in beta2-microglobulin (20-41) peptide in solution as revealed by replica exchange molecular dynamics simulations.An amyloid-forming segment of beta2-microglobulin suggests a molecular model for the fibrilK3 fragment of amyloidogenic beta(2)-microglobulin forms ion channels: implication for dialysis related amyloidosis.Glimpses of the molecular mechanisms of beta2-microglobulin fibril formation in vitro: aggregation on a complex energy landscapebeta(2)-microglobulin: from physiology to amyloidosis.The role of disulfide bond in the amyloidogenic state of beta(2)-microglobulin studied by heteronuclear NMR.Chiral recognition in amyloid fiber growth.Increase in the conformational flexibility of beta 2-microglobulin upon copper binding: a possible role for copper in dialysis-related amyloidosis.Regions which are Responsible for Swapping are also Responsible for Folding and Misfolding.NMR-based characterization of a refolding intermediate of beta2-microglobulin labeled using a wheat germ cell-free system.Competition between intramolecular and intermolecular interactions in an amyloid-forming protein.Fibril growth kinetics reveal a region of beta2-microglobulin important for nucleation and elongation of aggregation.A comprehensive model for packing and hydration for amyloid fibrils of beta2-microglobulin.Conformation of beta 2-microglobulin amyloid fibrils analyzed by reduction of the disulfide bond.Amyloid fibril formation in the context of full-length protein: effects of proline mutations on the amyloid fibril formation of beta2-microglobulin.Conformational stability of amyloid fibrils of beta2-microglobulin probed by guanidine-hydrochloride-induced unfolding.Cationic surfactant mediated fibrillogenesis in bovine liver catalase: a biophysical approach.FoldAmyloid: a method of prediction of amyloidogenic regions from protein sequence.Covalent Tethering and Residues with Bulky Hydrophobic Side Chains Enable Self-Assembly of Distinct Amyloid Structures.Is it possible to predict amyloidogenic regions from sequence alone?Structures of a peptide fragment of beta2-microglobulin studied by replica-exchange molecular dynamics simulations - towards the understanding of the mechanism of amyloid formation.Effects of N-Methylated Amyloid-β30-40 Peptides on the Fibrillation of Amyloid-β1-40.Solvent environment conducive to protein aggregation
P2860
Q24815235-31933809-6EE0-4CBC-9FAF-5380EA817681Q30010250-689647EE-B858-416D-85A2-0EC692C1DAFFQ30502077-DC607439-9B5F-484D-BF00-0899FF3DFAB4Q33267899-283B5A60-56B4-4785-A635-A45EA4C13E0AQ33384559-1F2F5F12-0D18-47CF-A904-C97E904B187AQ33411468-204AED64-C800-4130-B66E-58290149E1C2Q33495551-B288E9A6-9E6C-4D7E-9CCF-5C1A82B327E1Q33880330-6F50918D-01FE-4229-A037-0CF088A5BE0AQ33883237-B3B7031C-8716-41F9-8E50-88A7C4830346Q34059772-063F8AB9-7006-4684-A3B7-45DA979B04F2Q34355760-9EA92674-B178-4BA7-BC63-6A7DB329966DQ34466734-6864EBD5-114B-4A5D-A687-A6E23F526021Q34572928-2C0C3DF3-3FBF-4E16-B4C4-3F04804E0162Q35134538-F1025997-7D75-4BFE-8078-C98298DF4807Q35143223-BD727748-5EDB-4785-8310-DFA3DBCE4461Q35722137-09D38875-A96A-429E-AD10-1E700E8B18A6Q36129094-FE34A903-B27C-4A34-B259-CD264E1D9EF6Q36737187-68B324F7-C2AB-47F8-A86B-B4274F9D9533Q36986109-8D0548BA-D30D-4325-A396-7BE522E25D73Q37435767-67590575-F39E-4840-A3BF-8BB984DC963BQ37477467-489513DF-473D-4CE9-A6D7-21235890E883Q37573510-008F93B2-971C-4CDA-95F7-63FBFFB4E21BQ38269751-7676E46E-8A6C-417E-B408-53F613432FD5Q38901646-06D9A1BD-F7A9-4CE1-BA3B-27254360BD21Q41849521-E70EB336-D0D2-4E50-B149-34141DAFD4A1Q41987667-E5B9C59E-0C3D-4409-BFC4-B3E70337AB67Q42635761-F989CAA1-B7E1-40AD-B877-C1A1A2F1AC71Q43076154-30DA805A-2D55-4582-8F6C-CE6A4E509537Q43197716-A632A92F-7693-4595-B144-6B6C0F348ED1Q43816033-DBC160D9-FB66-45E0-9723-FCD6B56D623EQ43954441-4A3102E8-4438-41C6-809B-72EC89DBEB3DQ44575256-93585F9B-9290-4D76-A8A9-12504E379E14Q45118972-740EEDB4-CB9E-4454-9356-624E2F165131Q46764330-1A77A866-1FF8-4301-80BE-B1E2BFFEFF3EQ48239540-F92A5EEC-420F-48B1-A4F7-E631B2744C7AQ48314753-2BDA3DD1-F1E0-44EA-B528-36E2C1B5C604Q51938449-FBCF5E78-D6AF-4054-AC14-2938EEEA7B40Q51963068-61E874FE-E4FC-4AE5-AED8-42049A126422Q52664757-A4040CE0-6985-44DF-BC50-A21EF720F34EQ56970608-4D222807-E041-48AC-9933-64A967796276
P2860
Investigation of a peptide responsible for amyloid fibril formation of beta 2-microglobulin by achromobacter protease I.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh-hant
name
Investigation of a peptide res ...... n by achromobacter protease I.
@en
Investigation of a peptide res ...... n by achromobacter protease I.
@nl
type
label
Investigation of a peptide res ...... n by achromobacter protease I.
@en
Investigation of a peptide res ...... n by achromobacter protease I.
@nl
prefLabel
Investigation of a peptide res ...... n by achromobacter protease I.
@en
Investigation of a peptide res ...... n by achromobacter protease I.
@nl
P2093
P2860
P356
P1476
Investigation of a peptide res ...... n by achromobacter protease I.
@en
P2093
Gennady V Kozhukh
Hironobu Naiki
Kazuhiro Hasegawa
Toru Kawakami
P2860
P304
P356
10.1074/JBC.M108753200
P407
P577
2001-10-30T00:00:00Z