Effects of pH on aggregation kinetics of the repeat domain of a functional amyloid, Pmel17.
about
PMEL Amyloid Fibril Formation: The Bright Steps of PigmentationMelanocytes and their diseasesRapid generation of amyloid from native proteins in vitro.Molecular origin of pH-dependent fibril formation of a functional amyloidLysophospholipid-containing membranes modulate the fibril formation of the repeat domain of a human functional amyloid, pmel17.Unlocked concanavalin A forms amyloid-like fibrils from coagulation of long-lived "crinkled" intermediates.Toll-like receptor 2 and NLRP3 cooperate to recognize a functional bacterial amyloid, curliSegmental polymorphism in a functional amyloid.Probing fibril dissolution of the repeat domain of a functional amyloid, Pmel17, on the microscopic and residue levelBinding with nucleic acids or glycosaminoglycans converts soluble protein oligomers to amyloid.Insights into Kinetics of Agitation-Induced Aggregation of Hen Lysozyme under Heat and Acidic Conditions from Various Spectroscopic Methods.Seminal plasma accelerates semen-derived enhancer of viral infection (SEVI) fibril formation by the prostatic acid phosphatase (PAP248-286) peptide.Epithelial cells augment barrier function via activation of the Toll-like receptor 2/phosphatidylinositol 3-kinase pathway upon recognition of Salmonella enterica serovar Typhimurium curli fibrils in the gut.pH Induced Conformational Transitions in the Transforming Growth Factor β-Induced Protein (TGFβIp) Associated Corneal Dystrophy Mutants.PMEL: a pigment cell-specific model for functional amyloid formationCD14 protein acts as an adaptor molecule for the immune recognition of Salmonella curli fibers.Isolation, characterization, and aggregation of a structured bacterial matrix precursor.The PKD domain distinguishes the trafficking and amyloidogenic properties of the pigment cell protein PMEL and its homologue GPNMB.The yin and yang of amyloid: insights from α-synuclein and repeat domain of Pmel17Age-related carbonylation of fibrocartilage structural proteins drives tissue degenerative modification.Electrostatic unfolding and interactions of albumin driven by pH changes: a molecular dynamics study.Control of amyloid assembly by autoregulation.Mini-review: barnacle adhesives and adhesion.Study of Exosomes Shed New Light on Physiology of Amyloidogenesis.Amyloids, melanins and oxidative stress in melanomagenesis.A pH-dependent switch promotes β-synuclein fibril formation via glutamate residues.The impact of solubility and electrostatics on fibril formation by the H3 and H4 histones.Melanomagenesis: multifaceted attacks on the genome.Reversing the amyloid trend: Mechanism of fibril assembly and dissolution of the repeat domain from a human functional amyloid.Recent insights into the cellular and molecular determinants of aging.Identification of an amyloid fibril forming segment of human Pmel17 repeat domain (RPT domain).A β-solenoid model of the Pmel17 repeat domain: insights to the formation of functional amyloid fibrils.
P2860
Q28076932-369B0717-DE58-4B39-B3A4-C2E69DCCBEB3Q28658506-EB9EEA43-D43C-40F5-98C7-42821F711DA3Q33709292-AC82AEE4-A045-4E3C-A09C-47C69653B380Q34082608-A5E077B4-C980-4C67-AF69-9F7DC5639700Q34650262-B437FFFA-F3B0-411E-BC4C-0A010310C390Q34851754-FC4B571C-5691-4345-B471-009BC555E146Q34955574-84E946AE-1686-45CC-84DB-6A5D1D455918Q35512684-31F82074-BD82-46D2-800A-16216422AB77Q35597175-0A5D331C-6A69-4686-B31A-7417EDC69FB9Q35643865-70542216-F436-4D3E-982A-3F0866C04F18Q35842093-05F95162-269E-4B62-B41B-68E34142949CQ35874384-AE36DE06-7BDE-49C4-B5A5-09506E578FABQ36558731-DF5CEA5F-FC42-451D-81C9-7CD101C2DEC2Q36748354-EDA32F33-23EB-4C91-BB16-10DFEC586C82Q36788313-BE03F31A-A65A-4810-A2F2-7E0ACFCD1D03Q36850259-E56EC681-6E61-4240-BA1E-9052A7B4B33BQ36929038-71477BE2-49BA-4A4D-9C73-DC24D4DA3513Q36961713-1422BF73-2BE4-4D1C-88B6-1011E0C8E9BBQ37087338-A5257E37-9040-4355-B9CB-9295F336DF3AQ37136657-1AED0E00-ED23-491F-9AA3-D8F5AF84C1C0Q37697333-820AF447-11D5-4AA9-931D-6FB761B1C3EBQ38046670-BEE8F12F-99C5-442F-9FA7-7DD36C02A641Q38117193-EEC843F3-0DC9-475F-8536-08256F7015D6Q38777380-7C028EA7-F253-4636-9C6E-CD35DF85CDCAQ42089651-911A5210-90CE-4886-94B2-5807C6CD7607Q42285864-CEF803BA-4FF6-4BDB-8D21-5F9593E5D7A9Q42583698-D9E7EDFA-CA50-4378-8A4D-5AC58CDE9F2EQ46810960-5641C9A6-4B94-4F1D-9C1E-02E9E1CAD0E9Q47674191-F0E66887-A8A6-4C13-B119-97EAA701F3BBQ50115780-7851C083-8B4A-4632-9EBE-767082AE2979Q50436760-0183D6A9-81BA-43FC-A884-1601A9FBB0F3Q55059522-5E0D2992-D2B3-4EDE-9D8A-BD2A3CEBB01E
P2860
Effects of pH on aggregation kinetics of the repeat domain of a functional amyloid, Pmel17.
description
2010 nî lūn-bûn
@nan
2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի նոյեմբերին 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
Effects of pH on aggregation k ...... a functional amyloid, Pmel17.
@ast
Effects of pH on aggregation k ...... a functional amyloid, Pmel17.
@en
Effects of pH on aggregation k ...... a functional amyloid, Pmel17.
@nl
type
label
Effects of pH on aggregation k ...... a functional amyloid, Pmel17.
@ast
Effects of pH on aggregation k ...... a functional amyloid, Pmel17.
@en
Effects of pH on aggregation k ...... a functional amyloid, Pmel17.
@nl
prefLabel
Effects of pH on aggregation k ...... a functional amyloid, Pmel17.
@ast
Effects of pH on aggregation k ...... a functional amyloid, Pmel17.
@en
Effects of pH on aggregation k ...... a functional amyloid, Pmel17.
@nl
P2860
P356
P1476
Effects of pH on aggregation k ...... f a functional amyloid, Pmel17
@en
P2093
Candace M Pfefferkorn
Ryan P McGlinchey
P2860
P304
21447-21452
P356
10.1073/PNAS.1006424107
P407
P577
2010-11-24T00:00:00Z