Formation of amyloid fibrils from fully reduced hen egg white lysozyme.
about
Proinsulin is refractory to protein fibrillation: topological protection of a precursor protein from cross-beta assembly.Structural analysis of a helical peptide unfolding pathway.Simulation of two-dimensional ultraviolet spectroscopy of amyloid fibrils.Improving the Proteomic Analysis of Archival Tissue by Using Pressure-Assisted Protein Extraction: A Mechanistic Approach.Protein structural perturbation and aggregation on homogeneous surfaces.Antigen retrieval causes protein unfolding: evidence for a linear epitope model of recovered immunoreactivity.Anti-fibrillation propensity of a flavonoid baicalein against the fibrils of hen egg white lysozyme: potential therapeutics for lysozyme amyloidosis.Binding of lysozyme to phospholipid bilayers: evidence for protein aggregation upon membrane associationThe first step of hen egg white lysozyme fibrillation, irreversible partial unfolding, is a two-state transitionA common beta-sheet architecture underlies in vitro and in vivo beta2-microglobulin amyloid fibrilsGuiding protein aggregation with macromolecular crowdingBiosafety and bioapplication of nanomaterials by designing protein-nanoparticle interactions.Amphiphilic copolymers reduce aggregation of unfolded lysozyme more effectively than polyethylene glycol.Thermally induced fibrillar aggregation of hen egg white lysozyme.The effect of concentration, temperature and stirring on hen egg white lysozyme amyloid formation.Analysis of core region from egg white lysozyme forming amyloid fibrils.Amyloid formation in denatured single-mutant lysozymes where residual structures are modulated.Amyloid fibril formation can proceed from different conformations of a partially unfolded protein.A statistical-mechanical theory of fibril formation in dilute protein solutions.Towards lysozyme nanotube and 3D hybrid self-assembly.Global transition of human serum albumin to prefibrillar aggregates induced by temsirolimus: Insight into implications of anti-renal cancer drug.Photoinduced fibrils formation of chicken egg white lysozyme under native conditions.Modeling formalin fixation and histological processing with ribonuclease A: effects of ethanol dehydration on reversal of formaldehyde cross-links.Molecular dynamics simulations of lysozyme-lipid systems: probing the early steps of protein aggregation.How Do Gyrating Beads Accelerate Amyloid Fibrillization?Role of the Disulfide Bond in Prion Protein Amyloid Formation: A Thermodynamic and Kinetic Analysis.Appearance of annular ring-like intermediates during amyloid fibril formation from human serum albumin.Mechanistic insight of photo-induced aggregation of chicken egg white lysozyme: the interplay between hydrophobic interactions and formation of intermolecular disulfide bonds.Modulation of physiological and pathological activities of lysozyme by biological membranes.Self-assembly dynamics for the transition of a globular aggregate to a fibril network of lysozyme proteins via a coarse-grained Monte Carlo simulationThe extreme hyper-reactivity of Cys94 in lysozyme avoids its amorphous aggregation
P2860
Q33225633-4397F58F-4D35-46BC-8A4C-0D25A6046864Q33548401-DFF72C66-2D11-4378-A6B9-D617186A5366Q33675254-430F13B8-9B07-4A0D-8F1A-A98B43F03D19Q33919125-D6752D23-B71B-4CF7-BBCF-71ACED9142CEQ34188960-BD545D69-68E2-4DF0-A011-4BA601410EB1Q35440827-2DC22EB0-C2E2-4627-8692-A3A8411377CAQ35837281-1E3BA17D-351E-41E0-A7C2-D960FBB31348Q35881297-DAB42419-EADE-4BBF-B2D8-93D14492E747Q36393144-FEA8FBA3-9A51-4ABE-AC28-EBC21E2CD871Q36719294-C97C1D58-9BE9-477C-949C-E11B522ABA1DQ37178759-4A75415B-71CA-4863-B53F-8C4DEB3C309EQ38076084-D6E421B4-329B-4489-8A60-B677A0711EACQ38773864-BB6997DB-71DB-419F-9786-05992C32D892Q40312596-B295B2C5-608A-48F3-A704-94065C88073BQ40883999-885908D6-000C-4806-9858-26286F135722Q41855790-5F258AE3-CB97-4455-A50C-71A66C3692B7Q43043484-F91179A7-14FE-4B83-9527-67C9AEC294C4Q43203312-6154DE6C-1375-42AE-8899-C3EF35607AF2Q43221166-9828A7A6-77F7-4B7C-9378-149134A27C5DQ45791394-F3C8C46E-631F-4E45-8FA3-3D9246EC11EAQ46253683-05271844-A318-4DAC-A175-6DBD0300A1C3Q46375493-0DAD3183-A662-49A1-8542-42E10456AABDQ46587050-229B2830-5310-4A1B-AE71-55508249AF48Q50552522-9A1BA374-922E-4E23-87C0-50081085AA9AQ50932731-C850241D-AF6B-4A78-877E-C74BEA4577FDQ51746419-271DB388-82EB-46AE-916D-A4E4A7A49417Q51812569-71F3E7B6-B7D4-497E-B5B7-5F535C288A9CQ52612340-B1F6F074-42C3-4E8F-8541-D43DACCA2936Q52624824-9C93FD22-5673-4121-9E05-E54CC89612F4Q57436230-F8F23F58-6956-49C1-9AA2-1C9A3377321EQ58098877-31A1B6F1-92EC-4453-82BE-ADE3B6736C0D
P2860
Formation of amyloid fibrils from fully reduced hen egg white lysozyme.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
Formation of amyloid fibrils from fully reduced hen egg white lysozyme.
@ast
Formation of amyloid fibrils from fully reduced hen egg white lysozyme.
@en
type
label
Formation of amyloid fibrils from fully reduced hen egg white lysozyme.
@ast
Formation of amyloid fibrils from fully reduced hen egg white lysozyme.
@en
prefLabel
Formation of amyloid fibrils from fully reduced hen egg white lysozyme.
@ast
Formation of amyloid fibrils from fully reduced hen egg white lysozyme.
@en
P2093
P2860
P356
P1433
P1476
Formation of amyloid fibrils from fully reduced hen egg white lysozyme.
@en
P2093
P2860
P304
P356
10.1110/PS.03183404
P577
2004-01-10T00:00:00Z