about
Clusterin is an ATP-independent chaperone with very broad substrate specificity that stabilizes stressed proteins in a folding-competent stateThe thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compoundsStructural investigation of the hedamycin:d(ACCGGT)2 complex by NMR and restrained molecular dynamicsThe structured core domain of B-crystallin can prevent amyloid fibrillation and associated toxicityMeasurement of amyloid formation by turbidity assay-seeing through the cloudAmyloid-β oligomers are sequestered by both intracellular and extracellular chaperonesThe elusive role of the N-terminal extension of βA3- and βAl-crystallinSingle molecule characterization of the interactions between amyloid-β peptides and the membranes of hippocampal cells.Maculatin 1.1, an anti-microbial peptide from the Australian tree frog, Litoria genimaculata solution structure and biological activity.RNA-LIM: a novel procedure for analyzing protein/single-stranded RNA propensity data with concomitant estimation of interface structure.The solution structure of frenatin 3, a neuronal nitric oxide synthase inhibitor from the giant tree frog, Litoria infrafrenata.Carboxymethylated-kappa-casein: a convenient tool for the identification of polyphenolic inhibitors of amyloid fibril formation.The mammalian small heat-shock protein Hsp20 forms dimers and is a poor chaperone.Site-directed mutations in the C-terminal extension of human alphaB-crystallin affect chaperone function and block amyloid fibril formationProbing the structure and interactions of crystallin proteins by NMR spectroscopy.A quantitative NMR spectroscopic examination of the flexibility of the C-terminal extensions of the molecular chaperones, αA- and αB-crystallin.The interaction of alphaB-crystallin with mature alpha-synuclein amyloid fibrils inhibits their elongation.The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2.Small heat-shock proteins interact with a flanking domain to suppress polyglutamine aggregation.Gallic acid is the major component of grape seed extract that inhibits amyloid fibril formation.Gallic acid interacts with α-synuclein to prevent the structural collapse necessary for its aggregation.NMR identification of a partial helical conformation for bombesin in solution.αB-Crystallin inhibits the cell toxicity associated with amyloid fibril formation by κ-casein and the amyloid-β peptide.Monitoring the prevention of amyloid fibril formation by alpha-crystallin. Temperature dependence and the nature of the aggregating species.Unraveling the mysteries of protein folding and misfolding.A multi-pathway perspective on protein aggregation: implications for control of the rate and extent of amyloid formation.Binding of the molecular chaperone αB-crystallin to Aβ amyloid fibrils inhibits fibril elongationSmall heat-shock proteins and clusterin: intra- and extracellular molecular chaperones with a common mechanism of action and function?Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance.The quaternary organization and dynamics of the molecular chaperone HSP26 are thermally regulated.Monitoring the interaction between β2-microglobulin and the molecular chaperone αB-crystallin by NMR and mass spectrometry: αB-crystallin dissociates β2-microglobulin oligomers.Crystallin proteins and amyloid fibrils.Invited review: Caseins and the casein micelle: their biological functions, structures, and behavior in foods.Preventing α-synuclein aggregation: the role of the small heat-shock molecular chaperone proteins.Small heat-shock proteins: important players in regulating cellular proteostasis.Evidence that clusterin has discrete chaperone and ligand binding sites.The growing world of small heat shock proteins: from structure to functions.Dissociation from the oligomeric state is the rate-limiting step in fibril formation by kappa-casein.Recognizing and analyzing variability in amyloid formation kinetics: Simulation and statistical methods.The Effect of Milk Constituents and Crowding Agents on Amyloid Fibril Formation by κ-Casein.
P50
Q24290651-1FE8AC67-49AA-4117-B8D5-2BBD18308DC0Q24316146-0EC55AB0-54E0-4B64-9103-B94BF705CCB0Q27637542-48AE9CFC-1355-445C-8AA9-114E378AA60CQ27683083-6004817C-5275-44B2-B117-ECFB834D695BQ28080287-2375ABB5-8771-4EF5-931E-D7E781D02F16Q28771766-EC31A3E4-E2AE-491C-9D74-B41729F068E8Q29010752-B787A136-2E64-4AD7-BDCC-2234C57EBBD0Q30533868-18595712-ABF0-41FF-9010-3BC30EF04F0AQ30587692-F1C90AC4-AE0C-4124-9817-A02A477A9832Q30874832-E18CC019-262D-4384-9613-AF577422916AQ30882861-0F36EB7F-4C71-46F6-836F-0D008E753060Q30909484-723613AB-6D82-46C8-B5A6-D0726D3BA815Q31903510-EB60D6DF-3772-4792-869F-A1B0009725EEQ33302904-E30B4617-CF3E-4E5C-9778-4270228132BFQ33601863-85E8C661-1589-4EFB-82E0-3D36D373A40DQ33669731-A5D1A9B0-32C8-4906-97D3-E1F45F7EB575Q33696177-6A89C86C-FBBB-417A-B8F9-2E69FE237103Q33914643-A24CDF08-3272-43BA-8086-61B6062C3CB2Q33935094-11B1D441-EB16-448B-A72E-E2B2BBCAD675Q34038668-1AF0A254-E6F5-44EB-8755-66772780F062Q34040737-8B15D95E-7160-4638-B33F-6D5ACB8FDC48Q34431802-7622C8BD-CC2A-4246-830B-5AD6B77C8014Q34505802-2C7F433B-72AF-4003-AA7D-8F3ED4D24E30Q34713919-D32B7587-9506-4AE4-B729-5BDCE5F063FDQ34820123-FC6599BF-9E31-4DE0-ABD8-C33756EE4C34Q35146724-F8E3159C-EB6E-409F-8520-5F2AEE878131Q35246361-9EC805FF-021B-463E-A5AA-0AF934E88A6FQ35652185-9EB6AA06-2116-4760-92ED-47BAA41E3EF4Q35808887-B68C4D58-C262-442F-A82D-BC6D27CB06C1Q36072725-CDD789BD-5126-42A4-84E5-52F36AAF1B57Q36929132-74820108-7933-4C38-94EB-4862ECC85BB4Q37276684-039DA788-7DD5-46E9-8CD5-F0789EBA341BQ38129972-F899A69B-036B-4CC4-BD20-71879DAD2535Q38224023-C9D6B7F7-EF12-47CA-B578-4E2CB542583BQ38263437-88ECAE3B-E945-4B66-932E-940D16E01224Q38293431-9B951426-917C-425C-87B0-B167536636A6Q39212393-1AE70FDA-AA19-46D5-87FA-1071011CE2FAQ39260487-9C92560C-0A25-482C-85FF-F5143CDC798AQ39588302-AED7C4DE-F989-4BDB-B8E9-DB55ABBF7DB9Q40065327-99E1AAF2-E666-4952-9888-6C03A31606D5
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
John A Carver
@ast
John A Carver
@en
John A Carver
@es
John A Carver
@nl
John A Carver
@sl
type
label
John A Carver
@ast
John A Carver
@en
John A Carver
@es
John A Carver
@nl
John A Carver
@sl
altLabel
John A. Carver
@en
prefLabel
John A Carver
@ast
John A Carver
@en
John A Carver
@es
John A Carver
@nl
John A Carver
@sl
P1053
J-3825-2014
P106
P21
P31
P3829
P496
0000-0002-2441-8108