Kinetics and energetics of assembly, nucleation, and growth of aggregates and fibrils for an amyloidogenic protein. Insights into transition states from pressure, temperature, and co-solute studies.

Kinetics and energetics of assembly, nucleation, and growth of aggregates and fibrils for an amyloidogenic protein. Insights into transition states from pressure, temperature, and co-solute studies.

Item
http://www.wikidata.org/entity/Q44002179
Understanding the relationship between biotherapeutic protein stability and solid-liquid interfacial shear in constant region mutants of IgG1 and IgG4Intrinsic fibrillation of fast-acting insulin analogs.The critical role of the constant region in thermal stability and aggregation of amyloidogenic immunoglobulin light chainIn vitro aggregation behavior of a non-amyloidogenic λ light chain dimer deriving from U266 multiple myeloma cells.Differential recruitment efficacy of patient-derived amyloidogenic and myeloma light chain proteins by synthetic fibrils-A metric for predicting amyloid propensity.Effects of sucrose on conformational equilibria and fluctuations within the native-state ensemble of proteinsPlasmodium falciparum merozoite surface protein 2 is unstructured and forms amyloid-like fibrilsThe (1-63) region of the p53 transactivation domain aggregates in vitro into cytotoxic amyloid assemblies.Pressure-accelerated dissociation of amyloid fibrils in wild-type hen lysozyme.Effect of amino acid mutations on the conformational dynamics of amyloidogenic immunoglobulin light-chains: A combined NMR and in silico study.Kinetic analysis of amyloid formation in the presence of heparan sulfate: faster unfolding and change of pathwayHigh-pressure studies of aggregation of recombinant human interleukin-1 receptor antagonist: thermodynamics, kinetics, and application to accelerated formulation studies.Multistep aggregation pathway of human interleukin-1 receptor antagonist: kinetic, structural, and morphological characterization.Trinucleotide expansions leading to an extended poly-L-alanine segment in the poly (A) binding protein PABPN1 cause fibril formation.Congo red populates partially unfolded states of an amyloidogenic protein to enhance aggregation and amyloid fibril formation.Role of osmolytes as chemical chaperones during the refolding of aminoacylase.
P2860

Kinetics and energetics of assembly, nucleation, and growth of aggregates and fibrils for an amyloidogenic protein. Insights into transition states from pressure, temperature, and co-solute studies.

Item
http://www.wikidata.org/entity/Q44002179
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh-hant
name
Kinetics and energetics of ass ...... rature, and co-solute studies.
@en
Kinetics and energetics of ass ...... rature, and co-solute studies.
@nl
type
label
Kinetics and energetics of ass ...... rature, and co-solute studies.
@en
Kinetics and energetics of ass ...... rature, and co-solute studies.
@nl
prefLabel
Kinetics and energetics of ass ...... rature, and co-solute studies.
@en
Kinetics and energetics of ass ...... rature, and co-solute studies.
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698
P356
P1433
P1476
Kinetics and energetics of ass ...... rature, and co-solute studies.
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698