Transthyretin slowly exchanges subunits under physiological conditions: A convenient chromatographic method to study subunit exchange in oligomeric proteins.
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Mechanism of Action and Clinical Application of Tafamidis in Hereditary Transthyretin AmyloidosisHuman-murine transthyretin heterotetramers are kinetically stable and non-amyloidogenic. A lesson in the generation of transgenic models of diseases involving oligomeric proteinsTafamidis, a potent and selective transthyretin kinetic stabilizer that inhibits the amyloid cascadeProteolytic cleavage of Ser52Pro variant transthyretin triggers its amyloid fibrillogenesisProgress in transthyretin fibrillogenesis research strengthens the amyloid hypothesis.The V122I cardiomyopathy variant of transthyretin increases the velocity of rate-limiting tetramer dissociation, resulting in accelerated amyloidosis.The relative amounts of plasma transthyretin forms in familial transthyretin amyloidosis: a quantitative analysis by Fourier transform ion-cyclotron resonance mass spectrometry.Genistein, a natural product from soy, is a potent inhibitor of transthyretin amyloidosisInitial conformational changes of human transthyretin under partially denaturing conditionsQuantification of quaternary structure stability in aggregation-prone proteins under physiological conditions: the transthyretin case.Recent progress in the understanding and treatment of transthyretin amyloidosis.Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity.Binding site asymmetry in human transthyretin: insights from a joint neutron and X-ray crystallographic analysis using perdeuterated proteinModulating inhibitors of transthyretin fibrillogenesis via sulfation: polychlorinated biphenyl sulfates as models.Determinants of homodimerization specificity in histidine kinases.Personalized medicine approach for optimizing the dose of tafamidis to potentially ameliorate wild-type transthyretin amyloidosis (cardiomyopathy).Involvement of Macrophages in the Pathogenesis of Familial Amyloid Polyneuropathy and Efficacy of Human iPS Cell-Derived Macrophages in Its TreatmentA novel mechano-enzymatic cleavage mechanism underlies transthyretin amyloidogenesis.Targeting protein aggregation for the treatment of degenerative diseasesSmall heat shock proteins and α-crystallins: dynamic proteins with flexible functions.Effect of multiple symmetries on the association of R67 DHFR subunits bearing interfacial complementing mutations.Quantification of the thermodynamically linked quaternary and tertiary structural stabilities of transthyretin and its disease-associated variants: the relationship between stability and amyloidosis.Peripheral Blood Cell Gene Expression Diagnostic for Identifying Symptomatic Transthyretin Amyloidosis Patients: Male and Female Specific Signatures.Induced pluripotent stem cell modeling of multisystemic, hereditary transthyretin amyloidosis.Quantification of transthyretin kinetic stability in human plasma using subunit exchange.The transthyretin amyloidoses: from delineating the molecular mechanism of aggregation linked to pathology to a regulatory-agency-approved drug.Properties of Bacillus cereus hemolysin II: a heptameric transmembrane pore.Current and future treatment of amyloid diseases.Allosteric regulation of DegS protease subunits through a shared energy landscape.How far can we go with structural mass spectrometry of protein complexes?Partitioning conformational intermediates between competing refolding and aggregation pathways: insights into transthyretin amyloid disease.Endoplasmic Reticulum Proteostasis Influences the Oligomeric State of an Amyloidogenic Protein Secreted from Mammalian CellsThermodynamic stability and denaturation kinetics of a benign natural transthyretin mutant identified in a Danish kindred.L55P transthyretin accelerates subunit exchange and leads to rapid formation of hybrid tetramers.Kinetic analysis of the multistep aggregation pathway of human transthyretinUnderstanding and Ameliorating the TTR AmyloidosesR104H may suppress transthyretin amyloidogenesis by thermodynamic stabilization, but not by the kinetic mechanism characterizing T119 interallelic trans-suppressionThermal shift assay for evaluation of transthyretin stability in plasmaSpectroscopic Investigations of Pentobarbital Interaction with Transthyretin
P2860
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P2860
Transthyretin slowly exchanges subunits under physiological conditions: A convenient chromatographic method to study subunit exchange in oligomeric proteins.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
2001年论文
@zh
2001年论文
@zh-cn
name
Transthyretin slowly exchanges ...... change in oligomeric proteins.
@ast
Transthyretin slowly exchanges ...... change in oligomeric proteins.
@en
type
label
Transthyretin slowly exchanges ...... change in oligomeric proteins.
@ast
Transthyretin slowly exchanges ...... change in oligomeric proteins.
@en
prefLabel
Transthyretin slowly exchanges ...... change in oligomeric proteins.
@ast
Transthyretin slowly exchanges ...... change in oligomeric proteins.
@en
P2860
P356
P1433
P1476
Transthyretin slowly exchanges ...... xchange in oligomeric proteins
@en
P2093
F Schneider
P2860
P304
P356
10.1110/PS.8901
P577
2001-08-01T00:00:00Z