Recombinant immunoglobulin variable domains generated from synthetic genes provide a system for in vitro characterization of light-chain amyloid proteins.
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Amyloid formation in light chain amyloidosisChange in dimerization mode by removal of a single unsatisfied polar residue located at the interfaceIncreasing protein stability by polar surface residues: domain-wide consequences of interactions within a loop.Factors contributing to decreased protein stability when aspartic acid residues are in β-sheet regionsAltered Dimer Interface Decreases Stability in an Amyloidogenic ProteinStructural Insights into the Role of Mutations in AmyloidogenesisKinetic Control in Protein Folding for Light Chain Amyloidosis and the Differential Effects of Somatic MutationsBiologic and genetic characterization of the novel amyloidogenic lambda light chain-secreting human cell lines, ALMC-1 and ALMC-2.Structural relationship of kappa-type light chains with AL amyloidosis: multiple deletions found in a VkappaIV protein.A kinetic study of beta-lactoglobulin amyloid fibril formation promoted by urea.Mysterious oligomerization of the amyloidogenic proteinsSite-directed mutagenesis reveals regions implicated in the stability and fiber formation of human λ3r light chainsComplete primary sequences of two lambda immunoglobulin light chains in myelomas with nonamyloid (Randall-type) light chain deposition disease.Molecular anatomy and the pathological expression of antibody light chains.The pathogenesis and diagnosis of acute kidney injury in multiple myeloma.Light chain-associated amyloid deposits comprised of a novel kappa constant domainPhysicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains.Differential recruitment efficacy of patient-derived amyloidogenic and myeloma light chain proteins by synthetic fibrils-A metric for predicting amyloid propensity.Hsp70 and antifibrillogenic peptides promote degradation and inhibit intracellular aggregation of amyloidogenic light chains.Monitoring the assembly of Ig light-chain amyloid fibrils by atomic force microscopy.The effect of membranes on the in vitro fibrillation of an amyloidogenic light-chain variable-domain SMA.Effect of methionine oxidation on the structural properties, conformational stability, and aggregation of immunoglobulin light chain LEN.Light chain amyloidosis - current findings and future prospects.Systemic amyloidoses.Heat-induced native dimerization prevents amyloid formation by variable domain from immunoglobulin light-chain REI.Aggregation of Full-length Immunoglobulin Light Chains from Systemic Light Chain Amyloidosis (AL) Patients Is Remodeled by Epigallocatechin-3-gallate.Binding of nascent collagen by amyloidogenic light chains and amyloid fibrillogenesis in monolayers of human fibrocytes.MAK33 antibody light chain amyloid fibrils are similar to oligomeric precursors.Effect of amino acid mutations on the conformational dynamics of amyloidogenic immunoglobulin light-chains: A combined NMR and in silico study.The effects of sodium sulfate, glycosaminoglycans, and Congo red on the structure, stability, and amyloid formation of an immunoglobulin light-chain protein.Aggregates, crystals, gels, and amyloids: intracellular and extracellular phenotypes at the crossroads of immunoglobulin physicochemical property and cell physiology.Counteracting effects of renal solutes on amyloid fibril formation by immunoglobulin light chains.Effect of association state and conformational stability on the kinetics of immunoglobulin light chain amyloid fibril formation at physiological pH.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.Surface-catalyzed amyloid fibril formation.A model for amyloid fibril formation in immunoglobulin light chains based on comparison of amyloidogenic and benign proteins and specific antibody binding.Elucidation of the molecular mechanism during the early events in immunoglobulin light chain amyloid fibrillation. Evidence for an off-pathway oligomer at acidic pH.Congo red populates partially unfolded states of an amyloidogenic protein to enhance aggregation and amyloid fibril formation.Structure and energetic basis of overrepresented λ light chain in systemic light chain amyloidosis patients.Four structural risk factors identify most fibril-forming kappa light chains
P2860
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P2860
Recombinant immunoglobulin variable domains generated from synthetic genes provide a system for in vitro characterization of light-chain amyloid proteins.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
1995年學術文章
@zh
1995年學術文章
@zh-hant
name
Recombinant immunoglobulin var ...... light-chain amyloid proteins.
@ast
Recombinant immunoglobulin var ...... light-chain amyloid proteins.
@en
type
label
Recombinant immunoglobulin var ...... light-chain amyloid proteins.
@ast
Recombinant immunoglobulin var ...... light-chain amyloid proteins.
@en
prefLabel
Recombinant immunoglobulin var ...... light-chain amyloid proteins.
@ast
Recombinant immunoglobulin var ...... light-chain amyloid proteins.
@en
P2093
P2860
P356
P1433
P1476
Recombinant immunoglobulin var ...... light-chain amyloid proteins.
@en
P2093
D K Hanson
F A Westholm
M Berrios-Hammond
P W Stevens
P2860
P304
P356
10.1002/PRO.5560040309
P577
1995-03-01T00:00:00Z