Beta2-microglobulin isoforms display an heterogeneous affinity for type I collagen.
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Conformational Conversion during Amyloid Formation at Atomic ResolutionDialysis-related amyloidosis: challenges and solutionsSystemic amyloidosis: lessons from β2-microglobulin.Transthyretin-derived amyloidosis: probably a common cause of lumbar spinal stenosis.Characterization of the response of primary cells relevant to dialysis-related amyloidosis to β2-microglobulin monomer and fibrils.Calcium binding to beta-2-microglobulin at physiological pH drives the occurrence of conformational changes which cause the protein to precipitate into amorphous forms that subsequently transform into amyloid aggregates.A simulated intermediate state for folding and aggregation provides insights into ΔN6 β2-microglobulin amyloidogenic behavior.Molecular dynamics simulation suggests possible interaction patterns at early steps of beta2-microglobulin aggregation.beta(2)-microglobulin: from physiology to amyloidosis.Understanding the complex mechanisms of β2-microglobulin amyloid assembly.Misfolding of amyloidogenic proteins and their interactions with membranes.A systematic molecular dynamics approach to the structural characterization of amyloid aggregation propensity of β2-microglobulin mutant D76N.Natively folded HypF-N and its early amyloid aggregates interact with phospholipid monolayers and destabilize supported phospholipid bilayers.Influence of heparin molecular size on the induction of C- terminal unfolding in β2-microglobulin.Protein folding and misfolding on surfaces.Heparin strongly enhances the formation of beta2-microglobulin amyloid fibrils in the presence of type I collagen.Detailed computational analysis revealed mutation V210I on PrP induced conformational conversion on β2-α2 loop and α2-α3.Collagen plays an active role in the aggregation of beta2-microglobulin under physiopathological conditions of dialysis-related amyloidosisKnee osteoarthritis associated with different kinds of amyloid deposits and the impact of aging on type of amyloidC-terminal unfolding of an amyloidogenicβ2-microglobulin fragment:ΔN6β2-microglobulin
P2860
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P2860
Beta2-microglobulin isoforms display an heterogeneous affinity for type I collagen.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
2005年论文
@zh
2005年论文
@zh-cn
name
Beta2-microglobulin isoforms display an heterogeneous affinity for type I collagen.
@en
type
label
Beta2-microglobulin isoforms display an heterogeneous affinity for type I collagen.
@en
prefLabel
Beta2-microglobulin isoforms display an heterogeneous affinity for type I collagen.
@en
P2093
P2860
P356
P1433
P1476
Beta2-microglobulin isoforms display an heterogeneous affinity for type I collagen.
@en
P2093
Antonio Rossi
Gennaro Esposito
Giuseppe Cetta
Monica Stoppini
Palma Mangione
Paolo Viglino
Sara Marini
Sara Raimondi
Sofia Giorgetti
Vittorio Bellotti
P2860
P304
P356
10.1110/PS.041194005
P577
2005-02-02T00:00:00Z