A systematic investigation into the effect of protein destabilisation on beta 2-microglobulin amyloid formation (Q44512592)

3 December 2017

A systematic investigation into the effect of protein destabilisation on beta 2-microglobulin amyloid formation (English)

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3 December 2017

1

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3 December 2017

3

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3 December 2017

5

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3 December 2017

Margaret Sunde

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author name string

Susan Jones

series ordinal

2

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PubMed ID

12860118

3 December 2017

language of work or name

English

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publication date

1 July 2003

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Journal of Molecular Biology

3 December 2017

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3 December 2017

330

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3 December 2017

5

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3 December 2017

943-954

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Protein misfolding, evolution and disease

3 December 2017

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Amyloid fibrillogenesis: themes and variations

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Amyloid-fibril formation. Proposed mechanisms and relevance to conformational disease

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Amyloid fibril protein nomenclature -- 2002.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Amyloid fibrils from muscle myoglobin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

De novo designed peptide-based amyloid fibrils

7 January 2021

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https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

"Cross-beta" conformation in proteins.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

The structure of amyloid fibrils by electron microscopy and X-ray diffraction

7 January 2021

2 references

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

7 January 2021

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

inferred from DOI database lookup

7 January 2021

based on heuristic

[18] Quantification of β-sheet amyloid fibril structures with thioflavin T

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Partially unfolded states of beta(2)-microglobulin and amyloid formation in vitro

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Does the location of a mutation determine the ability to form amyloid fibrils?

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Designing conditions for in vitro formation of amyloid protofilaments and fibrils

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

A new form of amyloid protein associated with chronic hemodialysis was identified as beta 2-microglobulin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 A resolution

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Crystal structure of monomeric human -2-microglobulin reveals clues to its amyloidogenic properties

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Collagen-binding affinity of beta-2-microglobulin, a preprotein of hemodialysis-associated amyloidosis

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

beta 2-microglobulin can be refolded into a native state from ex vivo amyloid fibrils

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Beta(2)-microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Role of the single disulphide bond of beta(2)-microglobulin in amyloidosis in vitro

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Conformation of beta 2-microglobulin amyloid fibrils analyzed by reduction of the disulfide bond

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Structural properties of an amyloid precursor of beta(2)-microglobulin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

The role of disulfide bond in the amyloidogenic state of beta(2)-microglobulin studied by heteronuclear NMR.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Hierarchical assembly of beta2-microglobulin amyloid in vitro revealed by atomic force microscopy.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Removal of the N-terminal hexapeptide from human beta2-microglobulin facilitates protein aggregation and fibril formation

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Kidney dialysis-associated amyloidosis: a molecular role for copper in fiber formation

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

A partially structured species of beta 2-microglobulin is significantly populated under physiological conditions and involved in fibrillogenesis

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

The intrachain disulfide bond of beta(2)-microglobulin is not essential for the immunoglobulin fold at neutral pH, but is essential for amyloid fibril formation at acidic pH.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Amyloid-forming peptides from beta2-microglobulin-Insights into the mechanism of fibril formation in vitro.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Purification and complete amino acid sequence of novel beta 2-microglobulin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Detection of two partially structured species in the folding process of the amyloidogenic protein beta 2-microglobulin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Amyloid fibril formation by an SH3 domain

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

A role for destabilizing amino acid replacements in light-chain amyloidosis

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Physicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Probing the mechanism of insulin fibril formation with insulin mutants

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Formation of a copper specific binding site in non-native states of beta-2-microglobulin.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Both the environment and somatic mutations govern the aggregation pathway of pathogenic immunoglobulin light chain

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Conformational prerequisites for alpha-lactalbumin fibrillation

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Pathway complexity of prion protein assembly into amyloid

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Calculation of protein extinction coefficients from amino acid sequence data

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

The structure and stability of an HLA-A*0201/octameric tax peptide complex with an empty conserved peptide-N-terminal binding site

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900687-9

10.1016/S0022-2836(03)00687-9

7 January 2021

Identifiers

DOI

1 reference

release_32iugbucu5cxhf2zuvh3qnxjva

3 December 2017

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/32iugbucu5cxhf2zuvh3qnxjva

mapped directly with Wikidata item

24 November 2022

based on heuristic

PubMed ID

12860118

1 reference

PubMed ID

12860118