(Q30164898)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12584201%20AND%20SRC:MED&resulttype=core&format=json

31 October 2019

title

Amyloid-like fibril formation in an all beta-barrel protein. Partially structured intermediate state(s) is a precursor for fibril formation (English)

1 reference

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31 October 2019

0 references

Suresh Thallapuranam Kumar

2

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31 October 2019

author name string

Sampath Srisailam

1

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31 October 2019

Dakshinamurthy Rajalingam

3

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31 October 2019

Karuppanan Muthusamy Kathir

4

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31 October 2019

Hwo-Shuenn Sheu

5

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31 October 2019

Fuh-Jyh Jan

6

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31 October 2019

Pei-Chi Chao

7

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31 October 2019

Chin Yu

8

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31 October 2019

language of work or name

English

0 references

publication date

12 February 2003

1 reference

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Journal of Biological Chemistry

31 October 2019

published in

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31 October 2019

volume

278

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31 October 2019

issue

20

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31 October 2019

page(s)

17701-17709

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Commitment to folded and aggregated states occurs late in interleukin-1 beta folding

31 October 2019

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Interactions between prion protein isoforms: the kiss of death?

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A kinetic study of beta-lactoglobulin amyloid fibril formation promoted by urea

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Heparin and other glycosaminoglycans stimulate the formation of amyloid fibrils from alpha-synuclein in vitro.

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

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Amyloid fibril formation by a helical cytochrome.

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Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain

21 January 2018

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

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

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Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

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Evidence for a partially folded intermediate in alpha-synuclein fibril formation

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

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

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Oligomerization of acidic fibroblast growth factor is not a prerequisite for its cell proliferation activity.

21 January 2018

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Circular dichroic analysis of protein conformation: inclusion of the beta-turns.

21 January 2018

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Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set

21 January 2018

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Kinetic partitioning of protein folding and aggregation.

21 January 2018

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Folding and aggregation are selectively influenced by the conformational preferences of the alpha-helices of muscle acylphosphatase.

21 January 2018

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Amyloid deposits and amyloidosis: the beta-fibrilloses (second of two parts).

21 January 2018

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A beta fibrillogenesis: kinetic parameters for fibril formation from congo red binding

21 January 2018

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21 January 2018

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Amyloid-like fibril formation in an all beta-barrel protein involves the formation of partially structured intermediate(s).

21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M300336200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12584201%20AND%20SRC:MED&resulttype=core&format=json

31 October 2019

1 reference