(Q48182955)

9 February 2018

title

Fibrillogenic oligomers of human cystatin C are formed by propagated domain swapping. (English)

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9 February 2018

Mariusz Jaskolski

5

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Anders Grubb

object named as

Anders Grubb

6

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author name string

Maria Wahlbom

1

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9 February 2018

Xin Wang

2

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9 February 2018

Veronica Lindström

3

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9 February 2018

Eric Carlemalm

4

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9 February 2018

language of work or name

English

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publication date

29 April 2007

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9 February 2018

Journal of Biological Chemistry

published in

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9 February 2018

volume

282

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9 February 2018

issue

25

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9 February 2018

page(s)

18318-18326

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9 February 2018

Diseases of protein conformation: what do in vitro experiments tell us about in vivo diseases?

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Human cystatin C, an amyloidogenic protein, dimerizes through three-dimensional domain swapping

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Domain swapping in N-truncated human cystatin C.

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Domain swapping: entangling alliances between proteins

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Crystal structure of the human prion protein reveals a mechanism for oligomerization

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Oligomeric assembly of native-like precursors precedes amyloid formation by beta-2 microglobulin

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An amyloid-forming segment of beta2-microglobulin suggests a molecular model for the fibril

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Increased body temperature accelerates aggregation of the Leu-68-->Gln mutant cystatin C, the amyloid-forming protein in hereditary cystatin C amyloid angiopathy.

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Two stable unfolding intermediates of the disease-causing L68Q variant of human cystatin C.

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21 January 2018

Identifiers

DOI

10.1074/JBC.M611368200

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9 February 2018

PubMed ID

17470433

1 reference

9 February 2018