Crystal structure of human cystatin C stabilized against amyloid formation (Q27659998)

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Karolina Michalska

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object named as

Karolina Michalska

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author name string

Robert Kolodziejczyk

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Alejandra Hernandez-Santoyo

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Maria Wahlbom

Nomenclature and classification of the proteins homologous with the cysteine-proteinase inhibitor chicken cystatin.

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language of work or name

English

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publication date

April 2010

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published in

FEBS Journal

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volume

277

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page(s)

1726-37

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issue

7

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cites work

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

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3D domain swapping: as domains continue to swap

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

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Runaway domain swapping in amyloid-like fibrils of T7 endonuclease I.

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

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Prevention of domain swapping inhibits dimerization and amyloid fibril formation of cystatin C: use of engineered disulfide bridges, antibodies, and carboxymethylpapain to stabilize the monomeric form of cystatin C.

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Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation

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Crystal structure of human cystatin D, a cysteine peptidase inhibitor with restricted inhibition profile

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Structural basis of reduction-dependent activation of human cystatin F.

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