Engineering protein thermostability using a generic activity-independent biophysical screen inside the cell (Q27687991)

3

object named as

Henrik Engman

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Tobias Cornvik

7

object named as

Tobias Cornvik

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author name string

Ignacio Asial

1

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Yue Xiang Cheng

2

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Maria Dollhopf

4

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Binghuang Wu

A differential scanning calorimetric investigation of the domains of recombinant tissue plasminogen activator.

5

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language of work or name

English

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publication date

2013

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published in

Nature Communications

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volume

4

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page(s)

2901

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cites work

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A thermostable variant of fructose bisphosphate aldolase constructed by directed evolution also shows increased stability in organic solvents

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Engineering proteins for thermostability: the use of sequence alignments versus rational design and directed evolution

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Development of a stable freeze-dried formulation of recombinant human interleukin-1 receptor antagonist

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Multistep aggregation pathway of human interleukin-1 receptor antagonist: kinetic, structural, and morphological characterization

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A new cytokine-receptor binding mode revealed by the crystal structure of the IL-1 receptor with an antagonist

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Stability of human growth hormone: influence of methionine oxidation on thermal folding

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Generation of a highly stable, internalizing anti‐CD22 single‐chain Fv fragment for targeting non‐Hodgkin's lymphoma

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Screening for ligands using a generic and high-throughput light-scattering-based assay

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Biophysical characterization of structural properties and folding of interleukin-1 receptor antagonist

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