The 2.2 Å Crystal Structure of Hsp33 (Q57721635)

1

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Matthew K. Mukhergee

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Ursula Jakob

4

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Mark A. Saper

Hsp26: a temperature-regulated chaperone

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publication date

May 2001

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published in

Structure

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volume

9

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issue

5

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page(s)

367-375

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cites work

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Redox switch of hsp33 has a novel zinc-binding motif

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Mass spectrometry unravels disulfide bond formation as the mechanism that activates a molecular chaperone.

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Chaperone activity with a redox switch

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Activation of the Redox-Regulated Molecular Chaperone Hsp33—A Two-Step Mechanism

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Protein structure comparison by alignment of distance matrices

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The structure and function of the aspartic proteinases

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The structural basis for the oriented assembly of a TBP/TFB/promoter complex

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3D domain swapping: a mechanism for oligomer assembly

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Combining evolutionary information and neural networks to predict protein secondary structure

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The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity

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NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction

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Processing of X-ray diffraction data collected in oscillation mode

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Improved methods for building protein models in electron density maps and the location of errors in these models

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Improved Fourier coefficients for maps using phases from partial structures with errors

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

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Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

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SURFNET: a program for visualizing molecular surfaces, cavities, and intermolecular interactions

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