Crystal structure of chaperone protein PapD reveals an immunoglobulin fold (Q27690139)

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English	Crystal structure of chaperone protein PapD reveals an immunoglobulin fold	scientific article

Statements

instance of

scholarly article

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title

Crystal structure of chaperone protein PapD reveals an immunoglobulin fold (English)

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main subject

crystal structure

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protein folding

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protein structure

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molecular chaperones

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author name string

A Holmgren

series ordinal

1

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C I Bränden

series ordinal

2

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language of work or name

English

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publication date

16 November 1989

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published in

Nature

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volume

342

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issue

6247

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page(s)

248-51

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cites work

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The PapG adhesin of uropathogenic Escherichia coli contains separate regions for receptor binding and for the incorporation into the pilus

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Preliminary X-ray study of papD crystals from uropathogenic Escherichia coli.

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The immunoglobulin superfamily--domains for cell surface recognition

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Comparison of super-secondary structures in proteins

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Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution

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The relation between the divergence of sequence and structure in proteins

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Similarity of three-dimensional structure between the immunoglobulin domain and the copper, zinc superoxide dismutase subunit

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Isolation of complementary DNA clones encoding the human lymphocyte glycoprotein T1/Leu-1

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Molecular cloning of Ly-1, a membrane glycoprotein of mouse T lymphocytes and a subset of B cells: molecular homology to its human counterpart Leu-1/T1 (CD5).

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A year in the life of the immunoglobulin superfamily

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Homologous plant and bacterial proteins chaperone oligomeric protein assembly

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A highly evolutionarily conserved mitochondrial protein is structurally related to the protein encoded by the Escherichia coli groEL gene

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GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli.

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Proteins as molecular chaperones.

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Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis

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Protein, DNA, and virus crystallography with a focused imaging proportional counter

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Identifiers

DOI

10.1038/342248A0

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stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1000455

Dimensions Publication ID

1042393413

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OpenCitations bibliographic resource ID

1000455

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1000455

PubMed publication ID

2478891

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1000455

 

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