Molecular basis for the action of the collagen-specific chaperone Hsp47/SERPINH1 and its structure-specific client recognition (Q24616550)

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9 February 2020

title

Molecular basis for the action of the collagen-specific chaperone Hsp47/SERPINH1 and its structure-specific client recognition (English)

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9 February 2020

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2

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9 February 2020

Cord Drögemüller

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9 February 2020

author name string

Christine Widmer

1

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9 February 2020

Elena Brunstein

3

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9 February 2020

Sabrina Rosenbaum

4

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9 February 2020

Frank Zaucke

5

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9 February 2020

Ulrich Baumann

8

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Tosso Leeb

7

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9 February 2020

language of work or name

English

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publication date

30 July 2012

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Proceedings of the National Academy of Sciences of the United States of America

9 February 2020

published in

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9 February 2020

volume

109

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9 February 2020

issue

33

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page(s)

13243-13247

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Serpins flex their muscle: II. Structural insights into target peptidase recognition, polymerization, and transport functions

9 February 2020

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Homozygosity for a missense mutation in SERPINH1, which encodes the collagen chaperone protein HSP47, results in severe recessive osteogenesis imperfecta

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Embryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesis

7 April 2017

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Implications for collagen I chain registry from the structure of the collagen von Willebrand factor A3 domain complex

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7 April 2017

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Unique side chain conformation of a Leu residue in a triple-helical structure

7 April 2017

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Refinement of severely incomplete structures with maximum likelihood in BUSTER-TNT

7 April 2017

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Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin

7 April 2017

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7 April 2017

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Iterative model building, structure refinement and density modification with the PHENIX AutoBuild wizard

7 April 2017

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Conformational requirements of collagenous peptides for recognition by the chaperone protein HSP47

7 April 2017

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An efficient one-step site-directed and site-saturation mutagenesis protocol

7 April 2017

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Procollagen triple helix assembly: an unconventional chaperone-assisted folding paradigm

7 April 2017

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Type I collagen in Hsp47-null cells is aggregated in endoplasmic reticulum and deficient in N-propeptide processing and fibrillogenesis

27 September 2017

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Specific recognition of the collagen triple helix by chaperone HSP47. II. The HSP47-binding structural motif in collagens and related proteins

27 September 2017

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27 September 2017

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27 September 2017

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27 September 2017

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27 September 2017

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27 September 2017

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30 May 2018

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30 May 2018

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30 May 2018

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Specific recognition of the collagen triple helix by chaperone HSP47: minimal structural requirement and spatial molecular orientation

30 May 2018

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Sequence-specific recognition of collagen triple helices by the collagen-specific molecular chaperone HSP47.

21 January 2018

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Structure-function studies on hsp47: pH-dependent inhibition of collagen fibril formation in vitro

21 January 2018

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A new method for describing the helical conformation of collagen: dependence of the triple helical twist on amino acid sequence

21 January 2018

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Procollagen Traverses the Golgi Stack without Leaving the Lumen of Cisternae

21 January 2018

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Interactions between collagen-binding stress protein HSP47 and collagen. Analysis of kinetic parameters by surface plasmon resonance biosensor.

21 January 2018

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Folding mechanism of the triple helix in type-III collagen and type-III pN-collagen. Role of disulfide bridges and peptide bond isomerization

28 November 2018

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12 December 2020

A structure-activity relationship study elucidating the mechanism of sequence-specific collagen recognition by the chaperone HSP47

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12 December 2020

The collagen-specific molecular chaperone HSP47: is there a role in fibrosis?

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12 December 2020

Interaction of human alpha 1-proteinase inhibitor with chymotrypsinogen A and crystallization of a proteolytically modified alpha 1-proteinase inhibitor

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12 December 2020

Identifiers

DOI

10.1073/PNAS.1208072109

2 references

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22847422%20AND%20SRC:MED&resulttype=core&format=json

9 February 2020

ADS bibcode

2012PNAS..10913243W

0 references

1 reference

2 references

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22847422%20AND%20SRC:MED&resulttype=core&format=json

9 February 2020

2 references

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