(Q33302124)

25 July 2017

title

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

1 reference

25 July 2017

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Sergey Leikin

2

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author name string

Elena Makareeva

series ordinal

1

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25 July 2017

language of work or name

English

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publication date

10 October 2007

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25 July 2017

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25 July 2017

volume

2

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25 July 2017

issue

10

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25 July 2017

page(s)

e1029

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Creative Commons CC0 License

25 July 2017

copyright license

start time

10 October 2007

1 reference

April 2022 Public Data File from Crossref

copyright status

copyrighted, dedicated to the public domain by copyright holder

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cites work

Is SPARC an evolutionarily conserved collagen chaperone?

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Prolyl 3-hydroxylase 1 deficiency causes a recessive metabolic bone disorder resembling lethal/severe osteogenesis imperfecta

14 July 2018

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Deficiency of cartilage-associated protein in recessive lethal osteogenesis imperfecta

14 July 2018

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Consortium for osteogenesis imperfecta mutations in the helical domain of type I collagen: regions rich in lethal mutations align with collagen binding sites for integrins and proteoglycans.

14 July 2018

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CRTAP is required for prolyl 3- hydroxylation and mutations cause recessive osteogenesis imperfecta

14 July 2018

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How can biochemical reactions within cells differ from those in test tubes?

14 July 2018

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Protein aggregation in crowded environments.

14 July 2018

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

14 July 2018

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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

14 July 2018

1 reference

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Hsp47 a novel collagen binding serpin chaperone, autoantigen and therapeutic target.

14 July 2018

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Pathways of chaperone-mediated protein folding in the cytosol

14 July 2018

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Prolyl 3-hydroxylase 1, enzyme characterization and identification of a novel family of enzymes

14 July 2018

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14 July 2018

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Protein folding by the effects of macromolecular crowding

14 July 2018

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Mapping Hsp47 binding site(s) using CNBr peptides derived from type I and type II collagen

14 July 2018

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Unstable molecules form stable tissues

14 July 2018

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Type I collagen is thermally unstable at body temperature

14 July 2018

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Folding defects in fibrillar collagens

14 July 2018

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Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell

14 July 2018

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

14 July 2018

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Hsp47: a molecular chaperone that interacts with and stabilizes correctly-folded procollagen

14 July 2018

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Procollagen folding and assembly: the role of endoplasmic reticulum enzymes and molecular chaperones

14 July 2018

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Chaperone-mediated protein folding

14 July 2018

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The endoplasmic reticulum Ca2+ store: a view from the lumen

14 July 2018

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The effect of macromolecular crowding on chaperonin-mediated protein folding

14 July 2018

1 reference

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Intracellular interaction of collagen-specific stress protein HSP47 with newly synthesized procollagen

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2000351

Two collagen-binding proteins, osteonectin and HSP47, are coordinately induced in transformed keratinocytes by heat and other stresses

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2000351

Interaction of procollagen I and other collagens with colligin

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2000351

Collagens: molecular biology, diseases, and potentials for therapy

14 July 2018

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Cell surface-associated proteins which bind native type IV collagen or gelatin.

14 July 2018

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2000351

Renaturation of disulfide-linked procollagen.

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2000351

Mutations in collagen genes: causes of rare and some common diseases in humans

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2000351

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

14 July 2018

1 reference

https://api.crossref.org/works/10.1371%2FJOURNAL.PONE.0001029

The kinetics of the thermal denaturation of collagen in unrestrained rat tail tendon determined by differential scanning calorimetry.

21 January 2018

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https://api.crossref.org/works/10.1371%2FJOURNAL.PONE.0001029

Type I collagen triplet duplication mutation in lethal osteogenesis imperfecta shifts register of alpha chains throughout the helix and disrupts incorporation of mutant helices into fibrils and extracellular matrix

21 January 2018

1 reference

https://api.crossref.org/works/10.1371%2FJOURNAL.PONE.0001029

Formation of the triple helix of type I procollagen in cellulo. Temperature-dependent kinetics support a model based on cis in equilibrium trans isomerization of peptide bonds.

21 January 2018

1 reference

https://api.crossref.org/works/10.1371%2FJOURNAL.PONE.0001029

Procollagen is more stable in cellulo than in vitro.

21 January 2018

1 reference

https://api.crossref.org/works/10.1371%2FJOURNAL.PONE.0001029

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1371%2FJOURNAL.PONE.0001029

Efficacy of macromolecular crowding in forcing proteins to fold

21 January 2018

1 reference

https://api.crossref.org/works/10.1371%2FJOURNAL.PONE.0001029

Molecular mechanism of alpha 1(I)-osteogenesis imperfecta/Ehlers-Danlos syndrome: unfolding of an N-anchor domain at the N-terminal end of the type I collagen triple helix

21 January 2018

1 reference

https://api.crossref.org/works/10.1371%2FJOURNAL.PONE.0001029

Y-position cysteine substitution in type I collagen (alpha1(I) R888C/p.R1066C) is associated with osteogenesis imperfecta/Ehlers-Danlos syndrome phenotype.

21 January 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2000351

The influence of peptidyl-prolyl cis-trans isomerase on the in vitro folding of type III collagen.

31 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2000351

Procollagen Traverses the Golgi Stack without Leaving the Lumen of Cisternae

31 October 2018

1 reference

https://api.crossref.org/works/10.1371%2FJOURNAL.PONE.0001029

Proteolytic enzymes as probes for the triple-helical conformation of procollagen

21 January 2018

1 reference

12 December 2020

Isolation of unhydroxylated type I procollagen folding of the protein in vitro

1 reference

12 December 2020

Endoplasmic reticulum contains a common, abundant calcium-binding glycoprotein, endoplasmin

1 reference

12 December 2020

Thermal stability and folding of type IV procollagen and effect of peptidyl-prolyl cis-trans-isomerase on the folding of the triple helix

1 reference

12 December 2020

Self-assembly into fibrils of a homotrimer of type I collagen

1 reference

12 December 2020

Triple helix formation of procollagen type I can occur at the rough endoplasmic reticulum membrane

1 reference

12 December 2020

Mutations Near Amino End of α1(I) Collagen Cause Combined Osteogenesis Imperfecta/Ehlers-Danlos Syndrome by Interference with N-propeptide Processing

1 reference

12 December 2020

Chaperone-like activity revealed in the matricellular protein SPARC

1 reference

12 December 2020

Mixed macromolecular crowding accelerates the refolding of rabbit muscle creatine kinase: implications for protein folding in physiological environments

1 reference

12 December 2020

Introduction: molecular chaperones of the ER: their role in protein folding and genetic disease

1 reference

12 December 2020

HSP47 binds cooperatively to triple helical type I collagen but has little effect on the thermal stability or rate of refolding

1 reference

12 December 2020

10.1371/JOURNAL.PONE.0001029

Identifiers

DOI

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25 July 2017

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25 July 2017

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