Michel van der Rest

École Normale Supérieure de Lyon

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Trends

Author Order

Document Type

Co-Authors

Bernard Dublet

Institut de Biologie et de Chimie des Protéines

Sylvie Ricard‐Blum

Institut de Chimie et Biochimie Moléculaires et Supramoléculaires

Francis H. Glorieux

Shriners Hospitals for Children - Canada

Björn R. Olsen

Harvard University

Marion K. Gordon

Rutgers, The State University of New Jersey

Richard Mayne

Medawar Building for Pathogen Research

Björn Olsén

Uppsala University

R. Garrone

Fairfield University

Y Ninomiya

National Institute of Informatics

E. Aubert‐Foucher

Centre National de la Recherche Scientifique

Cooperative Institutions

Centre National de la Recherche Scientifique

Institut de Biologie et de Chimie des Protéines

McGill University

Université Claude Bernard Lyon 1

Inserm

Harvard University

Weatherford College

Shriners Hospitals for Children - Canada

Rutgers, The State University of New Jersey

University of Pennsylvania

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Field

Mapping of a human fibrillar collagen gene, pro α1(XI) (COL11A1), to the p21 region of chromosome 1

Genomics (1988)

Isabelle Henry Alain Bernheim Michael P. Bernard Michel van der Rest Tomoatsu Kimura

Collagen VI

10.1016/0888-7543(88)90165-6

Cite

Citations (28)

Modules et interactions moléculaires et caractère modulaire des protéines au sein des matrices extracellulaires

médecine/sciences (1994)

Claire Giry-Lozinguez Jean-Philippe Kleman Michel van der Rest

De nombreuses proteines comportent des motifs homologues, appeles modules. Les macromolecules secretees, malgre leur grande diversite, sont construites a partir d'un nombre relativement restreint de modules differents. La modularite des proteines de la matrice extracellulaire est importante, tant par les assemblages supramoleculaires que par son role physiologique. Les modules peuvent, en effet, etre impliques a la fois dans la structure de ces proteines et dans les interactions qu'elles menagent entre elles ou avec des recepteurs cellulaires qui leur sont propres, ce qui contribue a la coherence des matrices extracellulaires. Les mutations affectant la structure d'un module et/ou la fonction qui peut lui etre associee sont a l'origine de plusieurs maladies hereditaires des matrices extracellulaires

10.4267/10608/2562

Cite

Citations (2)

Identification of the type IX collagen polypeptide chains. The alpha 2(IX) polypeptide carries the chondroitin sulfate chain(s).

Journal of Biological Chemistry (1986)

Susanne Huber Michel van der Rest Peter Brückner Elida Rodriguez Kaspar H. Winterhalter

Here we demonstrate that the chondroitin sulfate carrying 115-kDa polypeptide of type IX collagen corresponds to the a2(IX) chain.In addition the 84-and 68-kDa polypeptides were identified as the al(1X) and the a3(IX) chains, respectively.This conclusion is based on a comparison of the tryptic fingerprints of the 84-, 115-, and 68-kDa chains of type IX collagen on high performance liquid chromatography with the similarly treated C2, C3, and C5 chains of the peptic fragment HMW.In addition, we provide evidence that both the C3 and C4 components of HMW are derived from the a2(IX) chain.Avian type IX collagen was first isolated from peptic digests of chicken cartilage in the form of high and low molecular weight disulfide-linked fragments, designated either HMW and LMW (1) or M1 and M2 (2).Evidence that HMW and LMW were different sections of the same molecule was obtained initially by their release, through pepsin cleavage, from the intact precursor to type IX collagen (3) and definitively by a comparison of the amino acid sequences of their components with those deduced from the nucleotide sequence of the cDNA clone pYN 1738 (4,5).Based on these data, LMW could be located adjacent to a short noncollagenous domain at the carboxyl-terminal of the intact molecule and was found to be separated by a second noncollagenous domain of 30 amino acids from HMW.A third noncollagenous domain interrupted the triple helix of HMW and a fourth extended from HMW until the amino-terminal.It was also shown by protein structural studies of LMW and HMW that the three polypeptide chains were separate gene products, leading to * This work was partly

Chain (unit)

Alpha (finance)

Identification

Polypeptide chain

10.1016/s0021-9258(17)38478-8

Cite

Citations (62)

Absence of collagen deficiency in familial cerebral aneurysms

Journal of neurosurgery (1989)

Richard Leblanc Andrés M. Lozano Michel van der Rest Ronald D. Guttmann

✓ It has been suggested that a deficiency in the expression of type III collagen may play a role in the pathogenesis of cerebral aneurysms. To test this hypothesis in cases of familial cerebral aneurysms, fibroblast cell cultures were established and the expression of collagen types I and III was studied in a patient with three cerebral aneurysms whose mother and sister also had cerebral aneurysms. Cultured skin fibroblasts were labeled with tritiated proline. The collagens and procollagens were precipitated and run on sodium dodecyl sulfate-polyacrylamide gel electrophoresis after reduction to analyze procollagen chains. Control cell lines were analyzed simultaneously. Quantitation of the ratios of type III to type I procollagen synthesis was achieved by integration of the intensities of the pro- α 1 (III), pro- α 1(I), and pro- α 2(I) bands on fluorograms of electrophoretic gels of medium proteins. There was no difference in type I and III procollagen levels observed between the cells from the aneurysm patient and those from the control cell lines. These data do not support the hypothesis that familial cerebral aneurysms are caused by a deficiency of type III collagen.

10.3171/jns.1989.70.6.0837

Cite

Citations (51)

Cloning of the chicken α3(IX) collagen chain completes the primary structure of type IX collagen

European Journal of Biochemistry (1992)

Randolph G. Brewton Maia V. Ouspenskaia Michel van der Rest Richard Mayne

Type IX collagen is composed of three genetically distinct polypeptides that contain several collagenous and non-collagenous domains. The alpha 2(IX) chain also contains a covalently bound glycosaminoglycan side chain. Type IX collagen is located on the surface of collagen fibrils of both hyaline cartilage and vitreous humor, such that one of the collagenous domains (COL3) projects from the surface of the fibril in a periodic manner. We have cloned and sequenced a full-length cDNA for the chicken alpha 3(IX) collagen chain from a cartilage cDNA library. Together with the sequence of the alpha 1(IX) and alpha 2(IX) chains, this completes the primary structure of type IX collagen for one species. These sequences will be useful to better understand the mechanism of triple-helix formation in type IX collagen and the nature of type II and type IX collagen interactions in fibril formation.

Collagen VI

Collagen helix

Hyaline cartilage

Type II collagen

10.1111/j.1432-1033.1992.tb16798.x

Cite

Citations (30)

Cloning and Sequencing of α1(VIII) Collagen cDNAs

Annals of the New York Academy of Sciences (1990)

Noriko Yamaguchi Paul D. Benya Michel van der Rest Yoshifumi Ninomiya

General hospital

10.1111/j.1749-6632.1990.tb17952.x

Cite

Citations (0)

An immunological and electrophoretic study of Rhodospirillum rubrum chromatophore fragments

Archives of Biochemistry and Biophysics (1974)

Michel van der Rest Henri Noël Gabriel Gingras

Rhodospirillum rubrum

Sodium dodecyl sulfate

Molecular mass

10.1016/0003-9861(74)90033-2

Cite

Citations (9)

Structure and function of carotenoids in the photoreaction center from Rhodospirillum rubrum

Biochimica et Biophysica Acta (BBA) - Bioenergetics (1977)

François Boucher Michel van der Rest Gabriel Gingras

Rhodospirillum rubrum

Photoprotection

Intersystem crossing

Absorbance

10.1016/0005-2728(77)90224-9

Cite

Citations (103)

Structural Analysis of the Heparin-Binding Site of the NC1 Domain of Collagen XIV by CD and NMR^,

Biochemistry (1999)

Roland Montserret E. Aubert‐Foucher Michael J. McLeish Joanna M. Hill D. Ficheux

Type XIV collagen, a fibril-associated collagen with interrupted triple helices (FACIT), interacts with the surrounding extracellular matrix and/or with cells via its binding to glycosaminoglycans (GAGs). To further characterize such interactions in the NC1 domain of chicken collagen XIV, we identified amino acids essential for heparin binding by affinity chromatography analysis after proteolytic digestion of the synthetic peptide NC1(84−116). The 3D structure of this peptide was then obtained using circular dichroism and NMR. The NC1(84−116) peptide appeared poorly structured in water, but the stabilization of its conformation by the interaction with hydrophobic surfaces or by using cosolvents (TFE, SDS) revealed a high propensity to adopt an α-helical folding. A 3D structure model of NC1(84−116), calculated from NMR data recorded in a TFE/water mixture, showed that the NC1-heparin binding site forms a amphipathic α-helix exhibiting a twisted basic groove. It is structurally similar to the consensus spatial α-helix model of heparin-binding [Margalit et al. (1993) J. Biol. Chem. 268, 19228−19231], except that the GAG binding domain of NC1 may be extended over 18 residues, that is, the NC1(94−111) segment. In addition, the formation of a hydrophobic groove upon helix formation suggests the contribution of additional sequences to ensure the stability of the GAG-binding domain. Overall the NC1(84−116) model exhibits a nativelike conformation which presents suitably oriented residues for the interaction with a specific GAG.

10.1021/bi9900222

Cite

Citations (31)

Structure of the carboxyl propeptide of chicken type II procollagen determined by DNA and protein sequence analysis

Biochemistry (1984)

Yoshifumi Ninomiya Allan M. Showalter Michel van der Rest Nabil G. Seidah Michel Chrètien

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTStructure of the carboxyl propeptide of chicken type II procollagen determined by DNA and protein sequence analysisYoshifumi Ninomiya, Allan M. Showalter, Michel Van der Rest, Nabil G. Seidah, Michel Chretien, and Bjorn R. OlsenCite this: Biochemistry 1984, 23, 4, 617–624Publication Date (Print):February 14, 1984Publication History Published online1 May 2002Published inissue 14 February 1984https://pubs.acs.org/doi/10.1021/bi00299a005https://doi.org/10.1021/bi00299a005research-articleACS PublicationsRequest reuse permissionsArticle Views28Altmetric-Citations44LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts

Altmetrics

Procollagen peptidase

10.1021/bi00299a005

Cite

Citations (56)