Proteomic analysis of the extracellular matrix in idiopathic pes equinovarus

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11110%2F15%3A10288178" target="_blank" >RIV/00216208:11110/15:10288178 - isvavai.cz</a>

Alternative codes found

RIV/67985823:_____/15:00447679 RIV/00216208:11130/15:10288178

Result on the web

<a href="http://dx.doi.org/10.1007/s11010-014-2300-3" target="_blank" >http://dx.doi.org/10.1007/s11010-014-2300-3</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s11010-014-2300-3" target="_blank" >10.1007/s11010-014-2300-3</a>

Result language

angličtina

Original language name

Proteomic analysis of the extracellular matrix in idiopathic pes equinovarus

Original language description

Idiopathic pes equinovarus is a congenital deformity of the foot and lower leg defined as a fixation of the foot in adduction, supination, and varus. Although the pathogenesis of clubfoot remains unclear, it has been suggested that fibroblasts and growthfactors are involved. To directly analyze the protein composition of the extracellular matrix in contracted tissue of patients with clubfoot. A total of 13 infants with idiopathic clubfoot treated with the Ponseti method were included in the present study. Tissue samples were obtained from patients undergoing surgery for relapsed clubfeet. Contracted tissues were obtained from the medial aspect of the talonavicular joint. Protein was extracted after digestion and delipidation using zip-tip C18. Individual collagenous fractions were detected using a chemiluminescent assay. Amino acid analysis of tissue samples revealed a predominance of collagens, namely collagen types I, III, and VI. The high content of glycine and h-proline suggests a

Czech name

—

Czech description

—

Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

FI - Traumatology and orthopaedics

OECD FORD branch

—

Project

<a href="/en/project/GA15-01948S" target="_blank" >GA15-01948S: Capillary electromigration techniques using affinity selectors & smart polymers for analysis and properties and interactions studies of biomolecules</a><br>

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2015

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Molecular and cellular biochemistry

ISSN

0300-8177

e-ISSN

—

Volume of the periodical

401

Issue of the periodical within the volume

1-2

Country of publishing house

NL - THE KINGDOM OF THE NETHERLANDS

Number of pages

7

Pages from-to

133-139

UT code for WoS article

000352848900013

EID of the result in the Scopus database

2-s2.0-84925496363