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pro vyhledávání: '"Collagen helix"'
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Publikováno v:
Egyptian Rheumatologist, Vol 44, Iss 1, Pp 11-14 (2022)
Aim of the work: To assess serum collagen triple helix repeat containing 1 (CTHRC1) protein level in rheumatoid arthritis (RA) patients and compare it with healthy controls. In addition, to evaluate the relation of its level with RA activity and seve
Publikováno v:
Acta Biochimica et Biophysica Sinica. 53:805-814
Collagen is the main component of the extracellular matrix. Hydroxylation of proline residues on collagen, catalyzed by collagen prolyl 4-hydroxylase (C-P4H), is essential for the stability of the collagen triple helix. Vertebrate C-P4H is an α2β2
Autor:
Anis Hanna, Linda Alex, Prasanth Balasubramanian, Arti V. Shinde, Ruoshui Li, Nikolaos G. Frangogiannis, Claudio Humeres
Publikováno v:
Matrix Biol
Tissue injury results in profound alterations in the collagen network, associated with unfolding of the collagen triple helix, proteolytic degradation and generation of fragments. In the infarcted myocardium, changes in the collagen network are criti
Publikováno v:
Biomacromolecules. 22:2137-2147
There is a noted lack of understood, controllable interactions for directing the organization of collagen triple helices. While the field has had success using charge-pair interactions and cation-π interactions in helix design, these alone are not a
Autor:
I-Che Li, Jeffrey D. Hartgerink, Sarah A. H. Hulgan, Douglas R. Walker, Kevin J. Gonzalez, Caroline M. Peterson
Publikováno v:
Nature Chemistry. 13:260-269
Robust methods for predicting thermal stabilities of collagen triple helices are critical for understanding natural structure and stability in the collagen family of proteins and also for designing synthetic peptides mimicking these essential protein
Autor:
Szu-Huan Wang, Yi-Ting Sun, Chen-Hsu Yu, Yan-Chen Chen, Shu-Chuan Jao, Wei-Ming Wang, Ting-Hsuan Chen, Richard P. Cheng, Jing-Yuan Chang
Publikováno v:
Organic & Biomolecular Chemistry. 19:1860-1866
Collagen is a major structural component of the extracellular matrix and connective tissue. The key structural feature of collagen is the collagen triple helix, with a Xaa-Yaa-Gly (glycine) repeating pattern. The most frequently occurring triplet is
Autor:
Xabier Martinez de Morentin, Núria Planell, Juan P. Romero, Ming Wu, Paula García-Olloqui, Erika Lorenzo-Vivas, Stefan Janssens, David Gomez-Cabrero, Patxi San Martin-Uriz, Felipe Prosper, Gorka Bastarrika, David Lara-Astiaso, Miren Lasaga, Volkhard Lindner, Laura Castro-Labrador, Beatriz Pelacho, E. Iglesias, Igor Prudovsky, Sergey Ryzhov, Adrián Ruiz-Villalba, Diego Alignani, Yong-Ri Jin, Nikolaus Fortelny, Gema Medal, Amaia Vilas-Zornoza, Haifeng Yin, Silvia C. Hernandez, Juan José Gavira, Christoph Bock, Gloria Abizanda, Marcel Palacio
Publikováno v:
Circulation
Background: Cardiac fibroblasts (CFs) have a central role in the ventricular remodeling process associated with different types of fibrosis. Recent studies have shown that fibroblasts do not respond homogeneously to heart injury. Because of the limit
Autor:
Szymon W. Manka, Keith Brew
Publikováno v:
Journal of Molecular Biology. 432:5985-5993
Local unwinding of the collagen triple helix is a necessary step for initiating the collagen degradation cascade in extracellular matrices. A few matrix metalloproteinases (MMPs) are known to support this key process, but its energetic aspects remain
Autor:
Ute Kolb, Galina Matveeva, Sebastian Bette, Jörg Stelzner, Thomas Schleid, Robert E. Dinnebier, Gerhard Eggert
Publikováno v:
Angewandte Chemie (International Ed. in English)
Helical motifs are common in nature, for example, the DNA double or the collagen triple helix. In the latter proteins, the helical motif originates from glycine, the smallest amino acid, whose molecular confirmation is closely related to acetic acid.