Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Emanuel Perugia"'
Publikováno v:
MRS Proceedings. 1422
We used atomic force microscope (AFM) to acquire high-resolution images of collagen type I triple-helices under ambient conditions in tapping mode. Angles between consecutive fixed-length segments were measured and analyzed to yield persistence lengt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::085ded59bb77a1ff58241dae81fd721a
https://doi.org/10.1557/opl.2012.107
https://doi.org/10.1557/opl.2012.107
Publikováno v:
Journal of the American Chemical Society. 132(12)
Amyloids are pathological fibrillar aggregates of proteins related to over 20 diseases. Amyloid fibers are characterized by the cross-beta motif, which is minimally defined as a series of beta-strands extended perpendicular to the fiber axis, joined
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca371c8108c470535e1f433307817070
https://pubmed.ncbi.nlm.nih.gov/20218685
https://pubmed.ncbi.nlm.nih.gov/20218685
Autor:
Arkady Bitler, Sidney R. Cohen, Emanuel Perugia, Inna Solomonov, Joseph P. R. O. Orgel, Hideaki Nagase, Robert Visse, Irit Sagi
Publikováno v:
Biophysical Journal. 98(3)
Collagen forms the main connective tissue in the body. Collagen turnover is intimately linked with healing of wounds, embryo development and tissue regeneration. Furthermore, the breakdown of collagen in various pathologies such as inflammatory arthr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d5207ad40c778f3221c5baa4f80dbf59
Publikováno v:
Advances in experimental medicine and biology. 611
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::1ee85a824cbca228b0f59bd13e458a0f
https://pubmed.ncbi.nlm.nih.gov/19400097
https://pubmed.ncbi.nlm.nih.gov/19400097
Publikováno v:
Advances in Experimental Medicine and Biology ISBN: 9780387736563
Introduction Serum amyloid A (SAA) is an acute phase protein associated with pathological amyloid deposits. The present study was aimed toward identification of the minimal amyloid-forming fragment of human SAA1 [1]. This information may lead to a be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a8795ef2b9c7f418d52af492772dd08e
https://doi.org/10.1007/978-0-387-73657-0_30
https://doi.org/10.1007/978-0-387-73657-0_30
Publikováno v:
Journal of the American Chemical Society. 130(14)
Amyloids are pathological fibrillar aggregates of proteins related to more than 20 different diseases. Amyloid fibers have a characteristic cross-beta structure consisting of a series of beta-strands extended perpendicular to the fiber axis and joine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64063fbc4bf70509758bdd9c251306e7
https://pubmed.ncbi.nlm.nih.gov/18338897
https://pubmed.ncbi.nlm.nih.gov/18338897