Stable Level of Giant Sarcomeric Cytoskeletal Proteins in Striated Muscles of the Edible Dormouse Glis glis during Hibernation

Autor: N. M. Zakharova, Ivan M. Vikhlyantsev, Oleg Gusev, S. S. Popova, L. F. Nurullin, D. A. Yurshenas, G. R. Gazizova, I. R. Nigmetzyanov, N. N. Salmov, L. G. Bobyleva, O. V. Tyapkina, G. Z. Mikhailova

Publikováno v: Journal of Evolutionary Biochemistry and Physiology. 57:886-895

The changes in the content of the giant sarcomeric cytoskeletal proteins titin (3000–3700 kDa) and nebulin (770 kDa) in skeletal muscles (m. soleus, m. gastrocnemius), and titin in the left ventricular myocardium, as well as of the submembrane cyto

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::fb2db7fae6a945cf9eec318a9dc7fd0e
https://doi.org/10.1134/s0022093021040128

Complement System Activation by Amyloid Aggregates of Aβ(1-40) and Aβ(1-42) Peptides: Facts and Hypotheses

Autor: L. G. Bobyleva, A. G. Bobylev, Elmira I Yakupova, Ivan M. Vikhlyantsev

Publikováno v: Biophysics. 65:18-21

—Here, we consider the problem of the activation of the complement system by amyloid aggregates, in particular, amyloid fibrils of the Aβ(1-40) and Aβ(1-42) peptides found in the brain of patients with Alzheimer’s disease . In 1992, based on th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::e75f3df8378b2efa83b672d9b362b347
https://doi.org/10.1134/s000635092001025x

Study of the complement activation by amyloid aggregates of smooth muscle titin in vitro

Autor: L. G. Bobyleva, A. G. Bobylev, Ivan M. Vikhlyantsev, Elmira I Yakupova

Publikováno v: Journal of Immunoassay and Immunochemistry. 41:132-143

The giant muscle protein, titin, is the third most abundant protein in muscle (after myosin and actin). It was shown previously that smooth muscle titin (SMT) with a molecular mass of 500 kDa can form in vitro amorphous amyloid aggregates in two cond

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a32dd04a989c5ab6f762952e9fcda794
https://doi.org/10.1080/15321819.2019.1694943

On the Peculiarities of the Aggregation of Multidomain Muscle Proteins

Autor: N. N. Salmov, L. G. Bobyleva, A. D. Ulanova, Sergey A Shumeyko, Ivan M. Vikhlyantsev, Elmira I Yakupova, A. G. Bobylev, S. N. Udaltsov

Publikováno v: Biophysics. 64:667-670

—The hypothesis that formed the basis of this work has been made on our studies that have shown that giant multi-domain muscle proteins of the titin family (titin isoforms and myosin-binding protein C paralogs) form amyloid aggregates in vitro. We

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::fd25391bf79a60258d4a24ea4b8aa1f6
https://doi.org/10.1134/s0006350919050026

Amyloid Aggregates of Smooth-Muscle Titin Impair Cell Adhesion

Autor: Daniil V. Popov, Ivan M. Vikhlyantsev, A. G. Bobylev, M. I. Kobyakova, L. G. Bobyleva, Yuri M. Shlyapnikov, R. S. Fadeev

Publikováno v: International Journal of Molecular Sciences
Volume 22
Issue 9
International Journal of Molecular Sciences, Vol 22, Iss 4579, p 4579 (2021)

Various amyloid aggregates, in particular, aggregates of amyloid β-proteins, demonstrate in vitro and in vivo cytotoxic effects associated with impairment of cell adhesion. We investigated the effect of amyloid aggregates of smooth-muscle titin on s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf594bdf90eaa7c4a57a93682e5a6a81