Search Results - "Bobylev, Alexander G"

Congo Red and amyloids: history and relationship by Yakupova, Elmira I, Bobyleva, Liya G, Vikhlyantsev, Ivan M, Bobylev, Alexander G

“…Staining with Congo Red (CR) is a qualitative method used for the identification of amyloids and in tissue sections. However, the drawbacks and artefacts…”
Get full text

Accumulation of storage proteins in plant seeds is mediated by amyloid formation by Antonets, Kirill S, Belousov, Mikhail V, Sulatskaya, Anna I, Belousova, Maria E, Kosolapova, Anastasiia O, Sulatsky, Maksim I, Andreeva, Elena A, Zykin, Pavel A, Malovichko, Yury V, Shtark, Oksana Y, Lykholay, Anna N, Volkov, Kirill V, Kuznetsova, Irina M, Turoverov, Konstantin K, Kochetkova, Elena Y, Bobylev, Alexander G, Usachev, Konstantin S, Demidov, Oleg N, Tikhonovich, Igor A, Nizhnikov, Anton A

“…Amyloids are protein aggregates with a highly ordered spatial structure giving them unique physicochemical properties. Different amyloids not only participate…”
Get full text

OmpC and OmpF Outer Membrane Proteins of Escherichia coli and Salmonella enterica Form Bona Fide Amyloids by Belousov, Mikhail V., Kosolapova, Anastasiia O., Fayoud, Haidar, Sulatsky, Maksim I., Sulatskaya, Anna I., Romanenko, Maria N., Bobylev, Alexander G., Antonets, Kirill S., Nizhnikov, Anton A.

“…Outer membrane proteins (Omps) of Gram-negative bacteria represent porins involved in a wide range of virulence- and pathogenesis-related cellular processes,…”
Get full text

Amyloid Aggregates of Smooth-Muscle Titin Impair Cell Adhesion by Bobylev, Alexander G, Fadeev, Roman S, Bobyleva, Liya G, Kobyakova, Margarita I, Shlyapnikov, Yuri M, Popov, Daniil V, Vikhlyantsev, Ivan M

“…Various amyloid aggregates, in particular, aggregates of amyloid β-proteins, demonstrate in vitro and in vivo cytotoxic effects associated with impairment of…”
Get full text

β-Barrels and Amyloids: Structural Transitions, Biological Functions, and Pathogenesis by Sulatskaya, Anna I, Kosolapova, Anastasiia O, Bobylev, Alexander G, Belousov, Mikhail V, Antonets, Kirill S, Sulatsky, Maksim I, Kuznetsova, Irina M, Turoverov, Konstantin K, Stepanenko, Olesya V, Nizhnikov, Anton A

“…Insoluble protein aggregates with fibrillar morphology called amyloids and β-barrel proteins both share a β-sheet-rich structure. Correctly folded β-barrel…”
Get full text

Human RAD51 Protein Forms Amyloid-like Aggregates In Vitro by Kachkin, Daniel V., Volkov, Kirill V., Sopova, Julia V., Bobylev, Alexander G., Fedotov, Sergei A., Inge-Vechtomov, Sergei G., Galzitskaya, Oxana V., Chernoff, Yury O., Rubel, Aleksandr A., Aksenova, Anna Y.

“…RAD51 is a central protein of homologous recombination and DNA repair processes that maintains genome stability and ensures the accurate repair of…”
Get full text

Amyloids: The History of Toxicity and Functionality by Yakupova, Elmira I., Bobyleva, Liya G., Shumeyko, Sergey A., Vikhlyantsev, Ivan M., Bobylev, Alexander G.

“…Proteins can perform their specific function due to their molecular structure. Partial or complete unfolding of the polypeptide chain may lead to the…”
Get full text

RopB protein of Rhizobium leguminosarum bv. viciae adopts amyloid state during symbiotic interactions with pea (Pisum sativum L.) by Kosolapova, Anastasiia O., Belousov, Mikhail V., Sulatsky, Maksim I., Tsyganova, Anna V., Sulatskaya, Anna I., Bobylev, Alexander G., Shtark, Oksana Y., Tsyganov, Viktor E., Volkov, Kirill V., Zhukov, Vladimir A., Tikhonovich, Igor A., Nizhnikov, Anton A.

“…Amyloids represent protein aggregates with highly ordered fibrillar structure associated with the development of various disorders in humans and animals and…”
Get full text

Nonspecific Amyloid Aggregation of Chicken Smooth-Muscle Titin: In Vitro Investigations by Bobylev, Alexander G, Yakupova, Elmira I, Bobyleva, Liya G, Molochkov, Nikolay V, Timchenko, Alexander A, Timchenko, Maria A, Kihara, Hiroshi, Nikulin, Alexey D, Gabdulkhakov, Azat G, Melnik, Tatiana N, Penkov, Nikita V, Lobanov, Michail Y, Kazakov, Alexey S, Kellermayer, Miklós, Mártonfalvi, Zsolt, Galzitskaya, Oxana V, Vikhlyantsev, Ivan M

“…A giant multidomain protein of striated and smooth vertebrate muscles, titin, consists of tandems of immunoglobulin (Ig)- and fibronectin type III (FnIII)-like…”
Get full text

Myosin Binding Protein-C Forms Amyloid-Like Aggregates In Vitro by Bobyleva, Liya G, Shumeyko, Sergey A, Yakupova, Elmira I, Surin, Alexey K, Galzitskaya, Oxana V, Kihara, Hiroshi, Timchenko, Alexander A, Timchenko, Maria A, Penkov, Nikita V, Nikulin, Alexey D, Suvorina, Mariya Yu, Molochkov, Nikolay V, Lobanov, Mikhail Yu, Fadeev, Roman S, Vikhlyantsev, Ivan M, Bobylev, Alexander G

“…This work investigated in vitro aggregation and amyloid properties of skeletal myosin binding protein-C (sMyBP-C) interacting in vivo with proteins of thick…”
Get full text

Anti-amyloid activities of three different types of water-soluble fullerene derivatives by Bobylev, Alexander G., Kraevaya, Olga A., Bobyleva, Liya G., Khakina, Ekaterina A., Fadeev, Roman S., Zhilenkov, Alexander V., Mishchenko, Denis V., Penkov, Nikita V., Teplov, Ilia Y., Yakupova, Elmira I., Vikhlyantsev, Ivan M., Troshin, Pavel A.

“…[Display omitted] •Amphiphilic fullerene derivatives interact with Ab(1-42)-peptide and destroy amyloid fibrils.•Fullerene derivatives fully suppress toxic…”
Get full text

Increased Autolysis of μ‐Calpain in Skeletal Muscles of Chronic Alcohol‐Fed Rats by Gritsyna, Yulia V., Salmov, Nikolay N., Bobylev, Alexander G., Ulanova, Anna D., Kukushkin, Nikolay I., Podlubnaya, Zoya A., Vikhlyantsev, Ivan M.

“…Background Proteolysis can proceed via several distinct pathways such as the lysosomal, calcium‐dependent, and ubiquitin–proteasome‐dependent pathways…”
Get full text

Study of the complement activation by amyloid aggregates of smooth muscle titin in vitro by Yakupova, Elmira I., Bobylev, Alexander G., Bobyleva, Liya G., Vikhlyantsev, Ivan M.

“…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)…”
Get full text

Different amyloid aggregation of smooth muscles titin in vitro by Yakupova, Elmira I., Vikhlyantsev, Ivan M., Bobyleva, Liya G., Penkov, Nikita V., Timchenko, Alexander A., Timchenko, Maria A., Enin, Gennady A., Khutzian, Sergei S., Selivanova, Olga M., Bobylev, Alexander G.

“…A comparative study of amyloid properties of the aggregates of smooth muscle titin (SMT) from chicken gizzard was carried out. These aggregates were formed in…”
Get full text

Topological Structure of Smooth-Muscle TITIN Molecules and Oligomers by Yakupova, Elmira I., Vikhlyantsev, Ivan M., Bobylev, Alexander G., Mártonfalvi, Zsolt, Kellermayer, Miklós S.

Get full text

OmpC and OmpF Outer Membrane Proteins of IEscherichia coli/I and ISalmonella enterica/I Form IBona Fide/I Amyloids by Belousov, Mikhail V, Kosolapova, Anastasiia O, Fayoud, Haidar, Sulatsky, Maksim I, Sulatskaya, Anna I, Romanenko, Maria N, Bobylev, Alexander G, Antonets, Kirill S, Nizhnikov, Anton A

“…Outer membrane proteins (Omps) of Gram-negative bacteria represent porins involved in a wide range of virulence- and pathogenesis-related cellular processes,…”
Get full text