JMB-HEADER RAS-JOURNALS EIMB Pleiades Publishing

RUS

             

ENG

YearIMPACT-FACTOR
2022  1,200
2021  1,540
2020  1,374
2019  1,023
2018  0,932
2017  0,977
2016  0,799
2015  0,662
2014  0,740
2013  0,739
2012  0,637
2011  0,658
2010  0,654
2009  0,570
2008  0,849
2007  0,805
2006  0,330
2005  0,435
2004  0,623
2003  0,567
2002  0,641
2001  0,490
2000  0,477
1999  0,762
1998  0,785
1997  0,507
1996  0,518
1995  0,502
Vol 42(2008) N 5 p. 710-719;
L.N. Mironova1, A.I. Goginashvili1, M.D. Ter-Avanesyan2

Biological functions of amyloids: Facts and hypotheses

1Department of Genetics and Breeding, St. Petersburg State University, St. Petersburg, 199034, Russia
2Russian Cardiology Research and Production Complex, Moscow, 121552, Russia
Received - 2008-02-07; Accepted - 2008-02-07

Amyloids are fibrous protein aggregates that arise via polymerization of proteins with their concurrent conformational rearrangement and the formation of a specific cross-β structure. Amyloids are of particular interest as a cause of a vast group of human and animal diseases called amyloidoses. Some of these diseases are caused by prions, a specific type of amyloids, and are transmissible. Apart from mammals, prion amyloids are described in lower eukaryotes, where they act as nonchromosomal genetic determinants. Although amyloids are usually associated with pathologies in humans and animals, the increasing number of findings suggests that the acquisition of an amyloid or prion form by a protein is of biological significance in some cases. The review summarizes the data on the biological significance of prion and nonprion amyloids in a wide range of species from bacteria to mammals.

Amyloids, mammalian prions, yeast prions, mammalian amyloidoses, protein-based inheritance, functions of amyloids



JMB-FOOTER RAS-JOURNALS