TY - JOUR

T1 - Functional mammalian amyloids and amyloid-like proteins

AU - Rubel, Maria S.

AU - Fedotov, Sergey A.

AU - Grizel, Anastasia V.

AU - Sopova, Julia V.

AU - Malikova, Oksana A.

AU - Chernoff, Yury O.

AU - Rubel, Aleksandr A.

N1 - Rubel, M.S.; Fedotov, S.A.; Grizel, A.V.; Sopova, J.V.; Malikova, O.A.; Chernoff, Y.O.; Rubel, A.A. Functional Mammalian Amyloids and Amyloid-Like Proteins. Life 2020, 10, 156.

PY - 2020/9

Y1 - 2020/9

N2 - Amyloids are highly ordered fibrous cross-β protein aggregates that are notorious primarily because of association with a variety of incurable human and animal diseases (termed amyloidoses), including Alzheimer’s disease (AD), Parkinson’s disease (PD), type 2 diabetes (T2D), and prion diseases. Some amyloid-associated diseases, in particular T2D and AD, are widespread and affect hundreds of millions of people all over the world. However, recently it has become evident that many amyloids, termed “functional amyloids,” are involved in various activities that are beneficial to organisms. Functional amyloids were discovered in diverse taxa, ranging from bacteria to mammals. These amyloids are involved in vital biological functions such as long-term memory, storage of peptide hormones and scaffolding melanin polymerization in animals, substrate attachment, and biofilm formation in bacteria and fungi, etc. Thus, amyloids undoubtedly are playing important roles in biological and pathological processes. This review is focused on functional amyloids in mammals and summarizes approaches used for identifying new potentially amyloidogenic proteins and domains.

AB - Amyloids are highly ordered fibrous cross-β protein aggregates that are notorious primarily because of association with a variety of incurable human and animal diseases (termed amyloidoses), including Alzheimer’s disease (AD), Parkinson’s disease (PD), type 2 diabetes (T2D), and prion diseases. Some amyloid-associated diseases, in particular T2D and AD, are widespread and affect hundreds of millions of people all over the world. However, recently it has become evident that many amyloids, termed “functional amyloids,” are involved in various activities that are beneficial to organisms. Functional amyloids were discovered in diverse taxa, ranging from bacteria to mammals. These amyloids are involved in vital biological functions such as long-term memory, storage of peptide hormones and scaffolding melanin polymerization in animals, substrate attachment, and biofilm formation in bacteria and fungi, etc. Thus, amyloids undoubtedly are playing important roles in biological and pathological processes. This review is focused on functional amyloids in mammals and summarizes approaches used for identifying new potentially amyloidogenic proteins and domains.

KW - Amyloid screening

KW - FUNCTIONAL AMYLOIDS

KW - Protein aggregation

KW - Peptide hormone

KW - Memory

KW - Amyloid screening

KW - Functional amyloid

KW - Memory

KW - Peptide hormone

KW - Protein aggregation

KW - memory

KW - amyloid screening

KW - REPEAT DOMAIN

KW - MIXED LINEAGE KINASE

KW - peptide hormone

KW - functional amyloid

KW - PRION-LIKE AGGREGATION

KW - RNA-BINDING PROTEINS

KW - ZONA-PELLUCIDA

KW - MESSENGER-RNA

KW - protein aggregation

KW - DE-NOVO APPEARANCE

KW - MENTAL-RETARDATION PROTEIN

KW - MAJOR BASIC-PROTEIN

KW - STRESS GRANULES

UR - http://www.scopus.com/inward/record.url?scp=85090612409&partnerID=8YFLogxK

UR - https://www.mendeley.com/catalogue/8b57ef87-5e0a-39c3-af35-011ad34b8eee/

U2 - 10.3390/life10090156

DO - 10.3390/life10090156

M3 - Review article

AN - SCOPUS:85090612409

VL - 10

JO - Life

JF - Life

SN - 0024-3019

IS - 9

M1 - 156

ER -