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Prions and Non-infectious Amyloids of Mammals – Similarities and Differences. / Galkin, A. P.; Velizhanina, M. E.; Sopova, Yu V.; Shenfeld, A. A.; Zadorsky, S. P.

In: Biochemistry (Moscow), Vol. 83, No. 10, 10.2018, p. 1184-1195.

Research output: Contribution to journal › Review article › peer-review

Harvard

Galkin, AP, Velizhanina, ME, Sopova, YV, Shenfeld, AA & Zadorsky, SP 2018, 'Prions and Non-infectious Amyloids of Mammals – Similarities and Differences', Biochemistry (Moscow), vol. 83, no. 10, pp. 1184-1195. https://doi.org/10.1134/S0006297918100048

APA

Galkin, A. P., Velizhanina, M. E., Sopova, Y. V., Shenfeld, A. A., & Zadorsky, S. P. (2018). Prions and Non-infectious Amyloids of Mammals – Similarities and Differences. Biochemistry (Moscow), 83(10), 1184-1195. https://doi.org/10.1134/S0006297918100048

Vancouver

Galkin AP, Velizhanina ME, Sopova YV, Shenfeld AA, Zadorsky SP. Prions and Non-infectious Amyloids of Mammals – Similarities and Differences. Biochemistry (Moscow). 2018 Oct;83(10):1184-1195. https://doi.org/10.1134/S0006297918100048

Author

Galkin, A. P. ; Velizhanina, M. E. ; Sopova, Yu V. ; Shenfeld, A. A. ; Zadorsky, S. P. / Prions and Non-infectious Amyloids of Mammals – Similarities and Differences. In: Biochemistry (Moscow). 2018 ; Vol. 83, No. 10. pp. 1184-1195.

BibTeX

@article{6d645c97edf34d21b023a48dd7f777e6,
title = "Prions and Non-infectious Amyloids of Mammals – Similarities and Differences",
abstract = "Amyloids are highly ordered aggregates of protein fibrils exhibiting cross-β structure formed by intermolecular hydrogen bonds. Pathological amyloid deposition is associated with the development of several socially significant incurable human diseases. Of particular interest are infectious amyloids, or prions, that cause several lethal neurodegenerative diseases in humans and can be transmitted from one organism to another. Because of almost complete absence of criteria for infectious and non-infectious amyloids, there is a lack of consensus, especially, in the definition of similarities and differences between prions and non-infectious amyloids. In this review, we formulated contemporary molecular-biological criteria for identification of prions and non-infectious amyloids and focused on explaining the differences between these two types of molecules.",
keywords = "amyloids, fibrils, infectivity, prions, protein aggregates, ALZHEIMERS-DISEASE, FUNCTIONAL PRION, SPONGIFORM ENCEPHALOPATHY, X-RAY-DIFFRACTION, AMYOTROPHIC-LATERAL-SCLEROSIS, PATHOLOGICAL ALPHA-SYNUCLEIN, LONG-TERM FACILITATION, SUPEROXIDE-DISMUTASE, HUNTINGTONS-DISEASE, PARKINSONS-DISEASE",
author = "Galkin, {A. P.} and Velizhanina, {M. E.} and Sopova, {Yu V.} and Shenfeld, {A. A.} and Zadorsky, {S. P.}",
year = "2018",
month = oct,
doi = "10.1134/S0006297918100048",
language = "English",
volume = "83",
pages = "1184--1195",
journal = "Biochemistry (Moscow)",
issn = "0006-2979",
publisher = "МАИК {"}Наука/Интерпериодика{"}",
number = "10",

}

RIS

TY - JOUR

T1 - Prions and Non-infectious Amyloids of Mammals – Similarities and Differences

AU - Galkin, A. P.

AU - Velizhanina, M. E.

AU - Sopova, Yu V.

AU - Shenfeld, A. A.

AU - Zadorsky, S. P.

PY - 2018/10

Y1 - 2018/10

N2 - Amyloids are highly ordered aggregates of protein fibrils exhibiting cross-β structure formed by intermolecular hydrogen bonds. Pathological amyloid deposition is associated with the development of several socially significant incurable human diseases. Of particular interest are infectious amyloids, or prions, that cause several lethal neurodegenerative diseases in humans and can be transmitted from one organism to another. Because of almost complete absence of criteria for infectious and non-infectious amyloids, there is a lack of consensus, especially, in the definition of similarities and differences between prions and non-infectious amyloids. In this review, we formulated contemporary molecular-biological criteria for identification of prions and non-infectious amyloids and focused on explaining the differences between these two types of molecules.

AB - Amyloids are highly ordered aggregates of protein fibrils exhibiting cross-β structure formed by intermolecular hydrogen bonds. Pathological amyloid deposition is associated with the development of several socially significant incurable human diseases. Of particular interest are infectious amyloids, or prions, that cause several lethal neurodegenerative diseases in humans and can be transmitted from one organism to another. Because of almost complete absence of criteria for infectious and non-infectious amyloids, there is a lack of consensus, especially, in the definition of similarities and differences between prions and non-infectious amyloids. In this review, we formulated contemporary molecular-biological criteria for identification of prions and non-infectious amyloids and focused on explaining the differences between these two types of molecules.

KW - amyloids

KW - fibrils

KW - infectivity

KW - prions

KW - protein aggregates

KW - ALZHEIMERS-DISEASE

KW - FUNCTIONAL PRION

KW - SPONGIFORM ENCEPHALOPATHY

KW - X-RAY-DIFFRACTION

KW - AMYOTROPHIC-LATERAL-SCLEROSIS

KW - PATHOLOGICAL ALPHA-SYNUCLEIN

KW - LONG-TERM FACILITATION

KW - SUPEROXIDE-DISMUTASE

KW - HUNTINGTONS-DISEASE

KW - PARKINSONS-DISEASE

UR - http://www.scopus.com/inward/record.url?scp=85055024370&partnerID=8YFLogxK

UR - http://link.springer.com/10.1134/S0006297918100048

UR - http://www.mendeley.com/research/prions-noninfectious-amyloids-mammals-similarities-differences

U2 - 10.1134/S0006297918100048

DO - 10.1134/S0006297918100048

M3 - Review article

AN - SCOPUS:85055024370

VL - 83

SP - 1184

EP - 1195

JO - Biochemistry (Moscow)

JF - Biochemistry (Moscow)

SN - 0006-2979

IS - 10

ER -

ID: 35479223