Effects of in vivo conditions on amyloid aggregation

J 2019

Effects of in vivo conditions on amyloid aggregation

OWEN, Michael Christopher, D. GNUTT, M.M. GAO, S.K.T.S. WARMLANDER, J. JARVET et. al.

Základní údaje

Originální název

Effects of in vivo conditions on amyloid aggregation

Autoři

OWEN, Michael Christopher (124 Kanada, garant, domácí), D. GNUTT, M.M. GAO, S.K.T.S. WARMLANDER, J. JARVET, A. GRASLUND, R. WINTER, S. EBBINGHAUS a B. STRODEL

Vydání

Chemical Society Reviews, Cambridge, RSC Publishing, 2019, 0306-0012

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10403 Physical chemistry

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 42.846

Kód RIV

RIV/00216224:14740/19:00113279

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1039/c8cs00034d

UT WoS

000475647600006

Klíčová slova anglicky

SINGLE-MOLECULE SPECTROSCOPY; A-BETA PEPTIDE; RECEPTOR-RELATED PROTEIN-1; ALZHEIMERS-DISEASE BRAIN

Štítky

rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 31. 3. 2020 21:33, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

One of the grand challenges of biophysical chemistry is to understand the principles that govern protein misfolding and aggregation, which is a highly complex process that is sensitive to initial conditions, operates on a huge range of length- and timescales, and has products that range from protein dimers to macroscopic amyloid fibrils. Aberrant aggregation is associated with more than 25 diseases, which include Alzheimer's, Parkinson's, Huntington's, and type II diabetes. Amyloid aggregation has been extensively studied in the test tube, therefore under conditions that are far from physiological relevance. Hence, there is dire need to extend these investigations to in vivo conditions where amyloid formation is affected by a myriad of biochemical interactions. As a hallmark of neurodegenerative diseases, these interactions need to be understood in detail to develop novel therapeutic interventions, as millions of people globally suffer from neurodegenerative disorders and type II diabetes. The aim of this review is to document the progress in the research on amyloid formation from a physicochemical perspective with a special focus on the physiological factors influencing the aggregation of the amyloid-beta peptide, the islet amyloid polypeptide, alpha-synuclein, and the hungingtin protein.

Citovat

OWEN, Michael Christopher, D. GNUTT, M.M. GAO, S.K.T.S. WARMLANDER, J. JARVET, A. GRASLUND, R. WINTER, S. EBBINGHAUS a B. STRODEL. Effects of in vivo conditions on amyloid aggregation. Chemical Society Reviews. Cambridge: RSC Publishing, 2019, roč. 48, č. 14, s. 3946-3996. ISSN 0306-0012. Dostupné z: https://dx.doi.org/10.1039/c8cs00034d.

@article{1636680,
   author = {Owen, Michael Christopher and Gnutt, D. and Gao, M.M. and Warmlander, S.K.T.S. and Jarvet, J. and Graslund, A. and Winter, R. and Ebbinghaus, S. and Strodel, B.},
   article_location = {Cambridge},
   article_number = {14},
   doi = {http://dx.doi.org/10.1039/c8cs00034d},
   keywords = {SINGLE-MOLECULE SPECTROSCOPY; A-BETA PEPTIDE; RECEPTOR-RELATED PROTEIN-1; ALZHEIMERS-DISEASE BRAIN},
   language = {eng},
   issn = {0306-0012},
   journal = {Chemical Society Reviews},
   title = {Effects of in vivo conditions on amyloid aggregation},
   url = {http://dx.doi.org/10.1039/c8cs00034d},
   volume = {48},
   year = {2019}
}

TY  - JOUR
ID  - 1636680
AU  - Owen, Michael Christopher - Gnutt, D. - Gao, M.M. - Warmlander, S.K.T.S. - Jarvet, J. - Graslund, A. - Winter, R. - Ebbinghaus, S. - Strodel, B.
PY  - 2019
TI  - Effects of in vivo conditions on amyloid aggregation
JF  - Chemical Society Reviews
VL  - 48
IS  - 14
SP  - 3946-3996
EP  - 3946-3996
PB  - RSC Publishing
SN  - 03060012
KW  - SINGLE-MOLECULE SPECTROSCOPY
KW  - A-BETA PEPTIDE
KW  - RECEPTOR-RELATED PROTEIN-1
KW  - ALZHEIMERS-DISEASE BRAIN
UR  - http://dx.doi.org/10.1039/c8cs00034d
L2  - http://dx.doi.org/10.1039/c8cs00034d
N2  - One of the grand challenges of biophysical chemistry is to understand the principles that govern protein misfolding and aggregation, which is a highly complex process that is sensitive to initial conditions, operates on a huge range of length- and timescales, and has products that range from protein dimers to macroscopic amyloid fibrils. Aberrant aggregation is associated with more than 25 diseases, which include Alzheimer's, Parkinson's, Huntington's, and type II diabetes. Amyloid aggregation has been extensively studied in the test tube, therefore under conditions that are far from physiological relevance. Hence, there is dire need to extend these investigations to in vivo conditions where amyloid formation is affected by a myriad of biochemical interactions. As a hallmark of neurodegenerative diseases, these interactions need to be understood in detail to develop novel therapeutic interventions, as millions of people globally suffer from neurodegenerative disorders and type II diabetes. The aim of this review is to document the progress in the research on amyloid formation from a physicochemical perspective with a special focus on the physiological factors influencing the aggregation of the amyloid-beta peptide, the islet amyloid polypeptide, alpha-synuclein, and the hungingtin protein.
ER  -

OWEN, Michael Christopher, D. GNUTT, M.M. GAO, S.K.T.S. WARMLANDER, J. JARVET, A. GRASLUND, R. WINTER, S. EBBINGHAUS a B. STRODEL. Effects of in vivo conditions on amyloid aggregation. \textit{Chemical Society Reviews}. Cambridge: RSC Publishing, 2019, roč.~48, č.~14, s.~3946-3996. ISSN~0306-0012. Dostupné z: https://dx.doi.org/10.1039/c8cs00034d.

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