Protein aggregation: mechanisms and functional consequences

Gaetano Invernizzi; Elena Papaleo; Raimon Sabate; Salvador Ventura

doi:10.1016/j.biocel.2012.05.023

Protein aggregation: mechanisms and functional consequences

Gaetano Invernizzi, Elena Papaleo, Raimon Sabate, Salvador Ventura

91 Citationer (Scopus)

Abstract

Understanding the mechanisms underlying protein misfolding and aggregation has become a central issue in biology and medicine. Compelling evidence show that the formation of amyloid aggregates has a negative impact in cell function and is behind the most prevalent human degenerative disorders, including Alzheimer's Parkinson's and Huntington's diseases or type 2 diabetes. Surprisingly, the same type of macromolecular assembly is used for specialized functions by different organisms, from bacteria to human. Here we address the conformational properties of these aggregates, their formation pathways, their role in human diseases, their functional properties and how bioinformatics tools might be of help to study these protein assemblies.

Originalsprog	Engelsk
Tidsskrift	International Journal of Biochemistry & Cell Biology
Vol/bind	44
Udgave nummer	9
Sider (fra-til)	1541-1554
Antal sider	14
ISSN	1357-2725
DOI	https://doi.org/10.1016/j.biocel.2012.05.023
Status	Udgivet - sep. 2012
Udgivet eksternt	Ja

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10.1016/j.biocel.2012.05.023

Citationsformater

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abstract = "Understanding the mechanisms underlying protein misfolding and aggregation has become a central issue in biology and medicine. Compelling evidence show that the formation of amyloid aggregates has a negative impact in cell function and is behind the most prevalent human degenerative disorders, including Alzheimer's Parkinson's and Huntington's diseases or type 2 diabetes. Surprisingly, the same type of macromolecular assembly is used for specialized functions by different organisms, from bacteria to human. Here we address the conformational properties of these aggregates, their formation pathways, their role in human diseases, their functional properties and how bioinformatics tools might be of help to study these protein assemblies.",

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author = "Gaetano Invernizzi and Elena Papaleo and Raimon Sabate and Salvador Ventura",

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TY - JOUR

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T2 - mechanisms and functional consequences

AU - Invernizzi, Gaetano

AU - Papaleo, Elena

AU - Sabate, Raimon

AU - Ventura, Salvador

PY - 2012/9

Y1 - 2012/9

N2 - Understanding the mechanisms underlying protein misfolding and aggregation has become a central issue in biology and medicine. Compelling evidence show that the formation of amyloid aggregates has a negative impact in cell function and is behind the most prevalent human degenerative disorders, including Alzheimer's Parkinson's and Huntington's diseases or type 2 diabetes. Surprisingly, the same type of macromolecular assembly is used for specialized functions by different organisms, from bacteria to human. Here we address the conformational properties of these aggregates, their formation pathways, their role in human diseases, their functional properties and how bioinformatics tools might be of help to study these protein assemblies.

AB - Understanding the mechanisms underlying protein misfolding and aggregation has become a central issue in biology and medicine. Compelling evidence show that the formation of amyloid aggregates has a negative impact in cell function and is behind the most prevalent human degenerative disorders, including Alzheimer's Parkinson's and Huntington's diseases or type 2 diabetes. Surprisingly, the same type of macromolecular assembly is used for specialized functions by different organisms, from bacteria to human. Here we address the conformational properties of these aggregates, their formation pathways, their role in human diseases, their functional properties and how bioinformatics tools might be of help to study these protein assemblies.

KW - Amyloid

KW - Animals

KW - Disease

KW - Humans

KW - Models, Molecular

KW - Protein Conformation

KW - Protein Multimerization

KW - Proteins

U2 - 10.1016/j.biocel.2012.05.023

DO - 10.1016/j.biocel.2012.05.023

M3 - Journal article

SN - 1357-2725

VL - 44

SP - 1541

EP - 1554

JO - International Journal of Biochemistry & Cell Biology

JF - International Journal of Biochemistry & Cell Biology

IS - 9

ER -

Protein aggregation: mechanisms and functional consequences

Abstract

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