Protein stability and degradation in health and disease

Publikation: Bidrag til bog/antologi/rapport › Bidrag til bog/antologi › Forskning › fagfællebedømt

Standard

Protein stability and degradation in health and disease. / Clausen, Lene; Abildgaard, Amanda Bering; Gersing, Sarah K.; Stein, Amelie; Lindorff-Larsen, Kresten; Hartmann-Petersen, Rasmus.

Molecular Chaperones in Human Disorders. red. / Rossen Donev. Academic Press, 2019. s. 61-83 (Advances in Protein Chemistry and Structural Biology, Bind 114).

Publikation: Bidrag til bog/antologi/rapport › Bidrag til bog/antologi › Forskning › fagfællebedømt

Harvard

Clausen, L, Abildgaard, AB, Gersing, SK, Stein, A, Lindorff-Larsen, K & Hartmann-Petersen, R 2019, Protein stability and degradation in health and disease. i R Donev (red.), Molecular Chaperones in Human Disorders. Academic Press, Advances in Protein Chemistry and Structural Biology, bind 114, s. 61-83. https://doi.org/10.1016/bs.apcsb.2018.09.002

APA

Clausen, L., Abildgaard, A. B., Gersing, S. K., Stein, A., Lindorff-Larsen, K., & Hartmann-Petersen, R. (2019). Protein stability and degradation in health and disease. I R. Donev (red.), Molecular Chaperones in Human Disorders (s. 61-83). Academic Press. Advances in Protein Chemistry and Structural Biology Bind 114 https://doi.org/10.1016/bs.apcsb.2018.09.002

Vancouver

Clausen L, Abildgaard AB, Gersing SK, Stein A, Lindorff-Larsen K, Hartmann-Petersen R. Protein stability and degradation in health and disease. I Donev R, red., Molecular Chaperones in Human Disorders. Academic Press. 2019. s. 61-83. (Advances in Protein Chemistry and Structural Biology, Bind 114). https://doi.org/10.1016/bs.apcsb.2018.09.002

Author

Clausen, Lene ; Abildgaard, Amanda Bering ; Gersing, Sarah K. ; Stein, Amelie ; Lindorff-Larsen, Kresten ; Hartmann-Petersen, Rasmus. / Protein stability and degradation in health and disease. Molecular Chaperones in Human Disorders. red. / Rossen Donev. Academic Press, 2019. s. 61-83 (Advances in Protein Chemistry and Structural Biology, Bind 114).

Bibtex

@inbook{ee312fecdbb1492ba609900c6e511ea0,
title = "Protein stability and degradation in health and disease",
abstract = "The cellular proteome performs highly varied functions to sustain life. Since most of these functions require proteins to fold properly, they can be impaired by mutations that affect protein structure, leading to diseases such as Alzheimer's disease, cystic fibrosis, and Lynch syndrome. The cell has evolved an intricate protein quality control (PQC) system that includes degradation pathways and a multitude of molecular chaperones and co-chaperones, all working together to catalyze the refolding or removal of aberrant proteins. Thus, the PQC system limits the harmful consequences of dysfunctional proteins, including those arising from disease-causing mutations. This complex system is still not fully understood. In particular the structural and sequence motifs that, when exposed, trigger degradation of misfolded proteins are currently under investigation. Moreover, several attempts are being made to activate or inhibit parts of the PQC system as a treatment for diseases. Here, we briefly review the present knowledge on the PQC system and list current strategies that are employed to exploit the system in disease treatment.",
keywords = "Chaperone, Misfolding, Proteasome, Protein folding, Protein quality control, Ubiquitin",
author = "Lene Clausen and Abildgaard, {Amanda Bering} and Gersing, {Sarah K.} and Amelie Stein and Kresten Lindorff-Larsen and Rasmus Hartmann-Petersen",
year = "2019",
doi = "10.1016/bs.apcsb.2018.09.002",
language = "English",
isbn = "978-0-12-815557-8",
series = "Advances in Protein Chemistry and Structural Biology",
publisher = "Academic Press",
pages = "61--83",
editor = "Rossen Donev",
booktitle = "Molecular Chaperones in Human Disorders",
address = "United States",

}

RIS

TY - CHAP

T1 - Protein stability and degradation in health and disease

AU - Clausen, Lene

AU - Abildgaard, Amanda Bering

AU - Gersing, Sarah K.

AU - Stein, Amelie

AU - Lindorff-Larsen, Kresten

AU - Hartmann-Petersen, Rasmus

PY - 2019

Y1 - 2019

N2 - The cellular proteome performs highly varied functions to sustain life. Since most of these functions require proteins to fold properly, they can be impaired by mutations that affect protein structure, leading to diseases such as Alzheimer's disease, cystic fibrosis, and Lynch syndrome. The cell has evolved an intricate protein quality control (PQC) system that includes degradation pathways and a multitude of molecular chaperones and co-chaperones, all working together to catalyze the refolding or removal of aberrant proteins. Thus, the PQC system limits the harmful consequences of dysfunctional proteins, including those arising from disease-causing mutations. This complex system is still not fully understood. In particular the structural and sequence motifs that, when exposed, trigger degradation of misfolded proteins are currently under investigation. Moreover, several attempts are being made to activate or inhibit parts of the PQC system as a treatment for diseases. Here, we briefly review the present knowledge on the PQC system and list current strategies that are employed to exploit the system in disease treatment.

AB - The cellular proteome performs highly varied functions to sustain life. Since most of these functions require proteins to fold properly, they can be impaired by mutations that affect protein structure, leading to diseases such as Alzheimer's disease, cystic fibrosis, and Lynch syndrome. The cell has evolved an intricate protein quality control (PQC) system that includes degradation pathways and a multitude of molecular chaperones and co-chaperones, all working together to catalyze the refolding or removal of aberrant proteins. Thus, the PQC system limits the harmful consequences of dysfunctional proteins, including those arising from disease-causing mutations. This complex system is still not fully understood. In particular the structural and sequence motifs that, when exposed, trigger degradation of misfolded proteins are currently under investigation. Moreover, several attempts are being made to activate or inhibit parts of the PQC system as a treatment for diseases. Here, we briefly review the present knowledge on the PQC system and list current strategies that are employed to exploit the system in disease treatment.

KW - Chaperone

KW - Misfolding

KW - Proteasome

KW - Protein folding

KW - Protein quality control

KW - Ubiquitin

U2 - 10.1016/bs.apcsb.2018.09.002

DO - 10.1016/bs.apcsb.2018.09.002

M3 - Book chapter

C2 - 30635086

AN - SCOPUS:85057239152

SN - 978-0-12-815557-8

T3 - Advances in Protein Chemistry and Structural Biology

SP - 61

EP - 83

BT - Molecular Chaperones in Human Disorders

A2 - Donev, Rossen

PB - Academic Press

ER -

ID: 212497738