Molecular chaperones: Small heat shock proteins in the limelight

Paul Van den IJssel; David G. Norman; Roy A. Quinlan

doi:10.1016/S0960-9822(99)80061-X

Molecular chaperones: Small heat shock proteins in the limelight

Paul Van den IJssel
, David G. Norman
, Roy A. Quinlan

Research output: Contribution to journal › Comment/debate › peer-review

71 Citations (Scopus)

Abstract

Small heat shock proteins have been the Cinderellas of the molecular chaperone world, but now the crystal structure of a small heat shock protein has been solved and mutation of two human homologues implicated in genetic disease. Intermediate filaments appear to be one of the key targets of their chaperone activity.

Original language	English
Pages (from-to)	R103-R105
Number of pages	3
Journal	Current Biology
Volume	9
Issue number	3
DOIs	https://doi.org/10.1016/S0960-9822(99)80061-X
Publication status	Published - 11 Feb 1999

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

ASJC Scopus subject areas

General Biochemistry,Genetics and Molecular Biology
General Agricultural and Biological Sciences

Access to Document

10.1016/S0960-9822(99)80061-X

Cite this

@article{52aef83a3b30446692b1ae2c4e7cd333,

title = "Molecular chaperones: Small heat shock proteins in the limelight",

abstract = "Small heat shock proteins have been the Cinderellas of the molecular chaperone world, but now the crystal structure of a small heat shock protein has been solved and mutation of two human homologues implicated in genetic disease. Intermediate filaments appear to be one of the key targets of their chaperone activity.",

author = "\{Van den IJssel\}, Paul and Norman, \{David G.\} and Quinlan, \{Roy A.\}",

note = "Funding Information: We are grateful to S.H. Kim for giving us access to the crystallographic details of M. jannaschii Hsp16.5. The financial support of the Wellcome Trust is gratefully acknowledged (RAQ/PvdIJ). ",

year = "1999",

month = feb,

day = "11",

doi = "10.1016/S0960-9822(99)80061-X",

language = "English",

volume = "9",

pages = "R103--R105",

journal = "Current Biology",

issn = "0960-9822",

publisher = "Cell Press",

number = "3",

}

TY - JOUR

T1 - Molecular chaperones

T2 - Small heat shock proteins in the limelight

AU - Van den IJssel, Paul

AU - Norman, David G.

AU - Quinlan, Roy A.

N1 - Funding Information: We are grateful to S.H. Kim for giving us access to the crystallographic details of M. jannaschii Hsp16.5. The financial support of the Wellcome Trust is gratefully acknowledged (RAQ/PvdIJ).

PY - 1999/2/11

Y1 - 1999/2/11

N2 - Small heat shock proteins have been the Cinderellas of the molecular chaperone world, but now the crystal structure of a small heat shock protein has been solved and mutation of two human homologues implicated in genetic disease. Intermediate filaments appear to be one of the key targets of their chaperone activity.

AB - Small heat shock proteins have been the Cinderellas of the molecular chaperone world, but now the crystal structure of a small heat shock protein has been solved and mutation of two human homologues implicated in genetic disease. Intermediate filaments appear to be one of the key targets of their chaperone activity.

UR - https://www.scopus.com/pages/publications/0033545355

U2 - 10.1016/S0960-9822(99)80061-X

DO - 10.1016/S0960-9822(99)80061-X

M3 - Comment/debate

C2 - 10021375

AN - SCOPUS:0033545355

SN - 0960-9822

VL - 9

SP - R103-R105

JO - Current Biology

JF - Current Biology

IS - 3

ER -

Molecular chaperones: Small heat shock proteins in the limelight

Abstract

UN SDGs

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this