Publication

HSP40/DNAJ Chaperones

Bergink, S., Kampinga, H. H., Kolbe Musskopf, M. & Preusser Mattos, E., 17-May-2018, In : eLS.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Bergink, S., Kampinga, H. H., Kolbe Musskopf, M., & Preusser Mattos, E. (2018). HSP40/DNAJ Chaperones. eLS. https://doi.org/10.1002/9780470015902.a0027633

Author

Bergink, Steven ; Kampinga, H.H. ; Kolbe Musskopf, Maiara ; Preusser Mattos, Eduardo. / HSP40/DNAJ Chaperones. In: eLS. 2018.

Harvard

Bergink, S, Kampinga, HH, Kolbe Musskopf, M & Preusser Mattos, E 2018, 'HSP40/DNAJ Chaperones', eLS. https://doi.org/10.1002/9780470015902.a0027633

Standard

HSP40/DNAJ Chaperones. / Bergink, Steven; Kampinga, H.H.; Kolbe Musskopf, Maiara; Preusser Mattos, Eduardo.

In: eLS, 17.05.2018.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Bergink S, Kampinga HH, Kolbe Musskopf M, Preusser Mattos E. HSP40/DNAJ Chaperones. eLS. 2018 May 17. https://doi.org/10.1002/9780470015902.a0027633


BibTeX

@article{bf29e86e71c04c709c0c3dce52efe503,
title = "HSP40/DNAJ Chaperones",
abstract = "Members of the HSP40/DNAJ family comprise oneof the largest groups of molecular chaperones, andare present in all living organisms from bacteriato humans. The hallmark of DNAJs is the presenceof a J-domain, which is crucial for interaction withHSP70. DNAJs can be seen as the workforce thatsteers HSP70 machines, regulating client input andspecificity. The different DNAJs are involved in processessuch as (re)folding, intracellular transportacross membranes, protein modifications, remodellingof protein complexes and protein degradation.In particular, different DNAJs are able tosuppress aggregate formation of several amyloidogenicproteins linked to human diseases. On theother hand, mutations in many DNAJs give rise to awide range of pathologies, attesting to their fundamentalrole in cellular homeostasis and generalprotein quality control.",
author = "Steven Bergink and H.H. Kampinga and {Kolbe Musskopf}, Maiara and {Preusser Mattos}, Eduardo",
year = "2018",
month = may,
day = "17",
doi = "10.1002/9780470015902.a0027633",
language = "English",
journal = "eLS",
publisher = "Wiley",

}

RIS

TY - JOUR

T1 - HSP40/DNAJ Chaperones

AU - Bergink, Steven

AU - Kampinga, H.H.

AU - Kolbe Musskopf, Maiara

AU - Preusser Mattos, Eduardo

PY - 2018/5/17

Y1 - 2018/5/17

N2 - Members of the HSP40/DNAJ family comprise oneof the largest groups of molecular chaperones, andare present in all living organisms from bacteriato humans. The hallmark of DNAJs is the presenceof a J-domain, which is crucial for interaction withHSP70. DNAJs can be seen as the workforce thatsteers HSP70 machines, regulating client input andspecificity. The different DNAJs are involved in processessuch as (re)folding, intracellular transportacross membranes, protein modifications, remodellingof protein complexes and protein degradation.In particular, different DNAJs are able tosuppress aggregate formation of several amyloidogenicproteins linked to human diseases. On theother hand, mutations in many DNAJs give rise to awide range of pathologies, attesting to their fundamentalrole in cellular homeostasis and generalprotein quality control.

AB - Members of the HSP40/DNAJ family comprise oneof the largest groups of molecular chaperones, andare present in all living organisms from bacteriato humans. The hallmark of DNAJs is the presenceof a J-domain, which is crucial for interaction withHSP70. DNAJs can be seen as the workforce thatsteers HSP70 machines, regulating client input andspecificity. The different DNAJs are involved in processessuch as (re)folding, intracellular transportacross membranes, protein modifications, remodellingof protein complexes and protein degradation.In particular, different DNAJs are able tosuppress aggregate formation of several amyloidogenicproteins linked to human diseases. On theother hand, mutations in many DNAJs give rise to awide range of pathologies, attesting to their fundamentalrole in cellular homeostasis and generalprotein quality control.

U2 - 10.1002/9780470015902.a0027633

DO - 10.1002/9780470015902.a0027633

M3 - Article

JO - eLS

JF - eLS

ER -

ID: 83112308