Chaperones and folding of MHC class I molecules in the endoplasmic reticulum.
(2003) In Biochimica et Biophysica Acta 1641(1). p.1-12- Abstract
- In this review we discuss the influence of chaperones on the general phenomena of folding as well as on the specific folding of an individual protein, MHC class I. MHC class I maturation is a highly sophisticated process in which the folding machinery of the endoplasmic reticulum (ER) is heavily involved. Understanding the MHC class I maturation per se is important since peptides loaded onto MHC class I molecules are the base for antigen presentation generating immune responses against virus, intracellular bacteria as well as tumours. This review discusses the early stages of MHC class I maturation regarding BiP and calnexin association, and differences in MHC class I heavy chain (HC) interaction with calnexin and calreticulin are... (More)
- In this review we discuss the influence of chaperones on the general phenomena of folding as well as on the specific folding of an individual protein, MHC class I. MHC class I maturation is a highly sophisticated process in which the folding machinery of the endoplasmic reticulum (ER) is heavily involved. Understanding the MHC class I maturation per se is important since peptides loaded onto MHC class I molecules are the base for antigen presentation generating immune responses against virus, intracellular bacteria as well as tumours. This review discusses the early stages of MHC class I maturation regarding BiP and calnexin association, and differences in MHC class I heavy chain (HC) interaction with calnexin and calreticulin are highlighted. Late stage MHC class I maturation with focus on the dedicated chaperone tapasin is also discussed. (C) 2003 Elsevier Science B.V. All rights reserved. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/116118
- author
- Paulsson, Kajsa M LU and Wang, Ping
- organization
- publishing date
- 2003
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- chaperone, tapasin, endoplasmic reticulum (ER), MEC class I, folding
- in
- Biochimica et Biophysica Acta
- volume
- 1641
- issue
- 1
- pages
- 1 - 12
- publisher
- Elsevier
- external identifiers
-
- pmid:12788224
- wos:000183481800001
- scopus:0038697962
- ISSN
- 0006-3002
- DOI
- 10.1016/S0167-4889(03)00048-X
- language
- English
- LU publication?
- yes
- id
- 5c4be31f-046d-4d5f-abcd-3d63f4214fdb (old id 116118)
- alternative location
- http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12788224&dopt=Abstract
- date added to LUP
- 2016-04-01 16:52:32
- date last changed
- 2023-08-16 15:12:55
@article{5c4be31f-046d-4d5f-abcd-3d63f4214fdb, abstract = {{In this review we discuss the influence of chaperones on the general phenomena of folding as well as on the specific folding of an individual protein, MHC class I. MHC class I maturation is a highly sophisticated process in which the folding machinery of the endoplasmic reticulum (ER) is heavily involved. Understanding the MHC class I maturation per se is important since peptides loaded onto MHC class I molecules are the base for antigen presentation generating immune responses against virus, intracellular bacteria as well as tumours. This review discusses the early stages of MHC class I maturation regarding BiP and calnexin association, and differences in MHC class I heavy chain (HC) interaction with calnexin and calreticulin are highlighted. Late stage MHC class I maturation with focus on the dedicated chaperone tapasin is also discussed. (C) 2003 Elsevier Science B.V. All rights reserved.}}, author = {{Paulsson, Kajsa M and Wang, Ping}}, issn = {{0006-3002}}, keywords = {{chaperone; tapasin; endoplasmic reticulum (ER); MEC class I; folding}}, language = {{eng}}, number = {{1}}, pages = {{1--12}}, publisher = {{Elsevier}}, series = {{Biochimica et Biophysica Acta}}, title = {{Chaperones and folding of MHC class I molecules in the endoplasmic reticulum.}}, url = {{http://dx.doi.org/10.1016/S0167-4889(03)00048-X}}, doi = {{10.1016/S0167-4889(03)00048-X}}, volume = {{1641}}, year = {{2003}}, }