Journal article
Lateral Diffusion of GFP-Tagged H2L d Molecules and of GFP-TAP1 Reports on the Assembly and Retention of These Molecules in the Endoplasmic Reticulum
Immunity (Cambridge, Mass.), v 11(2), pp 231-240
1999
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Lateral diffusion of GFP-tagged H2L
d molecules in the ER membrane reports on their interaction with the TAP complex during synthesis and peptide loading. Peptide-loaded H2L
d molecules diffuse rapidly, near the theoretical limit for proteins in a bilayer. However, these molecules are retained in the ER for some time after assembly. H2L
d molecules, associated with the TAP complex, diffuse slowly, as does GFP-tagged TAP1. This implies that the association of H2L
d molecules with the TAP complex is stable for at least several minutes. It also suggests that the TAP complex is very large, perhaps containing hundreds of proteins.
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Details
- Title
- Lateral Diffusion of GFP-Tagged H2L d Molecules and of GFP-TAP1 Reports on the Assembly and Retention of These Molecules in the Endoplasmic Reticulum
- Creators
- Didier Marguet - Johns Hopkins UniversityElias T Spiliotis - Johns Hopkins UniversityTsvetelina Pentcheva - Johns Hopkins UniversityMichael Lebowitz - Johns Hopkins MedicineJonathan Schneck - Johns Hopkins MedicineMichael Edidin - Johns Hopkins University
- Publication Details
- Immunity (Cambridge, Mass.), v 11(2), pp 231-240
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biology
- Web of Science ID
- WOS:000082383400012
- Scopus ID
- 2-s2.0-0033180470
- Other Identifier
- 991020112311304721
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Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Immunology