Ligand-independent assembly of recombinant human CD1 by using oxidative refolding chromatography
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Summary
The results suggest that “empty” MHC class I-like molecules can assemble and remain stable at physiological temperatures in the absence of ligand, and the use of oxidative refolding chromatography is extended to encompass complex multisubunit proteins.
- Type
- article
- Published
- 2001-03-13
- Cited by
- 44
- References
- 39
- Access
- Open access
- OpenAlex
- https://openalex.org/W11248071
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:30059126
Keywords
Computer science
References
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- Human CD1d–glycolipid tetramers generated by in vitro oxidative refolding chromatography
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- Beta 2-microglobulin-independent MHC class Ib molecule expressed by human intestinal epithelium.
- HLA-A2-peptide complexes: refolding and crystallization of molecules expressed in Escherichia coli and complexed with single antigenic peptides.
- Crystal structure of mouse CD1: An MHC-like fold with a large hydrophobic binding groove.
- Separate pathways for antigen presentation by CD1 molecules.
- Structural characterization of a soluble and partially folded class I major histocompatibility heavy chain/β2m heterodimer
- CD1c-mediated T-cell recognition of isoprenoid glycolipids in Mycobacterium tuberculosis infection
- CD1-restricted T cell recognition of microbial lipoglycan antigens.
- Cell-surface enzymes and lymphocyte functions.
- Presentation of peptide antigens by mouse CD1 requires endosomal localization and protein antigen processing.
- Natural ligand of mouse CD1d1: cellular glycosylphosphatidylinositol.
- Peptide binding and presentation by mouse CD1.
Cited by
- Lipid Protein Interactions: The Assembly of CD1d1 with Cellular Phospholipids Occurs in the Endoplasmic Reticulum1
- Intracellular pathways of CD1 antigen presentation
- Human CD1d–glycolipid tetramers generated by in vitro oxidative refolding chromatography
- The C-terminal SH3 domain of CRKL as a dynamic dimerization module transiently exposing a nuclear export signal.
- Mus81 cleavage of Holliday junctions: a failsafe for processing meiotic recombination intermediates?
- The crystal structure of human CD1d with and without α-galactosylceramide
- Systems biology of pathogen‐host interaction: Networks of protein‐protein interaction within pathogens and pathogen‐human interactions in the post‐genomic era
- Microbial small heat shock proteins and their use in biotechnology.
- A closer look at CD1d molecules: new horizons in studying NKT cells.
- Phage display‐derived recombinant antibodies with TCR‐like specificity against α‐galactosylceramide and its analogues in complex with human CD1d molecules
- CD1a and CD1b surface expression is independent from de novo synthesized glycosphingolipids
- CD1 tetramers: a powerful tool for the analysis of glycolipid-reactive T cells.
- Protein folding liquid chromatography and its recent developments
- Functional CD1a is stabilized by exogenous lipids
- The Third Way: Progress on pathways of antigen processing and presentation by CD1
- Synthesis of a Fluorescent Sulfatide for the Study of CD1 Antigen Binding Properties
- Manufacturing of recombinant therapeutic proteins in microbial systems
- A novel system for continuous protein refolding and on‐line capture by expanded bed adsorption
- CD1a-binding glycosphingolipids stimulating human autoreactive T-cells: synthesis of a family of sulfatides differing in the acyl chain moiety
- Biotechnical applications of small heat shock proteins from bacteria.
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