The basis for limited specificity and MHC restriction in a T cell receptor interface
Published 2013 View Full Article
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Title
The basis for limited specificity and MHC restriction in a T cell receptor interface
Authors
Keywords
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Journal
Nature Communications
Volume 4, Issue 1, Pages -
Publisher
Springer Nature
Online
2013-06-05
DOI
10.1038/ncomms2948
References
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Related references
Note: Only part of the references are listed.- Structural and dynamic control of T-cell receptor specificity, cross-reactivity, and binding mechanism
- (2012) Brian M. Baker et al. IMMUNOLOGICAL REVIEWS
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- (2012) W. F. Hawse et al. JOURNAL OF IMMUNOLOGY
- Structural insights into the editing of germ-line-encoded interactions between T-cell receptor and MHC class II by V CDR3
- (2012) L. Deng et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- T Cell Receptor Signaling Is Limited by Docking Geometry to Peptide-Major Histocompatibility Complex
- (2011) Jarrett J. Adams et al. IMMUNITY
- αβ T Cell Receptors that Do Not Undergo Major Histocompatibility Complex-Specific Thymic Selection Possess Antibody-like Recognition Specificities
- (2011) Anastasia N. Tikhonova et al. IMMUNITY
- Conformational Melding Permits a Conserved Binding Geometry in TCR Recognition of Foreign and Self Molecular Mimics
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- TCRs Used in Cancer Gene Therapy Cross-React with MART-1/Melan-A Tumor Antigens via Distinct Mechanisms
- (2011) O. Y. Borbulevych et al. JOURNAL OF IMMUNOLOGY
- Disparate Degrees of Hypervariable Loop Flexibility Control T-Cell Receptor Cross-Reactivity, Specificity, and Binding Mechanism
- (2011) Daniel R. Scott et al. JOURNAL OF MOLECULAR BIOLOGY
- How T cell receptors interact with peptide-MHCs: A multiple steered molecular dynamics study
- (2011) Michel A. Cuendet et al. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
- Membrane protein folding: how important are hydrogen bonds?
- (2010) James U Bowie CURRENT OPINION IN STRUCTURAL BIOLOGY
- Hard wiring of T cell receptor specificity for the major histocompatibility complex is underpinned by TCR adaptability
- (2010) S. R. Burrows et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Fluorine substitutions in an antigenic peptide selectively modulate T-cell receptor binding in a minimally perturbing manner
- (2009) Kurt H. Piepenbrink et al. BIOCHEMICAL JOURNAL
- Theory of Free Energy and Entropy in Noncovalent Binding
- (2009) Huan-Xiang Zhou et al. CHEMICAL REVIEWS
- Structural alterations in peptide–MHC recognition by self-reactive T cell receptors
- (2009) Kai W Wucherpfennig et al. CURRENT OPINION IN IMMUNOLOGY
- T Cell Receptor Cross-reactivity Directed by Antigen-Dependent Tuning of Peptide-MHC Molecular Flexibility
- (2009) Oleg Y. Borbulevych et al. IMMUNITY
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- Germline-encoded amino acids in the αβ T-cell receptor control thymic selection
- (2009) James P. Scott-Browne et al. NATURE
- The molecular basis of TCR germline bias for MHC is surprisingly simple
- (2009) K Christopher Garcia et al. NATURE IMMUNOLOGY
- Conformational changes and flexibility in T-cell receptor recognition of peptide–MHC complexes
- (2008) Kathryn M. Armstrong et al. BIOCHEMICAL JOURNAL
- TCR-MHC docking orientation: natural selection, or thymic selection?
- (2008) Edward J. Collins et al. IMMUNOLOGIC RESEARCH
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