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For: Beerbaum M, Ballaschk M, Erdmann N, Schnick C, Diehl A, Uchanska-ziegler B, Ziegler A, Schmieder P. NMR spectroscopy reveals unexpected structural variation at the protein–protein interface in MHC class I molecules. J Biomol NMR 2013;57:167-78. [DOI: 10.1007/s10858-013-9777-z] [Cited by in Crossref: 23] [Cited by in F6Publishing: 24] [Article Influence: 2.6] [Reference Citation Analysis]
Number Citing Articles
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5 Achour A, Broggini L, Han X, Sun R, Santambrogio C, Buratto J, Visentin C, Barbiroli A, De Luca CMG, Sormanni P, Moda F, De Simone A, Sandalova T, Grandori R, Camilloni C, Ricagno S. Biochemical and biophysical comparison of human and mouse beta-2 microglobulin reveals the molecular determinants of low amyloid propensity. FEBS J 2020;287:546-60. [PMID: 31420997 DOI: 10.1111/febs.15046] [Cited by in Crossref: 2] [Cited by in F6Publishing: 1] [Article Influence: 0.7] [Reference Citation Analysis]
6 Ayres CM, Baker BM. Peptide-dependent tuning of major histocompatibility complex motional properties and the consequences for cellular immunity. Curr Opin Immunol 2022;76:102184. [PMID: 35550277 DOI: 10.1016/j.coi.2022.102184] [Reference Citation Analysis]
7 Driller R, Ballaschk M, Schmieder P, Uchanska-Ziegler B, Ziegler A, Loll B. Metal-triggered conformational reorientation of a self-peptide bound to a disease-associated HLA-B*27 subtype. J Biol Chem 2019;294:13269-79. [PMID: 31296658 DOI: 10.1074/jbc.RA119.008937] [Cited by in Crossref: 5] [Cited by in F6Publishing: 4] [Article Influence: 1.7] [Reference Citation Analysis]
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11 Natarajan K, Jiang J, Margulies DH. Structural aspects of chaperone-mediated peptide loading in the MHC-I antigen presentation pathway. Crit Rev Biochem Mol Biol 2019;54:164-73. [PMID: 31084439 DOI: 10.1080/10409238.2019.1610352] [Cited by in Crossref: 7] [Cited by in F6Publishing: 6] [Article Influence: 2.3] [Reference Citation Analysis]
12 Wieczorek M, Abualrous ET, Sticht J, Álvaro-Benito M, Stolzenberg S, Noé F, Freund C. Major Histocompatibility Complex (MHC) Class I and MHC Class II Proteins: Conformational Plasticity in Antigen Presentation. Front Immunol 2017;8:292. [PMID: 28367149 DOI: 10.3389/fimmu.2017.00292] [Cited by in F6Publishing: 1] [Reference Citation Analysis]
13 Ma J, Ayres CM, Hellman LM, Devlin JR, Baker BM. Dynamic allostery controls the peptide sensitivity of the Ly49C natural killer receptor. J Biol Chem 2021;296:100686. [PMID: 33891944 DOI: 10.1016/j.jbc.2021.100686] [Reference Citation Analysis]
14 Thomas C, Tampé R. MHC I chaperone complexes shaping immunity. Current Opinion in Immunology 2019;58:9-15. [DOI: 10.1016/j.coi.2019.01.001] [Cited by in Crossref: 22] [Cited by in F6Publishing: 18] [Article Influence: 7.3] [Reference Citation Analysis]
15 Abella JR, Antunes D, Jackson K, Lizée G, Clementi C, Kavraki LE. Markov state modeling reveals alternative unbinding pathways for peptide-MHC complexes. Proc Natl Acad Sci U S A 2020;117:30610-8. [PMID: 33184174 DOI: 10.1073/pnas.2007246117] [Cited by in Crossref: 1] [Cited by in F6Publishing: 2] [Article Influence: 0.5] [Reference Citation Analysis]
16 Zaitoua AJ, Kaur A, Raghavan M. Variations in MHC class I antigen presentation and immunopeptidome selection pathways. F1000Res 2020;9:F1000 Faculty Rev-1177. [PMID: 33014341 DOI: 10.12688/f1000research.26935.1] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 1.0] [Reference Citation Analysis]
17 Abualrous ET, Fritzsche S, Hein Z, Al-Balushi MS, Reinink P, Boyle LH, Wellbrock U, Antoniou AN, Springer S. F pocket flexibility influences the tapasin dependence of two differentially disease-associated MHC Class I proteins. Eur J Immunol. 2015;45:1248-1257. [PMID: 25615938 DOI: 10.1002/eji.201445307] [Cited by in Crossref: 34] [Cited by in F6Publishing: 34] [Article Influence: 4.9] [Reference Citation Analysis]
18 Serçinoğlu O, Ozbek P. Computational characterization of residue couplings and micropolymorphism-induced changes in the dynamics of two differentially disease-associated human MHC class-I alleles. Journal of Biomolecular Structure and Dynamics 2018;36:724-40. [DOI: 10.1080/07391102.2017.1295884] [Cited by in Crossref: 11] [Cited by in F6Publishing: 9] [Article Influence: 2.2] [Reference Citation Analysis]
19 McShan AC, Natarajan K, Kumirov VK, Flores-Solis D, Jiang J, Badstübner M, Toor JS, Bagshaw CR, Kovrigin EL, Margulies DH, Sgourakis NG. Peptide exchange on MHC-I by TAPBPR is driven by a negative allostery release cycle. Nat Chem Biol 2018;14:811-20. [PMID: 29988068 DOI: 10.1038/s41589-018-0096-2] [Cited by in Crossref: 51] [Cited by in F6Publishing: 42] [Article Influence: 12.8] [Reference Citation Analysis]
20 Yoshimura Y, So M, Miyanoiri Y. Carbonyl 13C-detect solution-state protein NMR experiments to circumvent amide-solvent exchange broadening: Application to β2-microglobulin. Biochim Biophys Acta Proteins Proteom 2021;1869:140593. [PMID: 33359410 DOI: 10.1016/j.bbapap.2020.140593] [Reference Citation Analysis]
21 Yanaka S, Sugase K. Exploration of the Conformational Dynamics of Major Histocompatibility Complex Molecules. Front Immunol 2017;8:632. [PMID: 28611781 DOI: 10.3389/fimmu.2017.00632] [Cited by in Crossref: 8] [Cited by in F6Publishing: 7] [Article Influence: 1.6] [Reference Citation Analysis]
22 Truong HV, Sgourakis NG. Dynamics of MHC-I molecules in the antigen processing and presentation pathway. Curr Opin Immunol 2021;70:122-8. [PMID: 34153556 DOI: 10.1016/j.coi.2021.04.012] [Reference Citation Analysis]
23 Ayres CM, Abualrous ET, Bailey A, Abraham C, Hellman LM, Corcelli SA, Noé F, Elliott T, Baker BM. Dynamically Driven Allostery in MHC Proteins: Peptide-Dependent Tuning of Class I MHC Global Flexibility. Front Immunol 2019;10:966. [PMID: 31130956 DOI: 10.3389/fimmu.2019.00966] [Cited by in Crossref: 21] [Cited by in F6Publishing: 18] [Article Influence: 7.0] [Reference Citation Analysis]
24 Ayres CM, Corcelli SA, Baker BM. Peptide and Peptide-Dependent Motions in MHC Proteins: Immunological Implications and Biophysical Underpinnings. Front Immunol 2017;8:935. [PMID: 28824655 DOI: 10.3389/fimmu.2017.00935] [Cited by in Crossref: 27] [Cited by in F6Publishing: 24] [Article Influence: 5.4] [Reference Citation Analysis]
25 Wieczorek M, Abualrous ET, Sticht J, Álvaro-Benito M, Stolzenberg S, Noé F, Freund C. Major Histocompatibility Complex (MHC) Class I and MHC Class II Proteins: Conformational Plasticity in Antigen Presentation. Front Immunol 2017;8:292. [PMID: 28367149 DOI: 10.3389/fimmu.2017.00292] [Cited by in Crossref: 248] [Cited by in F6Publishing: 220] [Article Influence: 49.6] [Reference Citation Analysis]
26 Buckle AM, Borg NA. Integrating Experiment and Theory to Understand TCR-pMHC Dynamics. Front Immunol 2018;9:2898. [PMID: 30581442 DOI: 10.3389/fimmu.2018.02898] [Cited by in Crossref: 15] [Cited by in F6Publishing: 13] [Article Influence: 3.8] [Reference Citation Analysis]
27 Natarajan K, Jiang J, May NA, Mage MG, Boyd LF, McShan AC, Sgourakis NG, Bax A, Margulies DH. The Role of Molecular Flexibility in Antigen Presentation and T Cell Receptor-Mediated Signaling. Front Immunol 2018;9:1657. [PMID: 30065727 DOI: 10.3389/fimmu.2018.01657] [Cited by in Crossref: 34] [Cited by in F6Publishing: 30] [Article Influence: 8.5] [Reference Citation Analysis]