☰

Samuel J. Landry - Publications

Affiliations: 
Tulane University, New Orleans, LA, United States 
Area:
Biochemistry, General Biophysics, Microbiology Biology
Tree Info Similar researchers PubMed Report error

54 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2023 Landry SJ, Mettu RR, Kolls JK, Aberle JH, Norton E, Zwezdaryk K, Robinson J. Structural Framework for Analysis of CD4+ T-Cell Epitope Dominance in Viral Fusion Proteins. Biochemistry. PMID 37554055 DOI: 10.1021/acs.biochem.3c00335  0.367
2022 Noell K, Dai G, Pungan D, Ebacher A, McCombs JE, Landry SJ, Kolls JK. Germline IgM predicts T-cell immunity to Pneumocystis. Jci Insight. PMID 35917185 DOI: 10.1172/jci.insight.161450  0.313
2022 Charles T, Moss DL, Bhat P, Moore PW, Kummer NA, Bhattacharya A, Landry SJ, Mettu RR. CD4+ T-Cell Epitope Prediction by Combined Analysis of Antigen Conformational Flexibility and Peptide-MHCII Binding Affinity. Biochemistry. PMID 35834502 DOI: 10.1021/acs.biochem.2c00237  0.76
2021 Moss DL, Mettu RR, Landry SJ. The Serpin-like Loop Insertion of Ovalbumin Increases the Stability and Decreases the OVA 323-339 Epitope Processing Efficiency. Biochemistry. PMID 33956428 DOI: 10.1021/acs.biochem.1c00095  0.359
2020 Cassotta A, Paparoditis P, Geiger R, Mettu RR, Landry SJ, Donati A, Benevento M, Foglierini M, Lewis DJM, Lanzavecchia A, Sallusto F. Deciphering and predicting CD4+ T cell immunodominance of influenza virus hemagglutinin. The Journal of Experimental Medicine. 217. PMID 32644114 DOI: 10.1084/Jem.20200206  0.446
2019 Bascos NAD, Landry SJ. A History of Molecular Chaperone Structures in the Protein Data Bank. International Journal of Molecular Sciences. 20. PMID 31817979 DOI: 10.3390/Ijms20246195  0.337
2019 Moss DL, Park HW, Mettu RR, Landry SJ. Deimmunizing substitutions in pseudomonas exotoxin domain III perturb antigen processing without eliminating T-cell epitopes. The Journal of Biological Chemistry. PMID 30683694 DOI: 10.1074/Jbc.Ra118.006704  0.488
2017 Bascos NAD, Mayer MP, Bukau B, Landry SJ. The Hsp40 J-domain modulates Hsp70 conformation and ATPase activity with a semi-elliptical spring. Protein Science : a Publication of the Protein Society. PMID 28685898 DOI: 10.1002/Pro.3223  0.343
2017 Landry SJ, Moss DL, Cui D, Ferrie RP, Fullerton ML, Wells EA, Yang L, Zhou N, Dougherty T, Mettu RR. Structural Basis for CD4+ T Cell Epitope Dominance in Arbo-Flavivirus Envelope Proteins: A Meta-Analysis. Viral Immunology. PMID 28614011 DOI: 10.1089/vim.2017.0008  0.301
2016 Spanier JA, Frederick DR, Taylor JJ, Heffernan JR, Kotov DI, Martinov T, Osum KC, Ruggiero JL, Rust BJ, Landry SJ, Jenkins MK, McLachlan JB, Fife BT. Efficient generation of monoclonal antibodies against peptide in the context of MHCII using magnetic enrichment. Nature Communications. 7: 11804. PMID 27292946 DOI: 10.1038/Ncomms11804  0.366
2016 Mettu RR, Charles T, Landry SJ. CD4+ T-cell epitope prediction using antigen processing constraints. Journal of Immunological Methods. PMID 26891811 DOI: 10.1016/J.Jim.2016.02.013  0.758
2015 Nguyen HN, Steede NK, Robinson JE, Landry SJ. Conformational instability governed by disulfide bonds partitions the dominant from subdominant helper T-cell responses specific for HIV-1 envelope glycoprotein gp120. Vaccine. 33: 2887-96. PMID 25944298 DOI: 10.1016/J.Vaccine.2015.04.082  0.428
2015 Bascos NAD, Landry SJ. Structural Rigidity Regulates Functional Interactions in the Hsp40-Hsp70 Molecular Machine Biophysical Journal. 108: 210a. DOI: 10.1016/J.Bpj.2014.11.1160  0.337
2014 Li T, Steede NK, Nguyen HN, Freytag LC, McLachlan JB, Mettu RR, Robinson JE, Landry SJ. Comprehensive analysis of contributions from protein conformational stability and major histocompatibility complex class II-peptide binding affinity to CD4+ epitope immunogenicity in HIV-1 envelope glycoprotein. Journal of Virology. 88: 9605-15. PMID 24920818 DOI: 10.1128/Jvi.00789-14  0.478
2014 Charles T, Grimm CC, McBride J, Landry S, Maleki SJ. Simulated Roasting Affects Patient IgE Binding To Ara h 2 Journal of Allergy and Clinical Immunology. 133: AB116. DOI: 10.1016/J.Jaci.2013.12.431  0.723
2013 Steede NK, Rust BJ, Hossain MM, Freytag LC, Robinson JE, Landry SJ. Shaping T cell - B cell collaboration in the response to human immunodeficiency virus type 1 envelope glycoprotein gp120 by peptide priming. Plos One. 8: e65748. PMID 23776539 DOI: 10.1371/Journal.Pone.0065748  0.418
2013 Charles T, Grimm CC, Landry S, Maleki SJ. Chemical and Structural Alterations to Ara h 2 Following Simulated Roasting Journal of Allergy and Clinical Immunology. 131: AB20. DOI: 10.1016/J.Jaci.2012.12.749  0.721
2011 Charles T, Hurlburt B, Landry S, Maleki S. Cloning and High-Level Expression of Recombinant Ara h 6 Journal of Allergy and Clinical Immunology. 127: AB31-AB31. DOI: 10.1016/J.Jaci.2010.12.132  0.712
2010 Horne BE, Li T, Genevaux P, Georgopoulos C, Landry SJ. The Hsp40 J-domain stimulates Hsp70 when tethered by the client to the ATPase domain. The Journal of Biological Chemistry. 285: 21679-88. PMID 20448033 DOI: 10.1074/Jbc.M110.113118  0.357
2010 Mirano-Bascos D, Steede NK, Robinson JE, Landry SJ. Influence of disulfide-stabilized structure on the specificity of helper T-cell and antibody responses to HIV envelope glycoprotein gp120. Journal of Virology. 84: 3303-11. PMID 20089653 DOI: 10.1128/Jvi.02242-09  0.445
2009 Li H, Xu CF, Blais S, Wan Q, Zhang HT, Landry SJ, Hioe CE. Proximal glycans outside of the epitopes regulate the presentation of HIV-1 envelope gp120 helper epitopes. Journal of Immunology (Baltimore, Md. : 1950). 182: 6369-78. PMID 19414790 DOI: 10.4049/Jimmunol.0804287  0.41
2008 Melton SJ, Landry SJ. Three dimensional structure directs T-cell epitope dominance associated with allergy. Clinical and Molecular Allergy : Cma. 6: 9. PMID 18793409 DOI: 10.1186/1476-7961-6-9  0.475
2008 Mirano-Bascos D, Tary-Lehmann M, Landry SJ. Antigen structure influences helper T-cell epitope dominance in the human immune response to HIV envelope glycoprotein gp120. European Journal of Immunology. 38: 1231-7. PMID 18398933 DOI: 10.1002/Eji.200738011  0.445
2008 Landry SJ. Three-dimensional structure determines the pattern of CD4+ T-cell epitope dominance in influenza virus hemagglutinin. Journal of Virology. 82: 1238-48. PMID 18057238 DOI: 10.1128/Jvi.02026-07  0.405
2007 Carmicle S, Steede NK, Landry SJ. Antigen three-dimensional structure guides the processing and presentation of helper T-cell epitopes. Molecular Immunology. 44: 1159-68. PMID 16893568 DOI: 10.1016/J.Molimm.2006.06.014  0.776
2004 Shewmaker F, Kerner MJ, Hayer-Hartl M, Klein G, Georgopoulos C, Landry SJ. A mobile loop order-disorder transition modulates the speed of chaperonin cycling. Protein Science : a Publication of the Protein Society. 13: 2139-48. PMID 15238634 DOI: 10.1110/Ps.04773204  0.667
2004 Curiel TJ, Morris C, Brumlik M, Landry SJ, Finstad K, Nelson A, Joshi V, Hawkins C, Alarez X, Lackner A, Mohamadzadeh M. Peptides identified through phage display direct immunogenic antigen to dendritic cells. Journal of Immunology (Baltimore, Md. : 1950). 172: 7425-31. PMID 15187120 DOI: 10.4049/Jimmunol.172.12.7425  0.388
2003 Landry SJ. Swivels and stators in the Hsp40-Hsp70 chaperone machine. Structure (London, England : 1993). 11: 1465-6. PMID 14656429 DOI: 10.1016/J.Str.2003.11.012  0.348
2003 Guidry JJ, Shewmaker F, Maskos K, Landry S, Wittung-Stafshede P. Probing the interface in a human co-chaperonin heptamer: residues disrupting oligomeric unfolded state identified. Bmc Biochemistry. 4: 14. PMID 14525625 DOI: 10.1186/1471-2091-4-14  0.645
2003 Maleki SJ, Viquez O, Jacks T, Dodo H, Champagne ET, Chung SY, Landry SJ. The major peanut allergen, Ara h 2, functions as a trypsin inhibitor, and roasting enhances this function. The Journal of Allergy and Clinical Immunology. 112: 190-5. PMID 12847498 DOI: 10.1067/Mai.2003.1551  0.377
2003 Wittung-Stafshede P, Guidry J, Horne BE, Landry SJ. The J-domain of Hsp40 couples ATP hydrolysis to substrate capture in Hsp70. Biochemistry. 42: 4937-44. PMID 12718535 DOI: 10.1021/Bi027333O  0.353
2003 Landry SJ. Structure and energetics of an allele-specific genetic interaction between dnaJ and dnaK: correlation of nuclear magnetic resonance chemical shift perturbations in the J-domain of Hsp40/DnaJ with binding affinity for the ATPase domain of Hsp70/DnaK. Biochemistry. 42: 4926-36. PMID 12718534 DOI: 10.1021/Bi027070Y  0.362
2002 Carmicle S, Dai G, Steede NK, Landry SJ. Proteolytic sensitivity and helper T-cell epitope immunodominance associated with the mobile loop in Hsp10s. The Journal of Biological Chemistry. 277: 155-60. PMID 11673463 DOI: 10.1074/Jbc.M107624200  0.77
2002 Dai G, Carmicle S, Steede NK, Landry SJ. Structural basis for helper T-cell and antibody epitope immunodominance in bacteriophage T4 Hsp10. Role of disordered loops. The Journal of Biological Chemistry. 277: 161-8. PMID 11602571 DOI: 10.1074/Jbc.M102259200  0.771
2001 Dai G, Steede NK, Landry SJ. Allocation of helper T-cell epitope immunodominance according to three-dimensional structure in the human immunodeficiency virus type I envelope glycoprotein gp120. The Journal of Biological Chemistry. 276: 41913-20. PMID 11551929 DOI: 10.1074/Jbc.M106018200  0.425
2001 Shewmaker F, Maskos K, Simmerling C, Landry SJ. The disordered mobile loop of GroES folds into a defined beta-hairpin upon binding GroEL. The Journal of Biological Chemistry. 276: 31257-64. PMID 11395498 DOI: 10.1074/Jbc.M102765200  0.303
2001 Richardson A, Schwager F, Landry SJ, Georgopoulos C. The importance of a mobile loop in regulating chaperonin/ co-chaperonin interaction: humans versus Escherichia coli. The Journal of Biological Chemistry. 276: 4981-7. PMID 11050098 DOI: 10.1074/Jbc.M008628200  0.434
2000 Guidry JJ, Moczygemba CK, Steede NK, Landry SJ, Wittung-Stafshede P. Reversible denaturation of oligomeric human chaperonin 10: denatured state depends on chemical denaturant. Protein Science : a Publication of the Protein Society. 9: 2109-17. PMID 11152122 DOI: 10.1110/Ps.9.11.2109  0.335
2000 Greene MK, Steede NK, Landry SJ. Domain-specific spectroscopy of 5-hydroxytryptophan-containing variants of Escherichia coli DnaJ. Biochimica Et Biophysica Acta. 1480: 267-77. PMID 10899627 DOI: 10.1016/S0167-4838(00)00078-9  0.334
2000 Landry SJ. Helper T-cell epitope immunodominance associated with structurally stable segments of hen egg lysozyme and HIV gp120. Journal of Theoretical Biology. 203: 189-201. PMID 10716904 DOI: 10.1006/Jtbi.1999.1056  0.45
1999 Wang Z, Feng Hp, Landry SJ, Maxwell J, Gierasch LM. Basis of substrate binding by the chaperonin GroEL. Biochemistry. 38: 12537-46. PMID 10504222 DOI: 10.1021/Bi991070P  0.373
1999 Richardson A, van der Vies SM, Keppel F, Taher A, Landry SJ, Georgopoulos C. Compensatory changes in GroEL/Gp31 affinity as a mechanism for allele-specific genetic interaction. The Journal of Biological Chemistry. 274: 52-8. PMID 9867810 DOI: 10.1074/Jbc.274.1.52  0.353
1998 Greene MK, Maskos K, Landry SJ. Role of the J-domain in the cooperation of Hsp40 with Hsp70. Proceedings of the National Academy of Sciences of the United States of America. 95: 6108-13. PMID 9600925 DOI: 10.1073/Pnas.95.11.6108  0.36
1998 Richardson A, Landry SJ, Georgopoulos C. The ins and outs of a molecular chaperone machine. Trends in Biochemical Sciences. 23: 138-43. PMID 9584617 DOI: 10.1016/S0968-0004(98)01193-1  0.327
1997 Landry SJ. Local protein instability predictive of helper T-cell epitopes. Immunology Today. 18: 527-32. PMID 9386348 DOI: 10.1016/S0167-5699(97)01152-3  0.452
1997 Bramhall EA, Cross RL, Rospert S, Steede NK, Landry SJ. Identification of amino acid residues at nucleotide-binding sites of chaperonin GroEL/GroES and cpn10 by photoaffinity labeling with 2-azido-adenosine 5'-triphosphate. European Journal of Biochemistry / Febs. 244: 627-34. PMID 9119033 DOI: 10.1111/J.1432-1033.1997.00627.X  0.357
1996 Landry SJ, Taher A, Georgopoulos C, van der Vies SM. Interplay of structure and disorder in cochaperonin mobile loops. Proceedings of the National Academy of Sciences of the United States of America. 93: 11622-7. PMID 8876186 DOI: 10.1073/Pnas.93.21.11622  0.445
1996 Hunt JF, Weaver AJ, Landry SJ, Gierasch L, Deisenhofer J. The crystal structure of the GroES co-chaperonin at 2.8 A resolution. Nature. 379: 37-45. PMID 8538739 DOI: 10.1038/379037A0  0.342
1996 Taher A, Steede NK, Georgopoulos C, Landry SJ. Studies on the mechanism of groes-groel binding Faseb Journal. 10.  0.308
1993 Landry SJ, Zeilstra-Ryalls J, Fayet O, Georgopoulos C, Gierasch LM. Characterization of a functionally important mobile domain of GroES. Nature. 364: 255-8. PMID 8100614 DOI: 10.1038/364255A0  0.394
1993 Landry SJ. Nuclear Magnetic Resonance Studies of Peptides Bound to Chaperones Methods. 5: 233-241. DOI: 10.1006/Meth.1993.1029  0.372
1992 Landry SJ, Jordan R, McMacken R, Gierasch LM. Different conformations for the same polypeptide bound to chaperones DnaK and GroEL. Nature. 355: 455-7. PMID 1346469 DOI: 10.1038/355455A0  0.374
1991 Landry SJ, Gierasch LM. Recognition of nascent polypeptides for targeting and folding. Trends in Biochemical Sciences. 16: 159-63. PMID 1877092 DOI: 10.1016/0968-0004(91)90060-9  0.327
1991 Landry SJ, Gierasch LM. The chaperonin GroEL binds a polypeptide in an alpha-helical conformation. Biochemistry. 30: 7359-62. PMID 1677268 DOI: 10.1021/Bi00244A001  0.369
Show low-probability matches.