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Items: 1 to 50 of 58

1.

Deimmunizing substitutions in Pseudomonas exotoxin domain III perturb antigen processing without eliminating T-cell epitopes.

Moss DL, Park HW, Mettu RR, Landry SJ.

J Biol Chem. 2019 Mar 22;294(12):4667-4681. doi: 10.1074/jbc.RA118.006704. Epub 2019 Jan 25.

PMID:
30683694
2.

The Hsp40 J-domain modulates Hsp70 conformation and ATPase activity with a semi-elliptical spring.

Bascos NAD, Mayer MP, Bukau B, Landry SJ.

Protein Sci. 2017 Sep;26(9):1838-1851. doi: 10.1002/pro.3223. Epub 2017 Jul 17.

3.

Structural Basis for CD4+ T Cell Epitope Dominance in Arbo-Flavivirus Envelope Proteins: A Meta-Analysis.

Landry SJ, Moss DL, Cui D, Ferrie RP, Fullerton ML, Wells EA, Yang L, Zhou N, Dougherty T, Mettu RR.

Viral Immunol. 2017 Sep;30(7):479-489. doi: 10.1089/vim.2017.0008. Epub 2017 Jun 14.

4.

Efficient generation of monoclonal antibodies against peptide in the context of MHCII using magnetic enrichment.

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.

Nat Commun. 2016 Jun 13;7:11804. doi: 10.1038/ncomms11804.

5.

CD4+ T-cell epitope prediction using antigen processing constraints.

Mettu RR, Charles T, Landry SJ.

J Immunol Methods. 2016 May;432:72-81. doi: 10.1016/j.jim.2016.02.013. Epub 2016 Feb 15.

6.

Conformational instability governed by disulfide bonds partitions the dominant from subdominant helper T-cell responses specific for HIV-1 envelope glycoprotein gp120.

Nguyen HN, Steede NK, Robinson JE, Landry SJ.

Vaccine. 2015 Jun 9;33(25):2887-96. doi: 10.1016/j.vaccine.2015.04.082. Epub 2015 May 2.

7.
8.

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.

Li T, Steede NK, Nguyen HN, Freytag LC, McLachlan JB, Mettu RR, Robinson JE, Landry SJ.

J Virol. 2014 Sep 1;88(17):9605-15. doi: 10.1128/JVI.00789-14. Epub 2014 Jun 11.

9.

Shaping T cell - B cell collaboration in the response to human immunodeficiency virus type 1 envelope glycoprotein gp120 by peptide priming.

Steede NK, Rust BJ, Hossain MM, Freytag LC, Robinson JE, Landry SJ.

PLoS One. 2013 Jun 11;8(6):e65748. doi: 10.1371/journal.pone.0065748. Print 2013.

10.

The prediction and characterization of YshA, an unknown outer-membrane protein from Salmonella typhimurium.

Freeman TC Jr, Landry SJ, Wimley WC.

Biochim Biophys Acta. 2011 Jan;1808(1):287-97. doi: 10.1016/j.bbamem.2010.09.008. Epub 2010 Sep 20.

11.

The Hsp40 J-domain stimulates Hsp70 when tethered by the client to the ATPase domain.

Horne BE, Li T, Genevaux P, Georgopoulos C, Landry SJ.

J Biol Chem. 2010 Jul 9;285(28):21679-88. doi: 10.1074/jbc.M110.113118. Epub 2010 May 6.

12.

Influence of disulfide-stabilized structure on the specificity of helper T-cell and antibody responses to HIV envelope glycoprotein gp120.

Mirano-Bascos D, Steede NK, Robinson JE, Landry SJ.

J Virol. 2010 Apr;84(7):3303-11. doi: 10.1128/JVI.02242-09. Epub 2010 Jan 20.

13.

Proximal glycans outside of the epitopes regulate the presentation of HIV-1 envelope gp120 helper epitopes.

Li H, Xu CF, Blais S, Wan Q, Zhang HT, Landry SJ, Hioe CE.

J Immunol. 2009 May 15;182(10):6369-78. doi: 10.4049/jimmunol.0804287.

14.

Three dimensional structure directs T-cell epitope dominance associated with allergy.

Melton SJ, Landry SJ.

Clin Mol Allergy. 2008 Sep 15;6:9. doi: 10.1186/1476-7961-6-9.

15.

Antigen structure influences helper T-cell epitope dominance in the human immune response to HIV envelope glycoprotein gp120.

Mirano-Bascos D, Tary-Lehmann M, Landry SJ.

Eur J Immunol. 2008 May;38(5):1231-7. doi: 10.1002/eji.200738011.

17.

Antigen three-dimensional structure guides the processing and presentation of helper T-cell epitopes.

Carmicle S, Steede NK, Landry SJ.

Mol Immunol. 2007 Feb;44(6):1159-68. Epub 2006 Aug 8.

PMID:
16893568
18.

Goal activation, expectations, and the placebo effect.

Geers AL, Weiland PE, Kosbab K, Landry SJ, Helfer SG.

J Pers Soc Psychol. 2005 Aug;89(2):143-59.

PMID:
16162050
19.

Reconsidering the role of personality in placebo effects: dispositional optimism, situational expectations, and the placebo response.

Geers AL, Helfer SG, Kosbab K, Weiland PE, Landry SJ.

J Psychosom Res. 2005 Feb;58(2):121-7.

PMID:
15820839
20.

A mobile loop order-disorder transition modulates the speed of chaperonin cycling.

Shewmaker F, Kerner MJ, Hayer-Hartl M, Klein G, Georgopoulos C, Landry SJ.

Protein Sci. 2004 Aug;13(8):2139-48. Epub 2004 Jul 6.

21.

Peptides identified through phage display direct immunogenic antigen to dendritic cells.

Curiel TJ, Morris C, Brumlik M, Landry SJ, Finstad K, Nelson A, Joshi V, Hawkins C, Alarez X, Lackner A, Mohamadzadeh M.

J Immunol. 2004 Jun 15;172(12):7425-31.

22.

Tc1 effector diversity shows dissociated expression of granzyme B and interferon-gamma in HIV infection.

Kleen TO, Asaad R, Landry SJ, Boehm BO, Tary-Lehmann M.

AIDS. 2004 Feb 20;18(3):383-92.

PMID:
15090789
23.

Swivels and stators in the Hsp40-Hsp70 chaperone machine.

Landry SJ.

Structure. 2003 Dec;11(12):1465-6. No abstract available.

24.

The major peanut allergen, Ara h 2, functions as a trypsin inhibitor, and roasting enhances this function.

Maleki SJ, Viquez O, Jacks T, Dodo H, Champagne ET, Chung SY, Landry SJ.

J Allergy Clin Immunol. 2003 Jul;112(1):190-5.

PMID:
12847498
25.

The J-domain of Hsp40 couples ATP hydrolysis to substrate capture in Hsp70.

Wittung-Stafshede P, Guidry J, Horne BE, Landry SJ.

Biochemistry. 2003 May 6;42(17):4937-44.

PMID:
12718535
27.

A novel approach to grading pork carcasses: computer vision and ultrasound.

Fortin A, Tong AK, Robertson WM, Zawadski SM, Landry SJ, Robinson DJ, Liu T, Mockford RJ.

Meat Sci. 2003 Apr;63(4):451-62.

PMID:
22062514
28.
29.

Proteolytic sensitivity and helper T-cell epitope immunodominance associated with the mobile loop in Hsp10s.

Carmicle S, Dai G, Steede NK, Landry SJ.

J Biol Chem. 2002 Jan 4;277(1):155-60. Epub 2001 Oct 22.

30.

Structural basis for helper T-cell and antibody epitope immunodominance in bacteriophage T4 Hsp10. Role of disordered loops.

Dai G, Carmicle S, Steede NK, Landry SJ.

J Biol Chem. 2002 Jan 4;277(1):161-8. Epub 2001 Oct 15.

32.

Preparation of recombinant human Hsp10.

Steede NK, Guidry JJ, Landry SJ.

Methods Mol Biol. 2000;140:145-51. No abstract available.

PMID:
11484482
33.

Assay of chaperonin-assisted refolding of citrate synthase.

Steede NK, Temkin SL, Landry SJ.

Methods Mol Biol. 2000;140:133-8. No abstract available.

PMID:
11484480
34.

The disordered mobile loop of GroES folds into a defined beta-hairpin upon binding GroEL.

Shewmaker F, Maskos K, Simmerling C, Landry SJ.

J Biol Chem. 2001 Aug 17;276(33):31257-64. Epub 2001 Jun 6.

35.

Reversible denaturation of oligomeric human chaperonin 10: denatured state depends on chemical denaturant.

Guidry JJ, Moczygemba CK, Steede NK, Landry SJ, Wittung-Stafshede P.

Protein Sci. 2000 Nov;9(11):2109-17. Erratum in: Protein Sci 2000 Dec;9(12):2583.

36.

The importance of a mobile loop in regulating chaperonin/ co-chaperonin interaction: humans versus Escherichia coli.

Richardson A, Schwager F, Landry SJ, Georgopoulos C.

J Biol Chem. 2001 Feb 16;276(7):4981-7. Epub 2000 Oct 24.

37.

Domain-specific spectroscopy of 5-hydroxytryptophan-containing variants of Escherichia coli DnaJ.

Greene MK, Steede NK, Landry SJ.

Biochim Biophys Acta. 2000 Jul 14;1480(1-2):267-77.

PMID:
10899627
38.
39.

Basis of substrate binding by the chaperonin GroEL.

Wang Z, Feng Hp, Landry SJ, Maxwell J, Gierasch LM.

Biochemistry. 1999 Sep 28;38(39):12537-46.

PMID:
10504222
40.

Chaperonin function depends on structure and disorder in co-chaperonin mobile loops.

Landry SJ, Steede NK, Garaudy AM, Maskos K, Viitanen PV.

Pac Symp Biocomput. 1999:520-31.

41.

Compensatory changes in GroEL/Gp31 affinity as a mechanism for allele-specific genetic interaction.

Richardson A, van der Vies SM, Keppel F, Taher A, Landry SJ, Georgopoulos C.

J Biol Chem. 1999 Jan 1;274(1):52-8.

42.

Role of the J-domain in the cooperation of Hsp40 with Hsp70.

Greene MK, Maskos K, Landry SJ.

Proc Natl Acad Sci U S A. 1998 May 26;95(11):6108-13.

43.

The ins and outs of a molecular chaperone machine.

Richardson A, Landry SJ, Georgopoulos C.

Trends Biochem Sci. 1998 Apr;23(4):138-43. Review.

PMID:
9584617
44.

Local protein instability predictive of helper T-cell epitopes.

Landry SJ.

Immunol Today. 1997 Nov;18(11):527-32. Review.

PMID:
9386348
45.

Temperature dependence of backbone dynamics in loops of human mitochondrial heat shock protein 10.

Landry SJ, Steede NK, Maskos K.

Biochemistry. 1997 Sep 9;36(36):10975-86.

PMID:
9283089
46.
47.

Interplay of structure and disorder in cochaperonin mobile loops.

Landry SJ, Taher A, Georgopoulos C, van der Vies SM.

Proc Natl Acad Sci U S A. 1996 Oct 15;93(21):11622-7.

48.

The crystal structure of the GroES co-chaperonin at 2.8 A resolution.

Hunt JF, Weaver AJ, Landry SJ, Gierasch L, Deisenhofer J.

Nature. 1996 Jan 4;379(6560):37-45.

PMID:
8538739
49.

Induction of stress proteins in anoxic and hyperthermicSpodoptera frugiperda cells.

Hugler W, O'Connor KC, Landry SJ, Bivins JE.

Cytotechnology. 1995 Jan;17(2):91-101. doi: 10.1007/BF00749396.

PMID:
22358465
50.

Chaperone power in a virus?

Kelley WL, Landry SJ.

Trends Biochem Sci. 1994 Jul;19(7):277-8. No abstract available.

PMID:
7914037

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