Kevin L. Schey, Ph.D.


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Faculty Appointments
Professor of Biochemistry Professor of Ophthalmology and Visual SciencesProfessor of Chemistry
Ph.D., CHEMISTRY, Purdue University, West Lafayette, IndianaB.S., Muhlenberg College, Allentown, Pennsylvania
Office Address
Mass Spectrometry Research Center
Suite 9160, MRB III
465 21st Ave. So.
Nashville, TN 37232
Research Description
The Schey lab is interested in both method/instrument development in proteomics analysis as well as in applications of state-of-the-art proteomics technologies in the study of development and disease. Method development/technology projects include methods for integral membrane protein analysis, tandem mass spectrometry of intact proteins (top-down proteomics), spatially-resolved proteomics analysis, and quantitative proteomics. The major area of application is human lens protein modifications and protein-protein interactions. Other areas of interest are: proteomics analysis of heart valve development, and invertebrate (shrimp and oyster) innate immunity.

Integral membrane proteins play key roles in signaling, transport, and adhesion, yet they remain difficult to analyze using conventional proteomics methods. Our lab has developed methods to analyze integral membrane proteins and membrane associated proteins including their modifications. In addition, we have developed methods for membrane proteome analysis. Currently we are developing methods for spatially-resolved studies (see below), for tissue imaging of membrane proteins, and for examining the membrane protein phosphoproteome.
Standard proteomics analyses typically require tryptic digestion of the protein sample followed by LC/MS/MS analysis of the peptides in order to identify and quantitate the proteins present in the sample. This bottom-up approach relies on inferring protein level information from peptide level measurements. Top-down analysis involves analysis of the intact proteins for identification but requires sophisticated technologies and software. We have developed a method for top-down proteomics analysis in a MALDI TOF-TOF platform and generated a new software application for the interpretation of resulting data.
Spatially-resolved proteomics represents a critically important area of development that takes advantage of recent advances in instrumental sensitivity. The ability to examine region-specific changes in a proteome has wide applicability in both development and disease processes. Two approaches are being developed in our lab to address this issue: 1) laser capture microsdissection (LCM) coupled with shotgun proteomics analysis and 2) MALDI tissue imaging. We have combined our membrane protein analysis protocols with LCM capture to examine region-specific changes in the ocular lens membrane proteome. Also, we have developed new sample preparation methods to allow MALDI imaging of membrane proteins. The MALDI imaging method is being applied to lens aging, chick and mouse heart development, shrimp viral infection, brain changes in addiction, and lung infection.
Our long-standing project on ocular lens membrane proteins is focused on how these proteins change as lens cells differentiate and as they age. Since the proteins in the lens core are as old as the individual, the lens serves as a model tissue to study protein aging. Age- and cataract-specific modifications have been identified and regional changes in the membrane proteome are being examined. Functional consequences of lens protein modification are also being examined with confocal microscopic, molecular biology, and spectroscopic methods.
Research Keywords
Proteomics analysis in development and disease; mass spectrometry technology development.; imaging mass spectrometry
Grant JE, Bradshaw AD, Schwacke JH, Baicu CF, Zile MR, Schey KL. Quantification of protein expression changes in the aging left ventricle of Rattus norvegicus. J. Proteome Res. 2009 Sep; 8(9): 4252-63. PMID: 19603826, PMCID: PMC2752960, DOI: 10.1021/pr900297f, ISSN: 1535-3893.

Grey AC, Schey KL. Age-related changes in the spatial distribution of human lens alpha-crystallin products by MALDI imaging mass spectrometry. Invest. Ophthalmol. Vis. Sci [print-electronic]. 2009 Sep; 50(9): 4319-29. PMID: 19387068, PMCID: PMC2760347, PII: iovs.09-3522, DOI: 10.1167/iovs.09-3522, ISSN: 1552-5783.

Lim JC, Walker KL, Sherwin T, Schey KL, Donaldson PJ. Confocal microscopy reveals zones of membrane remodeling in the outer cortex of the human lens. Invest. Ophthalmol. Vis. Sci [print-electronic]. 2009 Sep; 50(9): 4304-10. PMID: 19357350, PMCID: PMC4572844, PII: iovs.09-3435, DOI: 10.1167/iovs.09-3435, ISSN: 1552-5783.

Xue Q, Itoh N, Schey KL, Cooper RK, La Peyre JF. Evidence indicating the existence of a novel family of serine protease inhibitors that may be involved in marine invertebrate immunity. Fish Shellfish Immunol [print-electronic]. 2009 Aug; 27(2): 250-9. PMID: 19464375, PII: S1050-4648(09)00166-1, DOI: 10.1016/j.fsi.2009.05.006, ISSN: 1095-9947.

Grey AC, Chaurand P, Caprioli RM, Schey KL. MALDI imaging mass spectrometry of integral membrane proteins from ocular lens and retinal tissue. J. Proteome Res. 2009 Jul; 8(7): 3278-83. PMID: 19326924, PMCID: PMC2715141, DOI: 10.1021/pr800956y, ISSN: 1535-3893.

Korlimbinis A, Berry Y, Thibault D, Schey KL, Truscott RJ. Protein aging: truncation of aquaporin 0 in human lens regions is a continuous age-dependent process. Exp. Eye Res [print-electronic]. 2009 May; 88(5): 966-73. PMID: 19135052, PMCID: PMC2713177, PII: S0014-4835(08)00443-0, DOI: 10.1016/j.exer.2008.12.008, ISSN: 1096-0007.

Robalino J, Carnegie RB, O'Leary N, Ouvry-Patat SA, de la Vega E, Prior S, Gross PS, Browdy CL, Chapman RW, Schey KL, Warr G. Contributions of functional genomics and proteomics to the study of immune responses in the Pacific white leg shrimp Litopenaeus vannamei. Vet. Immunol. Immunopathol [print-electronic]. 2009 Mar 3/15/2009; 128(1-3): 110-8. PMID: 19070907, PII: S0165-2427(08)00720-4, DOI: 10.1016/j.vetimm.2008.10.329, ISSN: 0165-2427.

Grey AC, Li L, Jacobs MD, Schey KL, Donaldson PJ. Differentiation-dependent modification and subcellular distribution of aquaporin-0 suggests multiple functional roles in the rat lens. Differentiation [print-electronic]. 2009 Jan; 77(1): 70-83. PMID: 19281766, PMCID: PMC2696237, PII: S0301-4681(08)00004-2, DOI: 10.1016/j.diff.2008.09.003, ISSN: 1432-0436.

Hill EG, Schwacke JH, Comte-Walters S, Slate EH, Oberg AL, Eckel-Passow JE, Therneau TM, Schey KL. A statistical model for iTRAQ data analysis. J. Proteome Res [print-electronic]. 2008 Aug; 7(8): 3091-101. PMID: 18578521, PMCID: PMC2722948, DOI: 10.1021/pr070520u, ISSN: 1535-3893.

Wang Z, Han J, Schey KL. Spatial differences in an integral membrane proteome detected in laser capture microdissected samples. J. Proteome Res [print-electronic]. 2008 Jul; 7(7): 2696-702. PMID: 18489132, PMCID: PMC2740381, DOI: 10.1021/pr700737h, ISSN: 1535-3893.

Thibault DB, Gillam CJ, Grey AC, Han J, Schey KL. MALDI tissue profiling of integral membrane proteins from ocular tissues. J. Am. Soc. Mass Spectrom [print-electronic]. 2008 Jun; 19(6): 814-22. PMID: 18396059, PMCID: PMC2430993, PII: S1044-0305(08)00186-4, DOI: 10.1016/j.jasms.2008.03.002, ISSN: 1044-0305.

Liu Z, Schey KL. Fragmentation of multiply-charged intact protein ions using MALDI TOF-TOF mass spectrometry. J. Am. Soc. Mass Spectrom [print-electronic]. 2008 Feb; 19(2): 231-8. PMID: 17693096, PMCID: PMC2288703, PII: S1044-0305(07)00466-7, DOI: 10.1016/j.jasms.2007.06.006, ISSN: 1044-0305.

Rose KM, Wang Z, Magrath GN, Hazard ES, Hildebrandt JD, Schey KL. Aquaporin 0-calmodulin interaction and the effect of aquaporin 0 phosphorylation. Biochemistry [print-electronic]. 2008 Jan 1/8/2008; 47(1): 339-47. PMID: 18081321, DOI: 10.1021/bi701980t, ISSN: 0006-2960.

Grey AC, Schey KL. Distribution of bovine and rabbit lens alpha-crystallin products by MALDI imaging mass spectrometry. Mol. Vis. 2008; 14: 171-9. PMID: 18334935, PMCID: PMC2254960, PII: v14/a22, ISSN: 1090-0535.

Ouvry-Patat SA, Schey KL. Characterization of antimicrobial histone sequences and posttranslational modifications by mass spectrometry. J Mass Spectrom. 2007 May; 42(5): 664-74. PMID: 17405180, DOI: 10.1002/jms.1200, ISSN: 1076-5174.

Xue QG, Itoh N, Schey KL, Li YL, Cooper RK, La Peyre JF. A new lysozyme from the eastern oyster (Crassostrea virginica) indicates adaptive evolution of i-type lysozymes. Cell. Mol. Life Sci. 2007 Jan; 64(1): 82-95. PMID: 17160350, DOI: 10.1007/s00018-006-6386-y, ISSN: 1420-682X.

Xue QG, Waldrop GL, Schey KL, Itoh N, Ogawa M, Cooper RK, Losso JN, La Peyre JF. A novel slow-tight binding serine protease inhibitor from eastern oyster (Crassostrea virginica) plasma inhibits perkinsin, the major extracellular protease of the oyster protozoan parasite Perkinsus marinus. Comp. Biochem. Physiol. B, Biochem. Mol. Biol [print-electronic]. 2006 Sep; 145(1): 16-26. PMID: 16872855, PII: S1096-4959(06)00139-4, DOI: 10.1016/j.cbpb.2006.05.010, ISSN: 1096-4959.

Han J, Schey KL. MALDI tissue imaging of ocular lens alpha-crystallin. Invest. Ophthalmol. Vis. Sci. 2006 Jul; 47(7): 2990-6. PMID: 16799044, PII: 47/7/2990, DOI: 10.1167/iovs.05-1529, ISSN: 0146-0404.

DiNovo AA, Schey KL, Vachon WS, McGuffie EM, Olson JC, Vincent TS. ADP-ribosylation of cyclophilin A by Pseudomonas aeruginosa exoenzyme S. Biochemistry. 2006 Apr 4/11/2006; 45(14): 4664-73. PMID: 16584201, DOI: 10.1021/bi0513554, ISSN: 0006-2960.

Lindsey Rose KM, Gourdie RG, Prescott AR, Quinlan RA, Crouch RK, Schey KL. The C terminus of lens aquaporin 0 interacts with the cytoskeletal proteins filensin and CP49. Invest. Ophthalmol. Vis. Sci. 2006 Apr; 47(4): 1562-70. PMID: 16565393, PII: 47/4/1562, DOI: 10.1167/iovs.05-1313, ISSN: 0146-0404.

Cook LA, Schey KL, Wilcox MD, Dingus J, Ettling R, Nelson T, Knapp DR, Hildebrandt JD. Proteomic analysis of bovine brain G protein gamma subunit processing heterogeneity. Mol. Cell Proteomics [print-electronic]. 2006 Apr; 5(4): 671-85. PMID: 16332732, PII: M500223-MCP200, DOI: 10.1074/mcp.M500223-MCP200, ISSN: 1535-9476.

Karnaukhova E, Schey KL, Crouch RK. Circular dichroism and cross-linking studies of bacteriorhodopsin mutants. Amino Acids [print-electronic]. 2006 Feb; 30(1): 17-23. PMID: 16477391, DOI: 10.1007/s00726-005-0255-0, ISSN: 0939-4451.

Liu Z, Schey KL. Optimization of a MALDI TOF-TOF mass spectrometer for intact protein analysis. J. Am. Soc. Mass Spectrom. 2005 Apr; 16(4): 482-90. PMID: 15792717, PII: S1044-0305(04)00853-0, DOI: 10.1016/j.jasms.2004.12.018, ISSN: 1044-0305.

Ervin LA, Ball LE, Crouch RK, Schey KL. Phosphorylation and glycosylation of bovine lens MP20. Invest. Ophthalmol. Vis. Sci. 2005 Feb; 46(2): 627-35. PMID: 15671292, PII: 46/2/627, DOI: 10.1167/iovs.04-0894, ISSN: 0146-0404.

Patat SA, Carnegie RB, Kingsbury C, Gross PS, Chapman R, Schey KL. Antimicrobial activity of histones from hemocytes of the Pacific white shrimp. Eur. J. Biochem. 2004 Dec; 271(23-24): 4825-33. PMID: 15606770, PII: EJB4448, DOI: 10.1111/j.1432-1033.2004.04448.x, ISSN: 0014-2956.

Xue QG, Schey KL, Volety AK, Chu FL, La Peyre JF. Purification and characterization of lysozyme from plasma of the eastern oyster (Crassostrea virginica). Comp. Biochem. Physiol. B, Biochem. Mol. Biol. 2004 Sep; 139(1): 11-25. PMID: 15364284, PII: S1096-4959(04)00178-2, DOI: 10.1016/j.cbpc.2004.05.011, ISSN: 1096-4959.

Ball LE, Garland DL, Crouch RK, Schey KL. Post-translational modifications of aquaporin 0 (AQP0) in the normal human lens: spatial and temporal occurrence. Biochemistry. 2004 Aug 8/3/2004; 43(30): 9856-65. PMID: 15274640, DOI: 10.1021/bi0496034, ISSN: 0006-2960.

Han J, Schey KL. Proteolysis and mass spectrometric analysis of an integral membrane: aquaporin 0. J. Proteome Res. 2004 Jul; 3(4): 807-12. PMID: 15359735, ISSN: 1535-3893.

Han J, Little M, David LL, Giblin FJ, Schey KL. Sequence and peptide map of guinea pig aquaporin 0. Mol. Vis. 2004 Mar 3/26/2004; 10: 215-22. PMID: 15064681, PII: v10/a27, ISSN: 1090-0535.

Ball LE, Little M, Nowak MW, Garland DL, Crouch RK, Schey KL. Water permeability of C-terminally truncated aquaporin 0 (AQP0 1-243) observed in the aging human lens. Invest. Ophthalmol. Vis. Sci. 2003 Nov; 44(11): 4820-8. PMID: 14578404, ISSN: 0146-0404.

Hamilton MH, Cook LA, McRackan TR, Schey KL, Hildebrandt JD. Gamma 2 subunit of G protein heterotrimer is an N-end rule ubiquitylation substrate. Proc. Natl. Acad. Sci. U.S.A [print-electronic]. 2003 Apr 4/29/2003; 100(9): 5081-6. PMID: 12700354, PMCID: PMC154301, PII: 0831228100, DOI: 10.1073/pnas.0831228100, ISSN: 0027-8424.

Walgren JL, Vincent TS, Schey KL, Buse MG. High glucose and insulin promote O-GlcNAc modification of proteins, including alpha-tubulin. Am. J. Physiol. Endocrinol. Metab [print-electronic]. 2003 Feb; 284(2): E424-34. PMID: 12397027, PII: 00382.2002, DOI: 10.1152/ajpendo.00382.2002, ISSN: 0193-1849.

Muradov KG, Granovsky AE, Schey KL, Artemyev NO. Direct interaction of the inhibitory gamma-subunit of Rod cGMP phosphodiesterase (PDE6) with the PDE6 GAFa domains. Biochemistry. 2002 Mar 3/26/2002; 41(12): 3884-90. PMID: 11900530, PII: bi015935m, ISSN: 0006-2960.

Nishida M, Schey KL, Takagahara S, Kontani K, Katada T, Urano Y, Nagano T, Nagao T, Kurose H. Activation mechanism of Gi and Go by reactive oxygen species. J. Biol. Chem [print-electronic]. 2002 Mar 3/15/2002; 277(11): 9036-42. PMID: 11781308, PII: M107392200, DOI: 10.1074/jbc.M107392200, ISSN: 0021-9258.

Schey KL, Busman M, Cook LA, Hamm HE, Hildebrandt JD. Structural characterization of intact G protein gamma subunits by mass spectrometry. Meth. Enzymol. 2002; 344: 586-97. PMID: 11771413, ISSN: 0076-6879.

McIntire WE, Schey KL, Knapp DR, Dingus J, Hildebrandt JD. Characterization of deamidated G protein subunits. Meth. Enzymol. 2002; 344: 481-505. PMID: 11771405, ISSN: 0076-6879.

Cook LA, Wilcox MD, Dingus J, Schey KL, Hildebrandt JD. Separation and analysis of G protein gamma subunits. Meth. Enzymol. 2002; 344: 209-33. PMID: 11771385, ISSN: 0076-6879.

Morinelli TA, Meier GP, Schey KL, Margolius HS. Radioiodination of the stable metabolic fragment of bradykinin, RPPGF. Peptides. 2001 Dec; 22(12): 2169-74. PMID: 11786206, PII: S0196978101005459, ISSN: 0196-9781.

Cook LA, Schey KL, Cleator JH, Wilcox MD, Dingus J, Hildebrandt JD. Identification of a region in G protein gamma subunits conserved across species but hypervariable among subunit isoforms. Protein Sci. 2001 Dec; 10(12): 2548-55. PMID: 11714923, PMCID: PMC2374038, DOI: 10.1110/, ISSN: 0961-8368.

Roberts JE, Finley EL, Patat SA, Schey KL. Photooxidation of lens proteins with xanthurenic acid: a putative chromophore for cataractogenesis. Photochem. Photobiol. 2001 Nov; 74(5): 740-4. PMID: 11723804, ISSN: 0031-8655.

Schey KL, Patat S, Chignell CF, Datillo M, Wang RH, Roberts JE. Photooxidation of lens alpha-crystallin by hypericin (active ingredient in St. John's Wort). Photochem. Photobiol. 2000 Aug; 72(2): 200-3. PMID: 10946573, ISSN: 0031-8655.

Schey KL, Finley EL. Identification of peptide oxidation by tandem mass spectrometry. Acc. Chem. Res. 2000 May; 33(5): 299-306. PMID: 10813874, PII: ar9800744, ISSN: 0001-4842.

Schey KL, Little M, Fowler JG, Crouch RK. Characterization of human lens major intrinsic protein structure. Invest. Ophthalmol. Vis. Sci. 2000 Jan; 41(1): 175-82. PMID: 10634618, ISSN: 0146-0404.

Schey KL, Fowler JG, Shearer TR, David L. Modifications to rat lens major intrinsic protein in selenite-induced cataract. Invest. Ophthalmol. Vis. Sci. 1999 Mar; 40(3): 657-67. PMID: 10067969, ISSN: 0146-0404.

McIntire WE, Dingus J, Schey KL, Hildebrandt JD. Characterization of the major bovine brain Go alpha isoforms. Mapping the structural differences between the alpha subunit isoforms identifies a variable region of the protein involved in receptor interactions. J. Biol. Chem. 1998 Dec 12/11/1998; 273(50): 33135-41. PMID: 9837880, ISSN: 0021-9258.

Finley EL, Dillon J, Crouch RK, Schey KL. Identification of tryptophan oxidation products in bovine alpha-crystallin. Protein Sci. 1998 Nov; 7(11): 2391-7. PMID: 9828005, PMCID: PMC2143850, DOI: 10.1002/pro.5560071116, ISSN: 0961-8368.

McIntire WE, Schey KL, Knapp DR, Hildebrandt JD. A major G protein alpha O isoform in bovine brain is deamidated at Asn346 and Asn347, residues involved in receptor coupling. Biochemistry. 1998 Oct 10/20/1998; 37(42): 14651-8. PMID: 9778339, PII: bi981642q, DOI: 10.1021/bi981642q, ISSN: 0006-2960.

Cook LA, Schey KL, Wilcox MD, Dingus J, Hildebrandt JD. Heterogeneous processing of a G protein gamma subunit at a site critical for protein and membrane interactions. Biochemistry. 1998 Sep 9/1/1998; 37(35): 12280-6. PMID: 9724542, PII: bi980230e, DOI: 10.1021/bi980230e, ISSN: 0006-2960.

Pawate S, Schey KL, Meier GP, Ullian ME, Mais DE, Halushka PV. Expression, characterization, and purification of C-terminally hexahistidine-tagged thromboxane A2 receptors. J. Biol. Chem. 1998 Aug 8/28/1998; 273(35): 22753-60. PMID: 9712907, ISSN: 0021-9258.

Finley EL, Dillon J, Crouch RK, Schey KL. Radiolysis-induced oxidation of bovine alpha-crystallin. Photochem. Photobiol. 1998 Jul; 68(1): 9-15. PMID: 9679446, ISSN: 0031-8655.

Finley EL, Busman M, Dillon J, Crouch RK, Schey KL. Identification of photooxidation sites in bovine alpha-crystallin. Photochem. Photobiol. 1997 Nov; 66(5): 635-41. PMID: 9383987, ISSN: 0031-8655.

Schey KL, Fowler JG, Schwartz JC, Busman M, Dillon J, Crouch RK. Complete map and identification of the phosphorylation site of bovine lens major intrinsic protein. Invest. Ophthalmol. Vis. Sci. 1997 Nov; 38(12): 2508-15. PMID: 9375569, ISSN: 0146-0404.

Swamy-Mruthinti S, Schey KL. Mass spectroscopic identification of in vitro glycated sites of MIP. Curr. Eye Res. 1997 Sep; 16(9): 936-41. PMID: 9288456, ISSN: 0271-3683.

Artemyev NO, Natochin M, Busman M, Schey KL, Hamm HE. Mechanism of photoreceptor cGMP phosphodiesterase inhibition by its gamma-subunits. Proc. Natl. Acad. Sci. U.S.A. 1996 May 5/28/1996; 93(11): 5407-12. PMID: 8643588, PMCID: PMC39259, ISSN: 0027-8424.

Schey KL. Hydrophobic proteins and peptides analyzed by matrix-assisted laser desorption/ionization. Methods Mol. Biol. 1996; 61: 227-30. PMID: 8930876, DOI: 10.1385/0-89603-345-7:227, ISSN: 1064-3745.

Wilcox MD, Schey KL, Busman M, Hildebrandt JD. Determination of the complete covalent structure of the gamma 2 subunit of bovine brain G proteins by mass spectrometry. Biochem. Biophys. Res. Commun. 1995 Jul 7/17/1995; 212(2): 367-74. PMID: 7626050, PII: S0006-291X(85)71979-1, DOI: 10.1006/bbrc.1995.1979, ISSN: 0006-291X.

Wilcox MD, Dingus J, Balcueva EA, McIntire WE, Mehta ND, Schey KL, Robishaw JD, Hildebrandt JD. Bovine brain GO isoforms have distinct gamma subunit compositions. J. Biol. Chem. 1995 Mar 3/3/1995; 270(9): 4189-92. PMID: 7876173, ISSN: 0021-9258.

Wilcox MD, Schey KL, Dingus J, Mehta ND, Tatum BS, Halushka M, Finch JW, Hildebrandt JD. Analysis of G protein gamma subunit heterogeneity using mass spectrometry. J. Biol. Chem. 1994 Apr 4/29/1994; 269(17): 12508-13. PMID: 8175659, ISSN: 0021-9258.

Busman M, Knapp DR, Schey KL. Observation of large multimers in the electrospray ionization mass spectrometry of peptides. Rapid Commun. Mass Spectrom. 1994 Feb; 8(2): 211-6. PMID: 8155900, DOI: 10.1002/rcm.1290080217, ISSN: 0951-4198.

Artemyev NO, Mills JS, Thornburg KR, Knapp DR, Schey KL, Hamm HE. A site on transducin alpha-subunit of interaction with the polycationic region of cGMP phosphodiesterase inhibitory subunit. J. Biol. Chem. 1993 Nov 11/5/1993; 268(31): 23611-5. PMID: 8226888, ISSN: 0021-9258.

Finch JW, Crouch RK, Knapp DR, Schey KL. Mass spectrometric identification of modifications to human serum albumin treated with hydrogen peroxide. Arch. Biochem. Biophys. 1993 Sep; 305(2): 595-9. PMID: 8373198, PII: S0003-9861(83)71466-9, DOI: 10.1006/abbi.1993.1466, ISSN: 0003-9861.

McMillan DC, Schey KL, Meier GP, Jollow DJ. Chemical analysis and hemolytic activity of the fava bean aglycon divicine. Chem. Res. Toxicol. 1993 Jul; 6(4): 439-44. PMID: 8374040, ISSN: 0893-228X.

Walle T, Walle UK, Thornburg KR, Schey KL. Stereoselective sulfation of albuterol in humans. Biosynthesis of the sulfate conjugate by HEP G2 cells. Drug Metab. Dispos. 1993 Jan; 21(1): 76-80. PMID: 8095231, ISSN: 0090-9556.

Schey KL, Papac DI, Knapp DR, Crouch RK. Matrix-assisted laser desorption mass spectrometry of rhodopsin and bacteriorhodopsin. Biophys. J. 1992 Nov; 63(5): 1240-3. PMID: 1477275, PMCID: PMC1261426, PII: S0006-3495(92)81699-5, DOI: 10.1016/S0006-3495(92)81699-5, ISSN: 0006-3495.

Papac DI, Schey KL, Knapp DR. Combination electrospray-liquid secondary ion mass spectrometry ion source. Anal. Chem. 1991 Aug 8/1/1991; 63(15): 1658-60. PMID: 1952088, ISSN: 0003-2700.

Grey AC and Schey KL. Age-related Changes in the Spatial Distribution of Human Lens Alpha-Crystallin Products by MALDI Imaging Mass Spectrometry. Invest. Ophthalmol. Vis. Sci. in press.

Lim J, Walker K, Sherwin T, Schey KL, Donaldson P. Confocal Microscopy Reveals a Zone of Membrane Remodelling in the Outer Cortex of the Human Lens. Invest. Ophthalmol. Vis. Sci. in press.

Grant, JE, Bradshaw AD, Schwacke JH, Baicu CF, Zile MR, Schey KL. Quantification of Protein Expression Changes in the Aging Left Ventricle of Rattus norvegicus. J. Proteom. Res. in press.

Wang Z and Schey KL. Phosphorylation and Truncation Sites of Bovine Lens Connexin 46 and Connexin 50. Exp. Eye Res. in press.

Available Postdoctoral Position Details
Posted: 1/3/2012
A post-doctoral training position is available to develop MALDI imaging mass spectrometry methods for ocular lens tissue. A special focus is on lens proteins, lipids, and metabolites and their changing distributions with age. Other tissues of interest are retina, lung and heart.