Marianne Schiffer

Publications by Author, Select Publication Author		Quick Link Maryka Bhattacharyya Liaohai Chen Frank Collart Mark Donnelly Robert F. Fischetti Carol Giometti David Glesne Deborah Hanson Andrzej Joachimiak Brian K. Kay Kenneth Kemner Philip Laible Lee Makowski Diane J. Rodi Marianne Schiffer Fred J. Stevens Rosemarie Wilton

1. Schiffer, M.  The determination of the crystal and molecular structure of DL-&beta-fluoromalic acid by x-ray diffraction.  Ph.D. Thesis, Columbia University (1965).
   
   
2. Monahan, J. E., M. Schiffer, and J. P. Schiffer.  On the scaling of x-ray     photographs.  Acta Cryst. 22, 322 (1967).
   
   
3. Schiffer, M., and A. B. Edmundson.  Use of helical wheels to represent the structures of proteins and to identify segments with helical potential.  Biophys. J. 7:121-135 (1967).
   
   
4. Schiffer, M. and A.B. Edmundson.  Correlation of amino acid sequence and conformation in tobacco mosaic virus.  Biophys. J. 8:29-39 (1968).
   
   
5. Schiffer, M., K. D. Hardman, M. K. Wood, A. B. Edmundson, M. E. Hook, K. R. Ely, and H. F. Deutsch.  A preliminary crystallographic investigation of a human &lambda-type Bence-Jones protein.  J. Biol. Chem. 245:728-730 (1970).
   
   
6. Edmundson, A.B., M.K. Wood, M. Schiffer, K.D. Hardman, C.F. Ainsworth, K.R. Ely, and H.F. Deutsch.  A crystallographic investigation of a human IGG immunoglobulin.  J. Biol. Chem. 245:2763-2764 (1970).
   
   
7. Schiffer, M. and A. B. Edmundson.  Prediction of a-helices in glucagon.  Biophys. J. 10:293-295 (1970).
   
   
8. Hardman, K.D., M.K. Wood, M. Schiffer, A.B. Edmundson, and C. Ainsworth.  Structure of concanavalin A at  4.25Å resolution.  Proc. Natl. Acad. Sci. USA 68:1393-1397 (1971).
   
   
9. Edmundson, A.B., M. Schiffer, M.K. Wood, K.D. Hardman, K.R. Ely, and C.F. Ainsworth.  Crystallographic studies of an Igg immunoglobulin and the Bence-Jones protein from one patient.  Cold Spring Harbor Symposium on Quantum Biology, Vol. 36, pp. 427-432 (1971).
   
   
10. Edmundson, A.B., M. Schiffer, K.R. Ely, and M.K. Wood.  Structure of a Lambda-type Bence-Jones protein at 6 Å resolution.  Biochemistry 11:1822-1827 (1972).
    
    
11. Ely, K.R., R.L. Girling, M. Schiffer, D.E. Cunningham, and A.B. Edmundson.  Preparation and properties of  crystals of a Bence-Jones dimer with mercury inserted into the interchain disulfide bond.  Biochemistry 12:4233-4237 (1973).
    
    
12. Schiffer, M., R. L. Girling, K. R. Ely, and A. B. Edmundson.  Structure of a lambda-type Bence-Jones protein at 3.5 angstrom resolution.  Biochemistry 12:4620-4631 (1973).
    
    
13. Colman, P.M., O. Epp, H. Fehlhammer, W. Bode, M. Schiffer, E.E. Lattman, T.A. Jones, and W. Palm.  X-ray studies on antibody fragments.  FEBS Lett. 44:194-199 (1974).
    
    
14. Edmundson, A.B., K.R. Ely, R.L. Girling, E.E. Abola, M. Schiffer, F.A. Westholm, M.D. Fausch, and H.F. Deutsch.  Binding of 2,4-dinitrophenyl compounds and other small molecules to a crystalline lambda-type Bence-Jones dimer.  Biochemistry 13:3816-3827 (1974).
    
    
15. Edmundson, A.B., K.R. Ely, R.L. Girling, E.E. Abola, M. Schiffer, and F.A. Westholm.  Structure and binding properties of a Lambda-type Bence-Jones dimer.  Progress in Immunology II, Vol. 1, L. Brent and J. Holborow, eds., North-Holland Publishing Company, Amsterdam, The Netherlands, pp. 103-113 (1974).
    
    
16. Epp, O., P.M. Colman, H. Fehlhammer, W. Bode, M. Schiffer, R. Huber, and W. Palm.  Crystal and molecular structure of a dimer composed of the variable portion of the Bence-Jones protein Rei.  Eur. J. Biochem. 45:513-524 (1974).
    
    
17. Fehlhammer, H., M. Schiffer, O. Epp, P. M. Colman, E. E. Lattman, P. Schwager, and W. Steigemann.  The structure determination of the variable portion of the Bence-Jones protein Au.  Biophys. Struct. Mech. 1:139-146 (1975).
    
    
18. Epp, O., E. E. Lattman, M. Schiffer, R. Huber, and W. Palm.  The molecular structure of a dimer composed of the variable portions of the Bence-Jones protein Rei refined at 2.0 Å resolution.  Biochemistry 14:4943-4952 (1975).
    
    
19. Edmundson, A.B., K.R. Ely, E.E. Abola, M. Schiffer, and N. Pangiotopoulos.  Rotational allomerism and divergent evolution of domains in immunoglobulin light chains.  Biochemistry 14:3953-3961 (1975).
    
    
20. Edmundson, A.B., K.R. Ely, E.E. Abola, M. Schiffer, N. Panagiotopoulos, and H.F. Deutsch.  Conformational isomerism, rotational allomerism, and divergent evolution in immunoglobulin light chains.  Fed. Proc. 35:2119-2123 (1976).
    
    
21. Schiffer, M., F. A. Westholm, N. Panagiotopoulos, and A. Solomon.  Crystallographic data on a complete kappa-type human Bence-Jones protein.  J. Molec. Biol. 124:287-290 (1978).
    
    
22. Ely, K.R., J.R. Firca, K.J. Williams, E.E. Abola, J.M. Fenton, M. Schiffer, N. Panagiotopoulos, and A.B. Edmundson.  Crystal properties as indicators of conformational changes during T ligand binding or interconversion of Mcg light chain isomers.  Biochemistry 17:158-167 (1978).
    
    
23. Stevens, F. J., F. A. Westholm, A. Solomon, and M. Schiffer.  Self-association of human immunoglobulin kappa-I light chains: role of the third hypervariable region.  Proc. Natl. Acad. Sci. USA 77:1144-1148 (1980).
    
    
24. Schiffer, M.  Possible distortion of antibody binding site of the Mcg Bence-Jones protein by lattice forces.  Biophys. J. 20:230-232 (1980).
    
    
25. Stevens, F. J., F. A. Westholm, N. Panagiotopoulos, A. Solomon, and M. Schiffer.  Preliminary crystallographic data on the human lambda-III Bence-Jones dimer Cle.  J. Mol. Biol. 147:179-183 (1981).
    
    
26. Stevens, F.J. and M. Schiffer.  Computer simulation of protein self-association during small-zone gel filtration: Estimation of equilibrium constants.  Biochem. J. 195:213-219 (1981).
    
    
27. Stevens, F.J., F. A. Westholm, N. Panagiotopoulos, M. Schiffer, R. A. Popp, and A. Solomon.  Characterization and preliminary crystallographic data for the VL related fragment of the human kappa-I Bence-Jones protein Wat.  J. Mol. Biol. 147:185-193 (1981).
    
    
28. Schiffer, M., F. J. Stevens, F. A. Westholm, S. S. Kim, and R. D. Carlson.  Small angle neutron scattering study of Bence-Jones protein Mcg: comparison of structures in solution and in the crystal.  Biochemistry 21:2874-2878 (1982).
    
    
29. Gast, P., M. R. Wasielewski, M. Schiffer, and J. R. Norris.  Orientation of the primary donor in single crystals of Rhodopseudomonas viridis reaction centres.  Nature 305:451-452 (1983).
    
    
30. Chang, C.-H., M. T. Short, F. A. Westholm, F. J. Stevens, B.-C. Wang, W. Furey, A. Solomon, and M. Schiffer.  Novel arrangement of immunoglobulin variable domains: x-ray crystallographic analysis of the &lambda chain dimer, Bence-Jones protein Loc.  Biochemistry 24:4890-4897 (1985).
    
    
31. Chang, C.-H., M. Schiffer, D. Tiede, U. Smith, and J. Norris.  Characterization of bacterial photosynthetic reaction center crystals from Rhodopseudomonas sphaeroides R-26 by x-ray diffraction.  J. Mol. Biol. 186:201-203 (1985).
    
    
32. Schiffer, M., C.-H. Chang, and F. J. Stevens.  Formation of an infinite b-sheet arrangement dominates the crystallization behavior of &lambdal-type antibody light chains.  J. Mol. Biol. 186:475-478 (1985).
    
    
33. Short, M.T., F.A. Westholm, M. Schiffer, and F.J. Stevens.  Comparison of chromatographic characteristics of a series of homologous Bence-Jones proteins during size-exclusion chromatography by high-performance liquid chromatography by high-performance liquid chromatography and by sephadex.  J. Chromatog. 323:418-423 (1985).
    
    
34. Chang, C.-H., D. Tiede, J. Tang, U. Smith, J. Norris, and M. Schiffer.  Structure of Rhodopseudomonas sphaeroides R-26 reaction center.  FEBS Lett. 205:82-86 (1986).
    
    
35. Schiffer, M., T.T. Wu, and E. A. Kabat.  Subgroups of variable region genes of &lambda-chains of T-cell receptors for antigen.  Proc. Natl. Acad. Sci. USA 83:4461-4463 (1986).
    
    
36. Stevens, F.J., J. Jwo, W.E. Carperos, H. Kohler, and M. Schiffer.  Relationships between liquid- and solid-phase antibody association characteristics: Implications for the use of competitive ELISA techniques to map the spatial location of itiotopes.  J. Immunol. 137:1937-1944 (1986).
    
    
37. Schiffer, M., C.-H. Chang, V. M. Naik, and F. Stevens.  Analysis of immunoglobulin domain interactions: Evidence for a dominant role of salt bridges.  J. Mol. Biol. 203:799-802 (1988).
    
    
38. Stevens, F. J., C.-H. Chang, and M. Schiffer.  Dual conformations of an immunoglobulin light chain dimer: heterogeneity of antigen specificity and idiotope profile may result from multiple variable domain interaction mechanisms.  Proc. Natl. Acad. Sci. USA 85:6895-6899 (1988).
    
    
39. Schiffer, M., C. Ainsworth, Z.-B. Xu, W. Carperos, K. Olsen, A. Solomon, F. J. Stevens, and C.-H. Chang.  Structure of a second crystal form of Bence-Jones protein Loc: strikingly different domain associations in two crystal forms of a single protein.  Biochemistry 28:4066-4072 (1989).
    
    
40. Arnoux, B., A. Ducruix, F. Reiss-Husson, M. Lutz, J. Norris, and M. Schiffer.  Structure of spheroidene in the photosynthetic reaction center from Y Rhodobacter sphaeroides.  FEBS Lett. 258:47-50 (1989).
    
    
41. Norris, J.R., D.E. Budil, P. Gast, C.-H. Chang, O. El-Kabbani, and M. Schiffer.  Correlation of paramagnetic states and molecular structure in bacterial photosynthetic reaction centers: The symmetry of the primary electron donor in Rhodopseudomonas viridis and Rhodobacter sphaeroides R-26.  Proc. Natl. Acad. Sci. USA 86:4335-4339 (1989).
    
    
42. Xu, Z.-B., C.-H. Chang, and M. Schiffer.  Testing the procedure of simulated annealing by refining homologous immunoglobulin light-chain dimers.  Protein Eng. 3:583-589 (1990).
    
    
43. Norris, J.R. and M. Schiffer.  Photosynthetic reaction centers in bacteria.  C&E News 68:22-37 (1990).
    
    
44. Chang, C.-H., O. El-Kabbani, D. Tiede, J. Norris, and M. Schiffer.  Structure of the membrane-bound protein photosynthetic reaction center from Rhodobacter sphaeroides.  Biochemistry 30:5352-5360 (1991).
    
    
45. El-Kabbani, O., C.-H. Chang, D. Tiede, J. Norris, and M. Schiffer.  Comparison of reaction centers from Rhodobacter sphaeroides and Rhodopseudomonas viridis: overall architecture and protein-pigment interactions.  Biochemistry 30:5361-5369 (1991).
    
    
46. Stevens, F. J., A. Solomon, and M. Schiffer.  Bence Jones proteins: A powerful tool for the fundamental study of protein chemistry and pathophysiology.  Biochemistry 30:6803-6805 (1991).
    
    
47. Chan, C.-K., L.X.-Q. Chen, T.J. DiMagno, D.K. Hanson, S.L. Nance, M. Schiffer, J.R. Norris, and G.R. Fleming.  Initial electron transfer in photosynthetic reaction centers of Rhodobacter capsulatus mutants.  Chem. Phys. Lett. 176:366-372 (1991).
    
    
48. Schiffer, M., E. A. Kabat, and T. T. Wu.  Subgroups of Tcr &alpha chains and correlation with T-cell function.  Immunogenetics 35:224-234 (1992).
    
    
49. Schiffer, M., C.-H. Chang, and F. J. Stevens.  The functions of tryptophan residues in membrane proteins.  Protein Engineering 5:213-214 (1992).
    
    
50. Du, M., S.J. Rosenthal, X. Xie, T.J. DiMagno, M. Schmidt, D.K. Hanson, M. Schiffer, J.R. Norris, and G.R. Fleming.  Femtosecond spontaneous-emission studies of reaction centers from photosynthetic bacteria.  Proc. Natl. Acad. Sci. USA 89:8517-8521 (1992).
    
    
51. Hanson, D.K., L. Baciou, D.M. Tiede, S.L. Nance, M. Schiffer, and P. Sebban.  In bacterial reaction centers protons can diffuse to the secondary quinone by alternative pathways.  Biochem. Biophys. Acta 1102:260-265 (1992).
    
    
52. Hanson, D.K., S.L. Nance, and M. Schiffer.  Second-site mutation at M43 (Asn &rarr Asp) compensates for the loss of two acidic residues in the Q_B site of the reaction center.  Photosyn. Res. 32:147-153 (1992).
    
    
53. Hanson, D. K., D. M. Tiede, S. L. Nance, C.-H. Chang, and M. Schiffer.  Site-specific and compensatory mutations imply unexpected pathways for proton delivery to the Q_B binding site of the photosynthetic reaction center.  Proc. Natl. Acad. Sci. USA 90:8929-8933 (1993).
    
    
54. Jia, Y., T.J. DiMagno, C.-K. Chan, Z. Wang, M.S. Popov, M.S. Du, D.K. Hanson, M. Schiffer, J.R. Norris, and G.R. Fleming.   Primary charge separation in mutant reaction centers of Rhodobacter capsulatus.  J. Phys. Chem. 97:13180-13191 (1993).
    
    
55. Ermler, U., H. Michel, and M. Schiffer.  Structure and function of the photosynthetic reaction center from Rhodobacter sphaeroides.  J. Bioenerg. Biomemb. 26:5-15 (1994).
    
    
56. Myatt, E. A., F. A. Westholm, D. T. Weiss, A. Solomon, M. Schiffer, and F. J. Stevens.  Pathogenic potential of human monoclonal immunoglobulin light chains: relationship of in vitro aggregation to in vivo organ deposition.  Proc. Natl. Acad. Sci. USA 91:3034-3038 (1994).
    
    
57. Maróti, P., D.K. Hanson, L. Baciou, M. Schiffer, and P. Sebban.  Proton conduction within the reaction centers of Rhodobacter capsulatus: The electrostatic role of the protein.  Proc. Natl. Acad. Sci. USA 91:5617-5621 (1994).
    
    
58. Li, D., F.J. Stevens, M. Schiffer, and L.E. Anderson.  Mechanism of light modulation: Identification of potential redox-sensitive cysteines distal to catalytic site in light-activated chloroplast enzymes.  Biophys. J. 67:29-35 (1994).
    
    
59. Huang, D.-B., C.-H. Chang, C. Ainsworth, A. T. Brünger, M. Eulitz, A. Solomon, F. J. Stevens, and M. Schiffer.  Comparison of crystal structures of two homologous proteins: structural origin of altered domain interactions in immunoglobulin light-chain dimers.  Biochemistry 33:14848-14857 (1994).
    
    
60. Rosenbach-Belkin, V., A. Scherz, T.J. Michalski, M. Schiffer, and J.R. Norris.  The effect of peripheral substitution on the bathochromic shift of the Qy transition of bacteriochlorophyll dimers: in vitro models of the protein effect on the spectrum of pigment centers in the light-harvesting complexes.  Photochem. Photobiol. 59:579-583 (1994).
    
    
61. Wilkins-Stevens, P., R. Raffen, D. K. Hanson, Y.-L. Deng, M. Berrios-Hammond, F.A. Westholm, C. Murphy, M. Eulitz, R. Wetzel, A. Solomon, M. Schiffer, and F.J. Stevens.  Recombinant immunoglobulin variable domains generated from synthetic genes provide a system for in vitro characterization of light-chain amyloid proteins.  Protein Science 4:421-432 (1995).
    
    
62. Muslin, E.H., D. Li, F.J. Stevens, M. Donnelly, M. Schiffer, and L. Anderson.  Engineering a domain-locking disulfide into a bacterial malate dehydrogenase produces a redox-sensitive enzyme.  Biophys. J. 68:2218-2223 (1995).
    
    
63. Stevens, F.J., E.A. Myatt, C.-H. Chang,  F.A. Westholm, D. Weiss, A. Solomon, and M. Schiffer.  A molecular model for the formation of amyloid: Immunoglobulin light chains.  Biochemistry 34:10697-10702 (1995).
    
    
64. Sebban, P., P. Maróti, M. Schiffer, D. K. Hanson.  Electrostatic Dominoes: Long Distance Propagation of Mutational Effects in Photosynthetic Reaction Centers of Rhodobacter capsulatus.  Biochemistry 34:8390-8397 (1995).
    
    
65. Maroti, P., D.K. Hanson, M. Schiffer, and P. Sebban.  Long-range electrostatic interaction in the bacterial photosynthetic reaction centre.  Nature Struct. Biol. 2:1057-1059 (1995).
    
    
66. Schiffer, M., C.F. Ainsworth, Y.-L. Deng, G. Johnson, F. H. Pascoe, and D. K. Hanson. Proline in a transmembrane helix compensates for cavities in the photosynthetic reaction center. J. Mol. Biol. 252:472-482 (1995).
    
    
67. Muslin, E.H., D. Li, F.J. Stevens, M. Donnelly, M. Schiffer, and L. Anderson.  Engineering a domain-locking disulfide into a bacterial malate dehydrogenase produces a redox-sensitive enzyme.  Biophys. J. 68:2218-2223 (1995).
    
    
68. Boernke, W.E., C. Sanville Millard, S.N. Kakar, V. Jackiw, M. Schiffer, F.J. Stevens, and M.I. Donnelly. Stringency of substrate specificity of Escherichia coli malate dehydrogenase.  Arch. Biochem. Biophys. 322:43-52 (1995).
    
    
69. Schiffer, M., D.-B. Huang, C. Ainsworth, and F.J. Stevens.  Three quaternary structures for a single protein.  Proc. Natl. Acad. Sci. USA 93:7017-7021 (1996).
    
    
70. Huang, D.-B., C. Ainsworth, A. Solomon, and M. Schiffer.  Pitfalls of molecular replacement: The structure determination of an immunoglobulin light-chain dimer.  Acta. Cryst. D52:1058-1066 (1996).
    
    
71. Rajagoplan, K., G. Pavlinkova, S. Levy, P.R. Pokkuluri, M. Schiffer, B.E. Halley, and H. Kohler.  Novel unconventional binding site in the variable region of immunoglobulin.  Proc. Natl. Acad. Sci. USA 93:6019-6024 (1996).
    
    
72. Schiffer, M.  Commentary: Molecular anatomy and the pathological expression of antibody light chains.  Am. J. Pathol. 148:1339-1344 (1996).
    
73. Huang, D.-B., C.A. Ainsworth, F.J. Stevens, and M. Schiffer.  Three quaternary structures for a single protein. Proc. Natl. Acad. Sci. USA 93:7017-7021 (1996).
    
    
74. Miksovska, J., P. Maróti, J. Tandori, M. Schiffer, D.K. Hanson, and P. Sebban.  Modulation of the free energy level of QA- by distant electrostatic interactions in the photosynthetic reaction center.  Biochemistry 35:15411-15417 (1996).
    
    
75. Anderson, L.E., D. Li, E.H. Muslin, F.J. Stevens, and M. Schiffer.  Predicting redox-sensitive cysteines in plant enzymes by homology modeling.  Comp. Rendu. Acad. Sci., Paris, 320:767-781 (1997).
    
    
76. Laible, P.D., Y. Zhang, A.L. Morris, S.W. Snyder, C. Ainsworth, S.R. Greenfield, M.R. Wasielewski, P. Parot, B. Schoepp, M. Schiffer, D.K. Hanson, and M.C. Thurnauer.  Spectroscopic characterization of quinone-site mutants of the bacterial photosynthetic reaction center.  Photosyn. Res., 52:93-103 (1997).
    
    
77. Miksovska, J., L. Kalman, M. Schiffer, P. Maroti, P. Sebban, and D.K. Hanson.  In bacterial reaction centers rapid delivery of the second proton to Q_B can be achieved in the absence of L212Glu.  Biochemistry 36:12216-12226 (1997).
    
    
78. Valerio-Lepiniec, M., J.-D. Delcroix, M. Schiffer, D.K. Hanson, and P. Sebban.  A native electrostatic environment near Q_B is not sufficient to ensure rapid proton delivery in photosynthetic reaction centers.  FEBS Lett. 407:159-163 (1997).
    
    
79. Huang, D-B., C.-H. Chang, C. Ainsworth, G. Johnson, M. Eulitz, A. Solomon, F.J. Stevens, and M. Schiffer.  Variable domain structure of the nonpathological human kIV light chain Len: High homology to the murine light chain McPC603. Molec. Immunol. 34:1291-1301(1997).
    
    
80. Laible, P.D., V. Chynwat, M.C. Thurnauer, M. Schiffer, D.K. Hanson, and H.A. Frank.  Protein modifications affecting triplet energy transfer in bacterial photosynthetic reaction centers.  Biophys. J., 74:2623-2637 (1998).
    
    
81. Raffen, R., P. Wilkins Stevens, C. Boogaard, M. Schiffer, and F.J. Stevens.  Altered immunoglobulin domain interactions through engineered salt bridges.  Protein Engineering 11:303-309 (1998).
    
    
82. Miksovska, J., M.Valerio-Lepiniec, M. Schiffer, D.K. Hanson, and P. Sebban.  In bacterial reaction centers, a key residue suppresses mutational blockage of two different proton transfer steps.  Biochemistry 37:2077-2083 (1998).
    
    
83. DiMagno, T.J., P.D. Laible, N.R. Reddy, G.J. Small, J.R. Norris, M. Schiffer, and D.K. Hanson.  Protein-chromophore interactions: Spectral shifts report the consequences of mutations in the bacterial photosynthetic reaction center.  Spectrochim. Acta A 54:1247-1267 (1998).
    
    
84. Hanson, D.K. and M. Schiffer.  Symmetry-related mutants in the quinone binding sites of the reaction center the effects of changes in charge distribution.  Photosyn. Res. 55:275-280 (1998).
    
    
85. Kálmán, L., P. Sebban, D.K. Hanson, M. Schiffer, and P. Maroti.  Flash-induced changes in buffering capacity of reaction centers from photosynthetic bacteria reveal complex interaction between quinone pockets.  Biochim. Biophys. Acta 1365:513-521 (1998).
    
    
86. Pokkuluri, P.R., D-B. Huang, R. Raffen, X. Cai, G. Johnson, P. Wilkins Stevens, F.J. Stevens, and M. SchifferA domain flip as a result of a single amino-acid substitution.  Structure 6:1067-1073 (1998).
    
    
87. Pokkuluri, P.R., D.-B. Huang, , R. Raffen, G. Johnson, P. Wilkins Stevens, F.J. Stevens, and M. Schiffer,.  A domain flip as a result of a single amino acid substitution. Structure 6:1067-1073 (1998).
    
    
88. Raffen, R., Diekman, L., Szpunar, M., Wunschl, C., Pokkuluri, P.R., Dave, P., Wilkins Stevens, P., Schiffer, M., and Stevens, F.J.  Physiochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains.  Protein Science 8, 509-517 (1999).
    
    
89. Kohler, H., S. Muller, M. Schiffer, and P.L. Nara.  Few clues for AIDS vaccines from structural data on gp120 and its receptors and antibodies.  J. Acquired Immune Deficiency Syndromes and Human Retrovirology 20:315-316 (1999).
    
    
90. Pokkuluri, P.R., A. Solomon, D.T. Weiss, F.J. Stevens, and M. Schiffer.  Tertiary structure of human λ 6 light chains.  Amyloid: Int. J. Exp. Clin. Invest. 6:165-171 (1999).
    
    
91. Valerio-Lepiniec, M., J. Miksovska, M. Schiffer, D.K. Hanson, and P. Sebban.  Mutations in the environment of the primary quinone facilitate proton delivery to the secondary quinone in bacterial photosynthetic reaction centers.  Biochemistry 38:390-398 (1999).
    
    
92. Miksovska, J., M. Schiffer, D.K. Hanson, and P. Sebban..  Proton uptake by bacterial reaction centers:  The protein complex responds in a similar manner to the reduction of either quinone acceptor.  Proc. Natl. Acad. Sci. USA, 96:14348-14353 (1999).
    
    
93. Alexov, E., J. Miksovska, L. Baciou, M. Schiffer, D.K. Hanson, P. Sebban, and M.R. Gunner.  Modeling the effects of mutations on the free energy of the first electron transfer from Q_A to Q_B in photosynthetic reaction centers.  Biochemistry 39:5940-5952 (2000).
    
    
94. Pokkuluri, P.R., X. Cai, F.J. Stevens, and M. Schiffer.  Change in Dimerization Mode by Removal of a Single Unsatisfied Polar Residue Located at the Interface. Prot. Sci. 9:1852-2855 (2000).
    
    
95. Stevens, F.J., P.R. Pokkuluri, and M. Schiffer.  Protein conformation and disease:  Pathological consequences of analogous mutations in homologous proteins.  Biochemistry 39:15291-15296 (2000).
    
    
96. Tandori, J., L. Baciou, E. Alexov, P. Maróti, M. Schiffer, D.K. Hanson, and P. Sebban.  Revealing the involvement of extended hydrogen bond networks in the cooperative function between distant sites in bacterial reaction centers.  J. Biol. Chem. 276:45513-45515 (2001).
    
    
97. Pokkuluri, P.R., R.Raffen, L. Dieckman, C. Boogaard, F.J. Stevens, and M. Schiffer.  Increasing protein stability by polar surface residues domain-wide consequences of interactions within a loop.  Biophysical J. 82:391-398 (2002).
    
    
98. Pokkuluri, P.R., M. Gu, X. Cai, R. Raffen, F.J. Stevens, and M. Schiffer. Factors contributing to decreased protein stability when aspartic acid residues are in β-sheet regions. Protein Science, 11: 1687-1694 (2002).
    
    
99. Pokkuluri, P.R., P.D. Laible, Y.-L. Deng, T.N. Wong, D.K. Hanson, and M. Schiffer. The structure of a mutant photosynthetic reaction center shows unexpected changes in main orientations and quinone position.  Biochemistry, 41, 5988-6007(2002).
    
    
100. Tandori, J., J. Miksovska, M. Valerio-Lepiniec, M. Schiffer, P. Maróti, D.K. Hanson, and P. Sebban. Proton uptake of Rhodobacter capsulatus reaction center mutants modified in the primary quinine environment. Photochemistry and Photobiology, 75; 126-133 (2002).
     
     
101. Morris Z.S., D.K. Hanson, P.R. Pokkuluri, D.G. Mets, A.N. Hata, O.G. Poluektov, M.C. Thurnauer, M. M. Schiffer, P.D. Laible. Lysine substitutions near photoactive cofactors in the bacterial photosynthetic reaction center have opposite effects on the rate of triplet energy transfer, Chemical Physics, 294; 329-346 (2003).
     
     
102. Laible P. D. , Z.S. Morris, M.C.Thurnauer, M. Schiffer, D.K. Hanson. Inter- and intraspecific variation in exited-state triplet energy transfer rates in reaction centers of photosynthetic bacteria, Photochemistry and Photobiology, 78; 114-123 (2003).
     
     
103. Pokkuluri, P.R., Y.Y. Londer, N. Duke, W.C. Long, and M. Schiffer. Family of cytochrome c₇ -type proteins from Geobacter sulfurreducens: The structure of one cytochrome c₇ at 1.45 Å resolution. Biochemistry, 43, 849-859 (2004).
     
     
104. Moy S., L. Dieckman, M. Schiffer, N. Maltsev, G.X. Yu, and A.F. Collart. Genome-scale expression of proteins from Bacillus subtilis. J Struct Funct Genomics. 5:103-9 (2004).
     
     
105. Pokkuluri, P.R., P.D. Laible, A.E. Crawford, J.F. Mayfield, M.A. Yousef, S.L. Ginell, D.K. Hanson, and M. Schiffer. Temperature and cryoprotectant influence secondary quinone binding position in bacterial reaction centers. FEBS Lett. 570:171-4 (2004).
     
     
106. Pokkuluri, P.R., Y.Y. Londer, N. Duke, J. Erickson, M. Pessanha, C.A. Salgueiro, and M. Schiffer. Structure of a novel c₇ -type three-heme cytochrome domain from a multidomain cytochrome c polymer. Protein Science, 13:1684-92 (2004).
     
     
107. Londer, Y.Y., P.R. Pokkuluri, M. Schiffer. Functional expression of multiheme cytochromes c in E. coli, PharmaGenomics 4; 24 – 30 (2004).
     
     
108. Pessanha, M.,  Y.Y. Londer, W.C. Long, J. Erickson, P.R. Pokkuluri, M. Schiffer, C.A.Salgueiro. Redox characterization of Geobacter sulfurreducens cytochrome c₇: Physiological relevance of the conserved residue F15 probed by site-specific mutagenesis. Biochemistry, 43; 9909 – 9917 (2004).
     
     
109. Londer, Y.Y.,  P.R. Pokkuluri, M. Schiffer. Functional expression of multiheme cytochromes c in E. coli. PharmaGenomics 4:24 – 30 (2004).
     
     
110. Londer, Y.Y., P. R. Pokkuluri, J. Erickson, V. Orshonsky, and M. Schiffer. Heterologous expression of hexaheme fragments of a multidomain cytochrome from Geobacter sulfurreducens representing a novel class of cytochromes c. Protein Expr. Purif. 39:254-260 (2005).
     
     
111. Afkar E., G.Reguera G, M.Schiffer, D. R. Lovley. A novel Geobacteraceae-specific outer membrane protein J (OmpJ) is essential for electron transport to Fe(III) and Mn(IV) oxides in Geobacter sulfurreducens. .BMC Microbiol. 5:41-51 (2005).
     
     
112. Londer, Y. Y.,  P.R. Pokkuluri,  V.Orshonsky, V., L.Orshonsky, M.Schiffer. Heterologous expression of dodecaheme "nanowire" cytochromes c from Geobacter sulfurreducens. Protein Express. Purifi, 47: 241-248 (2006).
     
     
113. Londer, Y.Y., I. S. Dementieva, C. A. D’Ausilio, P. R. Pokkuluri, M. Schiffer. Characterization of a c-type heme containing PAS sensor domain from Geobacter sulfurreducens representing a novel family of periplasmic sensors in Geobacteraceae and other bacteria. FEMS Microbiol. Lett, 258:173-181 (2006).

114. Chen Y, S. Borowicz , J. Fackenthal, F. R. Collart, E. Myatt, S. Moy, G. Babnigg, R. Wilton, W. E. Boernke , M. Schiffer, F. J.Stevens, O. I. Olopade. Primary structure-based function characterization of BRCT domain replicates in BRCA1.Biochem Biophys Res Commun. 345:188-96 (2006).

Meeting Proceedings and Books

• Hardman, K.D., M.K. Wood, M. Schiffer, A.B. Edmundson, and C.F. Ainsworth.  X-ray crystallographic studies of Concanavalin A.  Cold Spring Harbor Symposium on Quantum Biology, Vol. 36, pp. 271-276 (1971).

• Edmundson, A.B., M. Schiffer, K.R. Ely, and M.K. Wood.  Structural features of immunoglobulin light chains.  Progress in Molecular and Subcellular Biology, Vol. 3, F.E. Hahn, ed., Springer-Verlag, Berlin, pp. 159-182 (1973).

• Edmundson, A.B., E.E. Abola, K.R. Ely, J.R. Firca, N. Panagiotopoulos, M. Schiffer, and F.A. Westholm.  Implications of conformational isomerism and rotational allomerism to the binding of small molecules by the Mcg Bence-Jones dimer.  Antibodies in Human Diagnosis and Therapy, pp. 135-152 (1977).

• Budil, D.E., P. Gast, C.-H. Chang, M. Schiffer, and J.R. Norris.  Three-dimensional x-ray crystallography of membrane proteins: Insights into electron transfer.  Ann. Rev. Phys. Chem. 38:561-583 (1987).

• Stevens, F.J. and M. Schiffer.  Immunoglobulin structural diversities and idiotypic expression.  Int. Rev. Immunol. 2:357-378 (1987).

• Chang, C.-H., D. Tiede, J. Tang, J.R. Norris, and M. Schiffer.  Crystallographic studies of the photosynthetic reaction center from Rhodobacter sphaeroides.  Progress in Photosynthesis Research, J. Biggins, ed., Martinus Nijhoff Publishers, Dordrectht, The Netherlands, pp. 1.4.371-1.4.374 (1987).

• Tiede, D.M., D.E. Budil, J. Tang, O. El-Kabbani, J.R. Norris, C.-H. Chang, and M. Schiffer.  Symmetry breaking structures involved in the docking of cytochrome C and primary electron transfer in reaction centers of Rhodobacter sphaeroides.  The Photosynthetic Bacterial Reaction Center, J. Breton and A. Vesmiglio, eds., Plenum Publishing Corporation, New York, NY, pp. 13-20 (1988).

• Reiss-Husson, F., B. Arnoux, A. Ducruix, K. Steck, W. Mantele, M. Schiffer, and C.-H. Chang.  Spectroscopic and structural studies of crystallized reaction centers from wild-type Rhodobacter sphaeroides Y.  In: Molecular Biology of Membrane-Bound Complexes in Aphototropic Bacteria, pp. 323-328 (1990).

• Norris, J.R., T.J. DiMagno, A. Angerhofer, C.-H. Chang, O. El-Kabbani, and M. Schiffer.  A structural basis for electron transter in bacterial photosynthesis perspectives in photosynthesis.  Proceedings of the 22nd Jerusalem Symposium on Quantum Chemistry and Biochemistry, Jerusalem, Israel, May 15-18, 1989, pp. 11-21 (1990).

• DiMagno, T.J., S.J. Rosenthal, X. Xie, M. Du, C.-K. Chan, D.K. Hanson, M. Schiffer, J.R. Norris, and G.R. Fleming.  Recent experimental results for the initial step bacterial photosynthesis.  In: The Photosynthetic Bacterial Reaction Center: Structure, Spectroscopy, and Dynamics, J. Breton and A. Vermeglio, eds., NATO ASI Series, Plenum Press, London, pp. 209-217 (1992).

• Schiffer, M., C.-K. Chan, C.-H. Chang, T.J. DiMagno, G.R. Fleming, S. Nance, J. Norris, S. Snyder, M. Thurnauer, D.M. Tiede, and D.K. Hanson.  Study of reaction center function by analysis of the effects of site-specific and compensatory mutations.  In: The Photosynthetic Bacterial Reaction Center: Structure, Spectroscopy, and Dynamics, J. Breton and A. Vermeglio, eds., NATO ASI Series, Plenum Press, London, pp. 351-361 (1992).

• Schiffer, M., and J. R. Norris.  Structure and function of the photosynthetic reaction center of Rhodobacter sphaeroides.  In The Photosynthetic Reaction Center, Vol. 1, J. Deisenhofer and J. R. Norris, eds., 1993, Academic Press, Inc., pp. 1-12.

• Wang, Z., T.J. DiMagno, C.-K. Chan, M. Popov, J. Tang, D.K. Hanson, M. Schiffer, G. Fleming, and J.R. Norris.  Model photo reaction centers via genetic engineering.  In: Proceedings of the 9th International Conference on Photochemical and Photoelectrochemical Conversion and Storage of Solar Energy, International Academic Publishers, pp. 1-10 (1993).

• Stevens, F.J. and M. Schiffer.   Structure and properties of human immunoglobulin light chain dimers, in Methods in Molecular Biology, Vol. 51: Antibody Engineering Protocols, ed. S. Paul, pp. 51-81. Humana Press Inc., Totowa, NJ, (1995).

• Schiffer, M. and F.J. Stevens.  Crystallographic and chromatographic methods for study of antibody light chains and other proteins, in Methods in Molecular Biology, Vol. 51: Antibody Engineering Protocols, ed. S. Paul, pp. 83-98. Humana Press Inc., Totowa, NJ, (1995).

• Schiffer, M, Y.-L. Deng, A. Marrufo, and D.K. Hanson.  Effects of cavities in the bacterial reaction center.  In: Xth International Congress on Photosynthesis: From Light to Biosphere, Vol. 1, P. Mathis (ed.), Kluwer Academic Publishers,  Montpellier, France, pp. 855-858 (1995).

• Delcroix, J.D., P. Sebban, M. Schiffer, P. Maróti, and D.K. Hanson.  Long range electrostatic effects in bacterial reaction centers. In:   Xth International Congress on Photosynthesis: From Light to Biosphere, Vol. 1, P. Mathis (ed.), Kluwer Academic Publishers,  Montpellier, France, pp. 463-465 (1995).

• Hanson, D.K., Y.-L. Deng, P. Sebban, and M. Schiffer.  Compensation for L212GLU in bacterial reaction centers.  In:  Xth International Congress on Photosynthesis: From Light to Biosphere, Vol. 1, P. Mathis (ed.), Kluwer Academic Publishers, Montpellier, France, pp. 859-863 (1995).

• Miksovska, J., P. Sebban, M. Schiffer, D.K. Hanson, and P. Maróti.  In bacterial reaction centers L212Glu interacts with Q_Aat 17 Å distance.  In:  Xth International Congress on Photosynthesis: From Light to Biosphere, Vol. 1, P. Mathis (ed.), Kluwer Academic Publishers, Montpellier, France, pp. 467-470, August 20-25, 1995.

• Schiffer, M.  Structure determination of proteins by x-ray diffraction.  In: Biophysical Techniques in Photosynthesis, J. Amesz and A.J. Hoff (eds.), Kluwer Academic Publishers, pp. 317-324 (1996).

• Laible, P.D., C. Kirmaier, D. Holten, D.M. Tiede, M. Schiffer, and D.K. Hanson.  Formation of P+Q_B via B-branch electron transfer in mutant reaction centers.  In: Photosynthesis: Mechanisms and Effects (G. Garab, ed.), Kluwer, Dordrecht, pp. 849-852 (1998).

• Laible, P.D., D.K. Hanson, M.C. Thurnauer, and M. Schiffer.  The proteins role in triplet energy transfer in bacterial reaction centers.  In: Photosynthesis: Mechanisms and Effects (G. Garab, ed.), Kluwer, Dordrecht, pp. 779-782 (1998).
  
  
• Pokkuluri, P.R., D.K. Hanson, P.D. Laible, S. Ginell, G. Johnson and M. Schiffer. Structural Description of Reaction Center Mutants that Restore Proton Transfer to the L212Ala-L213Ala Double Mutant.
  
  
• Photosynthesis: Fundamental Aspects to Global Perspectives, Eds. A. van der Est and D. Bruce, Alliance Communications Group, Lawrence, Kansas, pp 272-274 (2005).