SEARCH

SEARCH BY CITATION

References

  • Alexander, D.C. and Speranza, G.P. 1989. Novel bismaleimide derivatives. Eur. Pat. Appl. 16 pp.
  • Amiranoff, B. and Lorinet-Laburthe, M. 1991. A clonal rat pancreatic Δ cell line (Rin14B) expresses a high number of galanin receptors negatively coupled to a pertussis-toxin-sensitive cAMP-production pathway. Eur. J. Biochem. 195: 459463.
  • Archambault, J. 2000. The oligomerization domain of the E1 helicase of papillomavirus and its role in viral replication and therapeutic use. PCT Int. Appl. 101 pp.
  • Bar-Peled, M. and Raikhel, N.V. 1996. A method for isolation and purification of specific antibodies to a protein fused to the GST. Anal. Biochem. 241: 140142.
  • Bauer, P.J. and Hagen, V. 1997. Dimaleimido-substituted dihydroxy alkanes which can be used as crosslinking reagents and process for their preparation. PCT Int. Appl. 12 pp.
  • Bhattacharjee, H. and Rosen, B.P. 1996. Spatial proximity of Cys113, Cys172, and Cys422 in the metalloactivation domain of the ArsA ATPase. J. Biol. Chem. 271: 2446524470.
  • Bladon, C.M., Mitchell, R., and Ogier, S.A. 1989. Preparation and use of biotinylated ligands for LHRH receptor purification. Tetrahedron Lett. 30: 14011404.
  • Bragg, P.D. and Hou, C. 1986. Chemical crosslinking of α subunits in the F1 adenosine triphosphatase of Escherichia coli. Arch. Biochem. Biophys. 244: 361372.
  • Bubis, J., Ortiz, J.O., Moeller, C., and Millan, E.J. 1995. Identification and characterization of transducin functional cysteines, lysines, and acidic residues by group-specific labeling and chemical crosslinking. Methods Protein Struct. Anal. 227250.
  • Caplow, M. and Shanks, J. 1990. Mechanism of the microtubule GTPase reaction. J. Biol. Chem. 265: 89358941.
  • Carl, S.A.L., Smith, T.M., and Kirley, T.L. 1998. Crosslinking induces homodimer formation and inhibits enzymic activity of chicken stomach ecto-apyrase. Biochem. Mol. Biol. Int. 44: 463470.
  • Chain, R.K. and Malkin, R. 1991. The chloroplast cytochrome b6f complex can exist in monomeric and dimeric states. Photosynth. Res. 28: 5968.
  • Chang, F.N. and Flaks, J.G. 1972. Specific crosslinking of two proteins from the Escherichia coli 30S ribosomal subunit. J. Mol. Biol. 68: 177180.
  • Chaussepied, P., Morales, M.F., and Kassab, R. 1988. The myosin (SH2-50-kilodalton fragment) cross-link: Location and consequences. Biochemistry 27: 17781785.
  • Chen, Y., Couvineau, A., Laburthe, M., and Amiranoff, B. 1992. Solubilization and molecular characterization of active galanin receptors from rat brain. Biochemistry 31: 24152422.
  • Cheronis, J.C., Whalley, E.T., Nguyen, K.T., Eubanks, S.R., Allen, L.G., Duggan, M.J., Loy, S.D., Bonham, K.A., and Blodgett, J.K. 1992. A new class of bradykinin antagonists: Synthesis and in vitro activity of bissuccinimidoalkane peptide dimers. J. Med. Chem. 35: 15631572.
  • Coggins, J.R. 1996. Crosslinking reagents for proteins. Proteins Labfax 307314.
  • Cohlberg, J.A., Pigiet, Jr. V.P, and Schachman, H.K. 1972. Structure and arrangement of the regulatory subunits in aspartate transcarbamylase. Biochemistry 11: 33963411.
  • Cornell, R. 1989. Chemical cross-linking reveals a dimeric structure for CTP : phosphocholine cytidylyltransferase. J. Biol. Chem. 264: 90779082.
  • Davies, G.E. and Kaplan, J.G. 1972. Use of a diimidoester crosslinking reagent to examine the subunit structure of rabbit muscle pyruvate kinase. Can. J. Biochem. 50: 416422.
  • Dubey, A.K., Bisaria, V.S., Mukhopadhyay, S.N., and Ghose, T.K. 1989. Stabilization of restriction endonuclease Bam Hi by cross-linking reagents. Biotechnol. Bioeng. 33: 13111316.
  • Eisman, J.M. and Schnaare, R.L. 1996. The formation of a crosslinked carboxyhemoglobin membrane at an organic-aqueous interface. Artif. Cells Blood Substit. Immobil. Biotechnol. 24: 185196.
  • Eliel, E.L. 1965. Conformational analysis. Interscience Publishers, New York.
  • Erarslan, A. and Ertan, H. 1995. Thermostabilization of penicillin G acylase obtained from a mutant of Escherichia coli ATCC 11105 by bisimidoesters as homobifunctional crosslinking agents. Enzyme Microb. Technol. 17: 629635.
  • Farries, T.C., Lachmann, P.J., and Harrison, R.A. 1988. Analysis of the interaction between properdin and factor B, components of the alternative-pathway C3 convertase of complement. Biochem. J. 253: 667675.
  • Fasold, H., Klappenberger, J., Meyer, C., and Remold, H. 1971. Bifunctional reagents for the cross-linking of proteins. Angew. Chem. Int. Ed. Engl. 10: 795801.
  • Franke, I. and Pingoud, A. 1999. Synthesis and biochemical characterization of obligatory dimers of the sugar non-specific nuclease from Serratia marcescens using specifically designed bismaleimidoalkanes as SH-specific crosslinking reagents. J. Protein Chem. 18: 137146.
  • Franke, I., Pingoud, A., Wende, W., and Meiss, G. 1999. Immobilized nuclease variants from Serratia marcescens which do not dissociate into subunits. PCT Int. Appl. 21 pp.
  • Fujioka, T., Inoue, F., Kuriyama, M., Miura, Y., and Higashijima, T. 1990. Identification of opioid-binding materials of rat brain. Chem. Pharm. Bull. 38: 168171.
  • Garlick, R.L., Martin, J.P., Jr., and Lyle, S.B. 1992. Imidoester cross-linked hemoglobin compositions. PCT Int. Appl. 22 pp.
  • Geisler, N., Schuenemann, J., and Weber, K. 1992. Chemical cross-linking indicates a staggered and antiparallel protofilament of desmin intermediate filaments and characterizes one higher-level complex between protofilaments. Eur. J. Biochem. 206: 841852.
  • Givol, D. 1969. Inactivation of glyceraldehyde-3-phosphate dehydrogenase by a bifunctional reagent. FEBS Lett. 5: 153156.
  • Goldberg, M., Knudsen, K.L., Platt, D., Kohen, F., Bayer, E.A., and Wilchek, M. 1991. Specific interchain crosslinking of antibodies using bismaleimides. Repression of ligand leakage in immunoaffinity chromatography. Bioconjug. Chem. 2: 275280.
  • Gotte, G., Testolin, L., Costanzo, C., Sorrentino, S., Armato, U., and Libonati, M. 1997. Cross-linked trimers of bovine ribonuclease A: Activity on double-stranded RNA and antitumor action. FEBS Lett. 415: 308312.
  • Greve, J.M. and McClelland, A. 1994. Multimeric forms of human rhinovirus receptor protein ICAM and their use in the treatment of infection. PCT Int. Appl. 69 pp.
  • Hansen, M.S.T. and Barklis, E. 1995. Structural interactions between retroviral Gag proteins examined by cysteine crosslinking. J. Virol. 69: 11501159.
  • Hartman, F.C. and Wold, F. 1967. Cross-linking of bovine pancreatic ribonuclease A with dimethyl adipimidate. Biochemistry 6: 24392448.
  • Herzig, M.C.S. and Leeb-Lundberg, L.M.F. 1995. The agonist binding site on the bovine bradykinin B2 receptor is adjacent to a sulfhydryl and is differentiated from the antagonist binding site by chemical crosslinking. J. Biol. Chem. 270: 2059120598.
  • Herzig, M.C.S., Nash, N.R., Connolly, M., Kyle, D.J., and Leeb-Lundberg, L.M.F. 1996. The N terminus of bradykinin when bound to the human bradykinin B2 receptor is adjacent to extracellular Cys20 and Cys277 in the receptor. J. Biol. Chem. 271: 2974629751.
  • Hesterkamp, T., Weeds, A.G., and Mannherz, H.G. 1993. The actin momomers in the ternary gelsolin: 2 actin complex are in an antiparallel orientation. Eur. J. Biochem. 218: 507513.
  • Hitchcock, S.E. 1975. Crosslinking of troponin with dimethylimido esters. Biochemistry 14: 51625167.
  • Holmes, K.C., Popp, D., Gebhard, D., and Kabsch, W. 1990. Atomic model of the actin filament. Nature 347: 4449.
  • Holwerda, B. 1999. Activity in monomers of human cytomegalovirus protease. Biochem. Biophys. Res. Commun. 259: 370373.
  • Horiguchi, T., Miwa, Y., and Shigesada, K. 1997. The quaternary geometry of transcription termination factor ρ: Assignment by chemical crosslinking. J. Mol. Biol. 269: 514528.
  • Hovinen, J., Guzaev, A., Azhayev, A., and Lonnberg, H. 1993. Synthesis of 3′-functionalized oligonucleotides on a single solid support. Tetrahedron Lett. 34: 81698172.
  • Hsia, J.C., Wong, L.T., Tan, C.T., Er, S.S., Kharouba, S., Balaskas, E., Tinker, D.O., and Feldhoff, R.C. 1984. Bovine serum albumin: Characterization of a fatty acid binding site on the N-terminal peptic fragment using a new spin-label. Biochemistry 23: 59305932.
  • Huey, R. and Hugli, T.E. 1985. Characterization of a C5a receptor on human polymorphonuclear leukocytes (PMN). J. Immunol. 135: 20632068.
  • Ishiguro, M., Matori, Y., Tanabe, S., Kawase, Y., Sekine, I., and Sakakibara, R. 1992. Biochemical studies on oral toxicity of ricin. V. The role of lectin activity in the intestinal absorption of ricin. Chem. Pharm. Bull. 40: 12161220.
  • Jansson, S., Andersen, B., and Scheller, H.V. 1996. Nearest-neighbor analysis of higher-plant photosystem I holocomplex. Plant Physiol. 112: 409420.
  • Kato, Y., Umemoto, N., Saito, M., and Hara, T. 1986. Preparation of cytotoxic complexes containing pharmaceuticals, albumins, and antibodies to target tissues. Jpn. Kokai Tokkyo Koho 18 pp.
  • Kiehm, D. and Ji, T.H. 1977. Photochemical crosslinking of cell membranes. A test for natural and random collisional crosslinks by millisecond crosslinking. J. Biol. Chem. 252: 85248531.
  • Kim, J.S. and Raines, R.T. 1995. Dibromobimane as a fluorescent crosslinking reagent. Anal. Biochem. 225: 174176.
  • King, D.J, Mountain, A., Owens, R.J., and Yarranton, G.T. 1991. Multivalent antigen-binding proteins and their production by recombinant DNA technology. PCT Int. Appl. 55 pp.
  • Kliche, W., Pfannstiel, J., Tiepold, M., Stoeva, S., and Faulstich, H. 1999. Thiol-specific cross-linkers of variable length reveal a similar separation of SH1 and SH2 in myosin subfragment 1 in the presence and absence of MgADP. Biochemisty 38: 1030710317.
  • Koga, R. 1987. Affinity of chemically cross-linked immunoglobulin to antigen. Seirigaku Kenkyusho Gijutsuka Hokoku 2: 57.
  • Konno, K., Ue, K., Khoroshev, M., Martinez, H., Ray, B., and Morales, M.F. 2000. Consequences of placing an intramolecular crosslink in myosin S1. Proc. Natl. Acad. Sci. 97: 14611466.
  • Korsgren, P., Ahlberg, P., and Baltzer, L. 2000. Covalent control of polypeptide folding. Induction of helix-loop-helix motifs by bridging. Perkin 2: 643647.
  • Kossmehl, G., Nagel, H.I., and Pahl, A. 1995. Crosslinking reactions on polyamides by bis- and tris(maleimide)s. Angew. Makromol. Chem. 227: 139157.
  • Krupenko, S.A., Kolesnik, O.I., Krupenk, N.I., and Strelchyonok, O.A. 1995. Organization of the transcortin-binding domain on placental plasma membranes. Biochim. Biophys. Acta 1235: 387394.
  • Kumar, P., Bose, N.K., and Gupta, K.C. 1991. A versatile solid phase method for the synthesis of oligonucleotide-3′-phosphates. Tetrahedron Lett. 32: 967970.
  • Kunkle, G.R., Mehrebian, M., and Matinson, G.H. 1986. Contact-site cross-linking reagents. Mol. Cell. Biochem. 234: 826836.
  • Kwaw, I., Sun, J., and Kaback, H.R. 2000. Thiol cross-linking of cytoplasmic loops in the lactose permease of Escherichia coli. Biochemistry 39: 31343140.
  • Lai, C.S. 1997. Antibodies directed against dithiocarbamates. PCT Int. Appl. 31 pp.
  • Leach, A. 1996. Molecular modelling: Principles and applications. Addison Wesley Longman Limited, Essex, UK.
  • Leonard, A.S., Davare, M.A., Horne, M.C., Garner, C.C., and Hell, J.W. 1998. SAP97 is associated with the α-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor GluR1 subunit. J. Biol. Chem. 273: 1951819524.
  • Lloyd, A.J. and Weitzman, P.D.J. 1987. Modification of the regulatory properties of Acinetobacter citrate synthase by cross-linking. Biochem. Soc. Trans. 15: 840.
  • Loester, K., Baum, O., Hofmann, W., and Reutter, W. 1995. Characterization of molecular aggregates of α1β1-integrin and other rat liver membrane proteins by combination of size-exclusion chromatography and chemical crosslinking. J. Chromatogr. A 711: 187199.
  • Loo, T.W. and Clarke, D.M. 1999. Identification of residues in the drug-binding domain of human P-glycoprotein. Analysis of transmembrane segment 11 by cysteine-scanning mutagenesis and inhibition by dibromobimane. J. Biol. Chem. 274: 3538835392.
  • Loo, T.W. and Clarke, D.M. 1997. Identification of residues in the drug-binding site of human P-glycoprotein using a thiol-reactive substrate. J. Biol. Chem. 272: 3194531948.
  • Lorenz, M., Popp, D., and Holmes, K.C. 1993. Refinement of the F-actin model against x-ray fiber diffraction data by the use of a directed mutation algorithm. J. Mol. Biol. 234: 826836.
  • Maman, J.D., Yager, T.D., and Allan, J. 1994. Self-association of the globular domain of histone H5. Biochemistry 33: 13001310.
  • Margolin, A.L., Persichetti, R.A., St. Clair, N.L., Khalaf, N.K., and Shenoy, B.C. 1998. Controlled dissolution crosslinked protein crystals. PCT Int. Appl. 153 pp.
  • Masuho, Y., Umemoto, N., Hara, T., and Ohtomo, N. 1981. Cytotoxicity of a hybrid prepared by coupling diphtheria toxin A-chain with immunoglobulin Fab′ with N,N′-o-phenylenedimaleimide. Biochem. Biophys. Res. Commun. 102: 561567.
  • Masuho, Y., Kishida, K., Saito, M., Umemoto, N., and Hara, T. 1982. Importance of the antigen-binding valency and the nature of the crosslinking bond in ricin A-chain conjugates with antibody. J. Biochem. (Tokyo) 91: 15831591.
  • Mayeux, P., Lacombe, C., Casadevall, N., Chretien, S., Dusanter, I., and Gisselbrecht, S. 1991. Structure of the murine erythropoietin receptor complex. Characterization of the erythropoietin cross-linked proteins. J. Biol. Chem. 266: 2338023385.
  • McDermott, J., Farrell, L., Ross, R., and Barklis, E. 1996. Structural analysis of human immunodeficiency virus type 1 Gag protein interactions, using cysteine-specific reagents. J. Virol. 70: 51065114.
  • Meunier, A.C., Voisin, C.P., Van Camp, G., Cenatiempo, Y., and Muller, J.M. 1991. Molecular characterization and peptide specificity of two vasoactive intestinal peptide (VIP) binding sites in the chicken pineal. Neuropeptides 19: 18.
  • Middleton, S.A., Johnson, D., McMahon, F.J., Mulkahy, L.S., and Jolliffe, L.K. 1997. Purification of human erythropoietin-binding protein from microbial fermentations and its uses in drug discovery. PCT Int. Appl. 64 pp.
  • Miller, L., Coppedge, J., and Reisler, E. 1982. The reactive SH1 and SH2 cysteines in myosin subfragment 1 are crosslinked at similar rates with reagents of different length. Biochem. Biophys. Res. Commun. 106: 117122.
  • Mita, S., Tominaga, A., Hitoshi, Y., Sakamoto, K., Honjo, T., Akagi, M., Kikuchi, Y., Yamaguchi, N., and Takatsu, K. 1989. Characterization of high-affinity receptors for interleukin 5 on interleukin 5-dependent cell lines. Proc. Natl. Acad. Sci. 86: 23112315.
  • Miyazaki, H., Kondoh, M., Watanabe, H., Masuda, Y., Murakami, K., Takahashi, M., Yanagisawa, M., Kimura, S., Goto, K., and Masaki, T. 1990. Affinity labeling of endothelin receptor and characterization of solubilized endothelin-endothelin-receptor complex. Eur. J. Biochem. 187: 125129.
  • Modesto, R.R. and Pesce, A.J. 1971. Reaction of 4,4′-difluoro-3,3′-dinitrodiphenyl sulfone with γ-globulin and horseradish peroxidase. Biochim. Biophys. Acta 229: 384395.
  • Mohamadi, F., Richards, N.G., Guida, W.C., Liskamp, R., Lipton, M., Canfield, C., Chang, G., Hendrickson, T., and Still, W.C. 1990. MacroModel—An integrated software system for modeling organic and bioorganic molecules using molecular mechanics. J. Comput. Chem. 11: 440467.
  • Moroney, J.V., Warncke, K., and McCarty, R.E. 1982. The distance between thiol groups in the g subunit of coupling factor 1 influences the proton permeability of thylakoid membranes. J. Bioenerg. Biomembr. 14: 347359.
  • Nadeau, O.W., Sacks, D.B., and Carlson, G.M. 1997. Differential affinity crosslinking of phosphorylase kinase conformers by the geometric isomers of phenylenedimaleimide. J. Biol. Chem. 272: 2619626201.
  • Nagy, J.K., Lau, F.W., Bowie, J.U., and Saunders, C.R. 2000. Mapping the oligomeric interface of diacylglycerol kinase by engineered thiol cross-linking: Homologous sites in the transmembrane domain. Biochemistry 39: 41544164.
  • Niehaus, W.G., Jr. and Wold, F. 1970. Cross-linking of erythrocyte membranes with dimethyl adipimidate. Biochim. Biophys. Acta 196: 170175.
  • Nitao, L.K. and Reisler, E. 1998. Probing the conformational states of the SH1-SH2 helix in myosin: A crosslinking approach. Biochemistry 37: 1670416710.
  • Oda, T. and Funatsu, G. 1979. Biochemical studies on ricin. Part XXIV. Cross-linking of the two constituent polypeptide chains of ricin D with N,N′-o-phenylenedimaleimide. Agric. Biol. Chem. 43: 547554.
  • Ohara, O., Takahashi, S., Ooi, T., and Fujiyoshi, Y. 1982. Cross-linking study on skeletal muscle actin: Properties of suberimidate-treated actin. J. Biochem. (Tokyo) 91: 19992012.
  • Pan, W., Ko, Y.H., and Pedersen, P.L. 1998 Subunit of rat liver mitochondrial ATP synthase: Molecular description and novel insights into the nature of its association with the F1-moiety. Biochemistry 37: 69116923.
  • Pennathur-Das, R., Heath, R.H., Mentzer, W.C., and Lubin, B.H. 1982. Modification of hemoglobin S with dimethyl adipimidate. Contribution of individual reacted subunits to changes in properties. Biochim. Biophys. Acta 704: 389397.
  • Perkins, W.J., Wells, J.A., and Yount, R.G. 1984. Characterization of the properties of ethenoadenosine nucleotides bound or trapped at the active site of myosin subfragment 1. Biochemistry 23: 39944002.
  • Persson, E. and Ezban, M. 1994. Characterization of chemically crosslinked human factor VIIIa. Biochem. Biophys. Res. Commun. 200: 233238.
  • Peters, K. and Richards, F.M. 1977. Chemical cross-linking: Reagents and problems in studies of membrane structure. Annu. Rev. Biochem. 46: 523551.
  • Pierce Chemicals. 1999. Double agents cross-linking reagents selection guide. Pierce Chemicals, Rockford, IL.
  • Pliszka, B. 1990. Influence of nucleotide on chemical crosslinking between alkali light chains and the heavy chain of myosin subfragment 1. Biochim. Biophys. Acta 1040: 8994.
  • Pliszka, B. 1993. Mapping of the region of the heavy chain of myosin subfragment 1 that can be crosslinked to the alkali light chains. Biochem. Mol. Biol. Int. 31: 381388.
  • Plouet, J. and Moukadiri, H. 1990. Characterization of the receptor to vasculotropin on bovine adrenal cortex-derived capillary endothelial cells. J. Biol. Chem. 265: 2207122074.
  • Polosukhina, K. and Highsmith, S. 1997. Kinetic investigation of the ligand dependence of rabbit skeletal muscle myosin subfragment 1 Cys-697 and Cys-707 reactivities. Biochemistry 36: 1195211958.
  • Poruchynsky, M.S. and Atkinson, P.H. 1991. Rotavirus protein rearrangements in purified membrane-enveloped intermediate particles. J. Virol. 65: 47204727.
  • Rappsilber, J., Siniossoglou, S., Hurt, E.C., and Mann, M. 2000. A generic strategy to analyze the spatial organization of multi-protein complexes by cross-linking and mass spectrometry. Anal. Chem. 72: 267275.
  • Russell-Jones, G.J., Westwood, S.W., Gould, A.R., and McInerney, B.V. 1994. Amplification of the vitamin B12 uptake system using polymers. PCT Int. Appl. 36 pp.
  • Schoffelmeer, A.N.M., Yao, Y.H., and Simon, E.J. 1989. Cross-linking of human 125I-β-endorphin to a μ-Δ opioid receptor complex in rat striatum. Eur. J. Pharmacol. 166: 357358.
  • Schwarzer, A., Kim, T.S.Y., Hagen, V., Molday, R.S., and Bauer, P.J. 1997. The Na/Ca-K exchanger of rod photoreceptor exists as dimer in the plasma membrane. Biochemistry 36: 1366713676.
  • Shivdasani, R.A. and Thomas, D.W. 1988. Molecular associations of IA antigens after T-B cell interactions. I. Identification of new molecular associations. J. Immunol. 141: 12521260.
  • Shoshan-Barmatz, V., Hadad-Halfon, N., and Ostersetzer, O. 1995. Crosslinking of the ryanodine receptor/Ca2+ release channel from skeletal muscle. Biochim. Biophys. Acta 1237: 151161.
  • Sinha, S.K. and Brew, K. 1981. A label selection procedure for determining the location of protein–protein interaction sites by cross-linking with bisimidoesters. Application to lactose synthase. J. Biol. Chem. 256: 41934204.
  • Smith, R.A., Kirstein, M., Fiers, W., and Baglioni, C. 1986. Species specificity of human and murine tumor necrosis factor. A comparative study of tumor necrosis factor receptors. J. Biol. Chem. 261: 1487114874.
  • Still, W.C., Tempczyk, A., Hawley, R.C., and Hendrickson, T. 1990. Semianalytical treatment of solvation for molecular mechanics and dynamics. J. Am. Chem. Soc. 121: 61276129.
  • Stout, J.G. and Kirley, T.L. 1996. Control of cell membrane ecto-ATPase by oligomerization state: intermolecular crosslinking modulates ATPase activity. Biochemistry 35: 82898298.
  • Stros, M. and Kolibalova, A. 1987. Interaction of non-histone proteins HMG1 and HMG2 with core histones in nucleosomes and core particles revealed by chemical cross-linking. Eur. J. Biochem. 162: 111118.
  • Stults, N.L. 1997. Preparation of photoprotein conjugates and methods of use thereof. U.S. 21 pp. Cont.-in-part of U.S. 5,486, 455.
  • Sun, J. and Kaback, H.R. 1997. Proximity of periplasmic loops in the lactose permease of Escherichia coli determined by site-directed crosslinking. Biochemistry 36: 1195911965.
  • Svoboda, M., De Neef, P., Tastenoy, M., and Christophe, J. 1988a. Molecular characteristics and evidence for internalization of vasoactive intestinal peptide (VIP) receptors in the tumoral rat-pancreatic acinar cell line AR 4-2 J. Eur. J. Biochem. 176: 707713.
  • Svoboda, M., Poloczek, P., Winand, J., Robberecht, P., and Christophe, J. 1988b. Species differences in the molecular characteristics of vasoactive intestinal peptide receptors in the pancreas from rat and guinea pig. Eur. J. Biochem. 174: 5966.
  • Swaney, J.B. 1986. Use of cross-linking reagents to study lipoprotein structure. Methods Enzymol. 128: 613626.
  • Tanaka, T., Inoue, M., Sakamoto, J., and Sone, N. 1996. Intra- and inter-complex crosslinking of subunits in the quinol oxidase super-complex from thermophilic Bacillus PS3. J. Biochem. 119: 482486.
  • Valenzuela, D., Leon, O., and Schulman, L.H. 1984. Modification of specific lysine residues in E. coli methionyl-tRNA synthetase by crosslinking to E. coli formylmethionine tRNA. Biochem. Biophys. Res. Commun. 119: 677684.
  • Vanhoutte, C. and Malaisse, W.J. 1997. d-Glucose metabolism in dimethyl suberimidate-treated tumoral pancreatic islet cells. Biochem. Mol. Biol. Int. 41: 12091216.
  • Walleczek, J., Martin, T., Redl, B., Stoeffler-Meilicke, M., and Stoeffler, G. 1989. Comparative cross-linking study on the 50S ribosomal subunit from Escherichia coli. Biochemistry 28: 40994105.
  • Wang, Q. and Kaback, H.R. 1999. Helix packing in the lactose permease of Escherichia coli determined by site-directed thiol crosslinking: Helix I is close to helices V and XI. Biochemistry 38: 31203126.
  • Wang, T.W. and Kassell, B. 1974. Preparation of a chemically cross-linked complex of the basic pancreatic trypsin inhibitor with trypsin. Biochemistry 13: 698702.
  • Wasylewska, E., Dulinska, J., Trubetskoi, V.S., Torchilin, V.P., and Ostrowski, W.S. 1987. Stabilization of human prostate acid phosphatase by cross-linking with diimidoesters. Acta Biochim. Pol. 34: 145156.
  • Watty, A., Methfessel, C., and Hucho, F. 1997. Fixation of allosteric states of the nicotinic acetylcholine receptor by chemical crosslinking. Proc. Natl. Acad. Sci. 94: 82028207.
  • Watty, A., Weise, C., Dreger, M., Franke, P., and Hucho, F. 1998. The accessible surface of the nicotinic acetylcholine receptor. Identification by chemical modification and crosslinking with 14C-dimethyl suberimidate. Eur. J. Biochem. 252: 222228.
  • Wells, J.A., Knoeber, C., Sheldon, M.C., Werber, M.M., and Yount, R.G. 1980. Cross-linking of myosin subfragment 1. Nucleotide-enhanced modification by a variety of bifunctional reagents. J. Biol. Chem. 255: 1113511140.
  • Wilbur, D.S. 1992. Radiohalogenation of proteins: An overview of radionuclides, labeling methods and reagents for conjugate labeling. Bioconjug. Chem. 3: 433470.
  • Wolff, J.A., Hagstrom, J.E., Budker, V.G., Trubetskoy, V.S., Slattum, P.M., and Hanson, L.J. 1998. Method for making a compound for delivery to cells by forming a polymer in the presence of a template drug, especially nucleic acid. PCT Int. Appl. 79 pp.
  • Wolff, J.A., Hagstrom, J.E., and Budker, V.G. 1999. Polymer formation in the presence of nucleic acid using template polymerization. PCT Int. Appl. 73 pp.
  • Wu, J., Voss, J., Hubbell, J.W., and Kaback, H.R. 1996. Site-directed spin labeling and chemical crosslinking demonstrate that helix V is close to helixes VII and VIII in the lactose permease of Escherichia coli. Proc. Natl. Acad. Sci. 93: 1012310127.
  • Xu, T., Vasilyeva, E., and Forgac, M. 1999. Subunit interactions in the clathrin-coated vesicle vacuolar (H+)-ATPase complex. J. Biol. Chem. 274: 2890928915.
  • Yu, R. and Carter, J. 1976. Cross-linking phytochrome to its receptor in situ using imidoesters. J. Exp. Bot. 27: 283293.
  • Yu, Y.Y., Wie, B.V.J., Koch, A.R., Moffett, D.F., and Davis, D.C. 1998. Preparation and characterization of bifunctional biopolymers for receptor-based liposomal immunosensing. Biotechnol. Prog. 14: 310317.
  • Zecherle, G.N., Oleinikov, A., and Traut, R.R. 1992. The proximity of the C-terminal domain of Escherichia coli ribosomal protein L7/L12 to L10 determined by cysteine site-directed mutagenesis and protein-protein cross-linking. J. Biol. Chem. 267: 58895896.