Graduate work on serum glycoproteins

Emura, J., Ikenaka, T., Collins, J.H. and Schmid, K.: The constant and variable regions of the carboxyl terminal CNBr fragment of alpha-1-acid glycoprotein. J Biol. Chem. 246: 7821-7823, 1971.

Schmid, K., Brgi, W., Collins, J.H. and Nanno, S.: The disulfide bridges of alpha-1-acid glycoprotein. Biochemistry 13: 2694-2697, l974.

Schmid, K., Hediger, M.A., Brossmer, R., Collins, J.H., Haupt, H., Marti, T., Offner, G.D., Schaller, J., Takagaki, K., Walsh, M.T., Schwick, G., Rosen, F.S., and Remold-O'Donnell, E.: Amino acid sequence of human plasma galactoglycoprotein: Identity with the extracellular region of CD43 (sialophorin). Proc. Natl. Acad. Sci. USA 89: 663-667, 1992.

Postdoctoral work on actin and myosin

Elzinga, M. and Collins, J.H.: The amino acid sequence of rabbit skeletal muscle actin. Cold Spring Harbor Symp. Quant. Biol. 37: l-7, 1972.

Elzinga, M., Collins, J.H., Kuehl, W.M. and Adelstein, R.S.: Complete amino acid sequence of actin of rabbit skeletal muscle. Proc. Natl. Acad. Sci. USA 70: 2687-2691, 1973.

Elzinga, M. and Collins, J.H.: The primary structure of actin from rabbit skeletal muscle: Five cyanogen bromide peptides including the amino and carboxyl termini. J. Biol. Chem. 250: 5897-5905, 1975.

Collins, J.H. and Elzinga, M.: The primary structure of actin from skeletal muscle: Three cyanogen bromide peptides that are insoluble at neutral pH. J. Biol. Chem 250: 5906-5914, 1975.

Collins, J.H. and Elzinga, M.: The primary structure of actin from rabbit skeletal muscle: Completion and analysis of the amino acid sequence. J. Biol. Chem. 250: 5915-5919, 1975.

Elzinga, M. and Collins, J.H.: The amino acid sequence of a myosin fragment that contains SH-1, SH-2 and N-methylhistidine. Proc. Natl. Acad. Sci. USA 74: 4281-4284, 1977.

Studies on actin protease

Khaitlina, S.Yu., Collins, J.H., Kuznetsova, I.M., Pershina, V.P., Synakevich, I.G., Turoverov, K.K., and Usmanova, A.M.: Physico-chemical properties of actin cleaved with bacterial protease from E. coli A2 strain. FEBS Lett. 279: 49-51, 1991.

Matveyev, V.V., Usmanova, A.M., Morozova, A.V., Collins, J.H. and Khaitlina, S.Yu.: Purification and characterization of the protease ECP 32 from Escherichia coli A2 strain. Biochim. Biophys. Acta 1296: 55-62, 1996.

Khaitlina, S, Antropova, O., Kuznetsova, I., Turoverov, K., and Collins, J.H.: Correlation Between Polymerizability and Conformation in Scallop $-like Actin and Rabbit Skeletal Muscle "-Actin. Arch. Biochem. Biophys. 368: 105-111, 1999.

Structural studies on myosin light chains

Collins, J.H., Theibert, J.L. and Dalla Libera, L.: Amino acid sequence of rabbit ventricular light chain-2: identity with the slow skeletal muscle isoform. Bioscience Reports 6: 655-662, 1986.

Dalla Libera, L., and Collins, J.H.: Analysis of myosin isoforms by gel electrophoresis and liquid chromatography. In: Proceedings Symposium Toward the Artificial Heart (Stagarno, E., ed.) pp. 215-219, 1986.

Collins, J.H., Jakes, R., Kendrick-Jones, J., Leszyk, J., Barouch, W., Theibert, J.L., Spiegel, J. and Szent-Gyrgyi, A.G.: The amino acid sequence of myosin essential light chain from the scallop Aquipecten irradians. Biochemistry 25: 7651-7656, 1986.

Barouch, W., Breese, K., Davidoff, S.-A., Leszyk, J., Szent-Gyrgyi, A.G., Theibert, J.L., and Collins, J.H.: Amino acid sequences of myosin essential and regulatory light chains from two clam species: comparison with other molluscan myosin light chains. J. Muscle Res. Cell Motil. 12: 321-332, 1991.

Dalla Libera, L., Carpene, E., Theibert, J.L., and Collins, J.H.: Fish myosin alkali light chains originate from two different genes. J. Muscle Res. Cell Motil. 12: 366-371, 1991.

Kobayashi, T., Zot, H., Pollard, T., and Collins, J.H.: Functional implications of the unusual amino acid sequence of the regulatory light chain of Acanthamoeba castellanii myosin-II. J. Muscle Res. Cell Motil. 12: 553-559, 1991.

Kwon, H., Hardwicke, P.M.D., Collins, J.H., Zhao, X., and Szent-Gyrgyi, A.G.: Myosins trapped by intramolecularly cross-linked actin. J. Muscle Res. Cell Motil. 15: 555-562, 1994.

First reports on homology of troponin C, myosin light chains and parvalbumins

Collins, J.H., Potter, J.D., Horn, M.J., Wilshire, G. and Jackman, N.: The amino acid sequence of rabbit skeletal muscle troponin C: Gene replication and homology with calcium binding proteins from carp and hake muscle. FEBS Lett. 36: 268-272, l973.

Collins, J.H., Potter, J.D., Horn, M.J., Wilshire, G. and Jackman, N.: Structural studies on rabbit skeletal muscle troponin C: Evidence for gene replication and homology with calcium binding proteins from carp and hake muscle, in: Calcium Binding Proteins (Drabikowski, W., Strzelecka-Golaszewska, H. and Carafoli, E., eds.), pgs. 51-64, Elsevier, Amsterdam, 1974.

Collins, J.H.: Homology of myosin light chains, troponin C and parvalbumins deduced from comparison of their amino acid sequences. Biochem. Biophys. Res. Commun. 58: 30l-308, 1974.

Collins, J.H.: Homology of myosin DTNB light chain with alkali light chains, troponin C and parvalbumin. Nature 259: 699-700, 1976.

Reviews on the structure, function and evolution of myosin light chains and troponin C

Collins, J.H.: Structure and evolution of troponin C and related proteins, In: Calcium in Biological Systems (Soc. Exptl. Biol. Symp. 30, Duncan, C.J., ed.) pgs. 303-334, Cambridge University Press, 1976.

Collins, J.H.: Myosin light chains and troponin C: structural and evolutionary relationships revealed by amino acid sequence comparisons. J. Muscle Res. Cell Motil. 12: 3-25, 1991.

Structural studies on troponin subunits

Collins, J.H.: Purification and analysis of the cyanogen bromide peptides of troponin T from rabbit skeletal muscle. Biochem. Biophys. Res. Commun. 65: 604-610, 1975.

Collins, J.H., Greaser, M.L., Potter, J.D. and Horn, M.J.: Determination of the amino acid sequence of troponin C from rabbit skeletal muscle. J. Biol. Chem. 252: 6357-6362, 1977.

Collins, J.H.: An improved method for isolation of Ca2+ binding cyanogen bromide peptides from rabbit skeletal muscle troponin C. Preparative Biochemistry 10: 77-84, 1980.

Leszyk, J., Dumaswala, R., Potter, J.D., Gusev, N.B., Verin, A.D., Tobacman, L.S., and Collins, J.H.: Bovine cardiac troponin T: amino acid sequences of the two isoforms. Biochemistry 26: 7035-7042, 1987.

Collins, J.H., Leszyk, J., Gusev, N.B., Verin, A.D., Potter, J.D., and Tobacman, L.S.: Analysis of troponin T isoforms. In: Calcium Binding Proteins in Health and Disease (Norman, A.W., Vanaman, T.C., and Means, A.R., eds.), pp. 570-572. Academic Press, 1987.

Leszyk, J., Dumaswala, R., Potter, J.D., and Collins, J.H.: Amino acid sequence of bovine cardiac troponin I. Biochemistry 27: 2821-2827, 1988.

Collins, J.H., Theibert, J.L., Franois,J.-M., Ashley, C.C., and Potter, J.D.: Amino acid sequences and Ca2+-binding properties of two isoforms of barnacle troponin C. Biochemistry 30: 702-707, 1991.

Garone, L., Theibert, J.L., Miegel, A., Mada, Y., Murphy, C., and Collins, J.H.: Lobster troponin C: amino acid sequences of three isoforms. Arch. Biochem. Biophys. 291: 89-91, 1991.

Cross-linking studies on troponin

Leszyk, J., Collins, J.H., Leavis, P.C., and Tao, T.: Crosslinking of rabbit skeletal muscle troponin with the photoactive reagent 4-maleimidobenzophenone: identification of residues in troponin I that are close to Cysteine-98 of troponin C. Biochemistry 26: 7042-7047, 1987.

Leszyk, J., Collins, J.H., Leavis, P.C., and Tao, T.: Crosslinking of rabbit skeletal muscle troponin subunits: labeling cysteine-98 of troponin C with 4-maleimidobenzophenone and analysis of products formed in the binary complex with troponin T and the ternary complex with troponins I and T. Biochemistry 27: 6983-6987, 1988.

Collins, J.H., Leszyk, J.D., Leavis, P.C., and Tao, T.: Sequencing of benzophenone-crosslinked troponin peptides. J. Protein Chem. 7: 214-215, 1988.

Leszyk, J. Grabarek, Z., Gergely, J., and Collins, J.H.: Characterization of zero length cross-links between rabbit skeletal muscle troponin C and troponin I: first evidence for a direct interaction between the inhibitory region of troponin I and the N-terminal, regulatory domain of troponin C. Biochemistry 29: 299-304, 1990.

Kobayashi, T., Tao, T., Grabarek, Z., Gergely, J., and Collins, J.H.: Crosslinking of residue 57 in the regulatory domain of a mutant rabbit skeletal muscle troponin C to the inhibitory region of troponin I. J. Biol. Chem. 266: 13,746-13,751. 1991.

Kobayashi, T., Tao, T., Gergely, J., and Collins, J.H.: Structure of the troponin complex: implications of photocross-linking of troponin I to troponin C thiol mutants. J. Biol. Chem. 269: 5725-5729, 1994.

Kobayashi, T., Grabarek, Z., Gergely, J., and Collins, J.H.: Extensive interactions between troponins C and I: zero length cross-linking of troponin I and acetylated troponin C. Biochemistry 34: 10946-10952, 1995.

Zhao, X., Collins, J.H., Falendysch, O.E., and Gusev, N.B: Identification of reactive carboxyl groups in troponin C. Biochem. Molec. Biol. International 38: 467-475, 1996.

Kobayashi, T., Leavis, P.L., and Collins, J.H.: Interaction of a troponin I inhibitory peptide with both domains of troponin C. Biochim. Biophys. Acta 1294: 25-30, 1996.

Kobayashi, T., Zhao, X., Wade, R., and Collins, J.H.: Ca2+-Dependent Interaction of the Inhibitory Region of Troponin I with Acidic Residues in the N-terminal Domain of Troponin C. Biochimica et Biophysica Acta 1430: 214-221, 1999.

Kobayashi, T., Zhao, X., Wade, R., and Collins, J.H.: Involvement of Conserved, Acidic Residues in the N-Terminal Domain of Troponin C in Calcium-Dependent Regulation. Biochemistry 38: 5386-5391, 1999.

Digel, J., Abugo, O., Kobayashi, T., Gryczynski, Z., Lakowicz, J.R., and Collins, J.H.: Calcium- and magnesium-dependent interactions between the C-terminus of troponin I and the N-terminal, regulatory domain of troponin C. Arch. Biochem. Biophys. 387: 243-249, 2001.

Fluorescence studies on troponin

Johnson, J.D., Collins, J.H. and Potter, J.D.: Dansylaziridine labelled troponin C: A fluorescent probe of Ca2+ binding to the Ca2+ specific regulatory sites. J. Biol. Chem. 253: 6451-6458, 1978.

Johnson, J.D., Collins, J.H., Robertson, S.P. and Potter, J.D.: A fluorescent probe study of Ca2+ binding to the Ca2+-specific sites of cardiac troponin and troponin C. J. Biol. Chem. 255: 9635-9640, 1980.

Zhao, X., Kobayashi, T., Malak, H., Gryczynski, I., Lakowicz, J., Wade, R.W., and Collins, J.H.: Calcium-induced troponin flexibility revealed by distance distribution measurements between engineered sites. J. Biol. Chem. 270: 15507-15514, 1995.

Zhao, X., Kobayashi, T., Gryczynski, Z., Gryczynski, I., Lakowicz, Wade, and Collins, J.H. (2000): Calcium-induced flexibility changes in the troponin C-troponin I complex. Biochim. Biophys. Acta, 1479: 247-254, 2000.

Kobayashi, T., Kobayashi, M., Gryczynski, Z., Lakowicz, J.R., and Collins, J.H.: Inhibitory Region of Troponin I: Ca2+-dependent Structural and Environmental Changes in the Troponin-Tropomyosin Complex and in Reconstituted Thin Filaments. Biochemistry 39: 86-91, 2000.

Kobayashi, T., Kobayashi, M., and Collins, J.H.: Ca2+-Dependent, myosin subfragment 1-induced proximity changes between actin and the inhibitory region of Troponin I. Biochim. Biophys. Acta 154: 148-154, 2001.

Structural studies on caldesmon

Leszyk, J., Mornet, D., Audemard, E., and Collins, J.H.: Amino acid sequence of a 15 kilodalton actin-binding fragment of turkey gizzard caldesmon: similarity with dystrophin, tropomyosin and the tropomyosin-binding region of troponin T. Biochem. Biophys. Res. Commun. 160: 210-216, 1989.

Leszyk, J., Mornet, D., Audemard, E., and Collins, J.H.: Caldesmon structure and function: sequence analysis of a 35 kilodalton actin- and calmodulin-binding fragment from the C-terminus of the turkey gizzard protein. Biochem. Biophys. Res. Commun. 160: 1371-1378, 1989.

Collins, J.H., Leszyk, J., Mornet, D., and Audemard, E.: Turkey gizzard caldesmon: complete sequence of a C-terminal thrombic fragment that binds actin, tropomyosin and calmodulin. Protein Sequences & Data Analysis 4: 29-32, 1991.

Wawrzynow, A., Collins, J.H., Bogatcheva, N.V., Vorotnikov, A.V., and Gusev, N.B.: Identification of the site phosphorylated by casein kinase II in smooth muscle caldesmon. FEBS Lett. 289: 213-216, 1991.

Vorotnikov, A.V., Gusev, N.B., Hua, S., Collins, J.H., Redwood, C.S., and Marston, S.B.: Identification of casein kinase II as a major endogenous caldesmon kinase in sheep aorta. FEBS Lett. 334: 18-22, 1993.

Vorotnikov, A.V., Gusev, N.B., Hua, S., Collins, J.H., Redwood, C.S., and Marston, S.B.: Phosphorylation of Aorta caldesmon by endogenous proteolytic fragments of protein kinase C. J. Muscle Res. Cell Motil. 15: 37-48, 1994.

Studies on miscellaneous Ca 2+-binding proteins

Crouch, T.H., Holroyde, M.J., Collins, J.H., Solaro, R.J. and Potter, J.D.: Interaction of calmodulin with skeletal muscle myosin light chain kinase. Biochemistry, 20: 6318-6325, 1981.

Collins, J.H., Johnson, J.D. and Szent-Gyrgyi, A.G.: Purification and characterization of a scallop sarcoplasmic high-affinity calcium-binding protein. Biochemistry 22: 341-345, 1983.

Collins, J.H., Cox, J.A., and Theibert, J.L.: Amino acid sequence of a sarcoplasmic calcium binding protein from the sandworm Nereis diversicolor. J. Biol. Chem. 263: 15378-15385, 1988.

Collins, J.H., Xi, Z., Alderson-Lang, B.H., Treves, S., and Volpe, P.: Sequence homology of a canine brain calcium-binding protein with calregulin and the human Ro/SS-A antigen. Biochem. Biophys. Res. Commun. 164: 575-579, 1989.

Dalla Libera, L., and Collins, J.H.: Myosin light chain kinase expression during smooth muscle development. Bioscience Reports 13: 289-295, 1993.

Structural studies on sarcoplasmic reticulum Ca2+-ATPase

Andersen, J., Vilsen, B., Collins, J.H., and Jrgensen, P.L.: Localization of E1-E2 conformational transitions of sarcoplasmic reticulum Ca2+-ATPase by tryptic cleavage and hydrophobic labelling. J. Membrane Biol. 93: 85-92, 1986.

Submilla, C., Cantilina, T., Collins, J.H., Malak, H., Lakowicz, J.R., and Inesi, G.: Structural perturbation of the transmembrane region interferes with calcium binding by the Ca2+ transport ATPase. J. Biol. Chem. 266: 12682-12689, 1991.

Wawrzynow, A., Collins, J.H., and Coan, C.: An iodoacetamide spin-label selectively labels a cysteine side chain in an occluded site on the Ca2+-ATPase of rabbit fast skeletal muscle sarcoplasmic reticulum. Biochemistry 32: 10803-10811, 1993.

Wawrzynow, A., and Collins, J.H.: Chemical modification of the Ca2+-ATPase of rabbit skeletal muscle sarcoplasmic reticulum: identification of sites labeled with aryl isothiocyanates and thiol-directed conformational probes. Biochim. Biophys. Acta 1203: 60-70, 1993.

Structural studies on calsequestrin

Scott, B.T., Simmerman, H.K.B., Collins, J.H., Nadal-Ginard, B., and Jones, L.R.: Complete amino acid sequence of canine cardiac calsequestrin deduced by cDNA cloning. J. Biol. Chem. 263: 8958-8964, 1988.

Collins, J.H., Tarcsafalvi, A., and Ikemoto, N.: Identification of a region of calsequestrin that binds to the junctional face membrane of sarcoplasmic reticulum. Biochem. Biophys. Res. Commun. 167: 189-193, 1990.

Volpe, P., Alderson-Lang, B.H., Madeddu, L., Damiani, E., Collins, J.H., and Margreth, A.: Calsequestrin, a component of the 1,4,5-triphosphate-sensitive Ca2+ store of chicken cerebellum. Neuron, 5: 713-721, 1990.

Structural studies on sarcolipin

Collins, J.H., Zot, A.S. and Kranias, E.G.: Isolation of two proteolipids from rabbit skeletal muscle sarcoplasmic reticulum. Prep. Biochem., 12: 255-264, 1982.

Wawrzynow, A., Theibert, J.L., Murphy, C., Jona, I., Martonosi, A., and Collins, J.H.: Sarcolipin, the "proteolipid" of skeletal muscle sarcoplasmic reticulum, is a unique, amphipathic, 31-residue peptide. Arch. Biochem. Biophys. 298: 620-623, 1992.

First report of FKBP association with the ryanodine receptor

Collins, J.H.: Sequence analysis of the ryanodine receptor: possible association with a 12K, FK506-binding immunophilin/protein kinase C inhibitor. Biochem. Biophys. Res. Commun. 178: 1288-1290, 1991.

Structural studies on phospholamban

Collins, J.H., Kranias, E.G., Reeves, A.S., Bilezikjian, L.M. and Schwartz, A.: Isolation of phospholamban and a second proteolipid component from canine cardiac sarcoplasmic reticulum. Biochem. Biophys. Res. Commun., 99: 796-803, 1981.

Simmerman, H.K.B., Collins, J.H., Theibert, J.L., Wegener, A.D., and Jones, L.R.: Sequence analysis of phospholamban: identification of phosphorylation sites and two major structural domains. J. Biol. Chem. 261: 13333-13341, 1986.

Collins, J.H., Jones, L.R., Simmerman, H.K.B., and Tada, M.: The structure of phospholamban and its role in activating Ca2+ transport in the sarcoplasmic reticulum. In: Calcium Binding Proteins in Health and Disease (Norman, A.W., Vanaman, T.C., and Means, A.R., eds.), pp. 92-94, Academic Press, 1987.

Structural studies on the alpha subunit of Na+,K+-ATPase

Lane, L.K., Potter, J.D. and Collins, J.H.: Large-scale purification of Na+,K+-ATPase and its protein subunits from lamb kidney medulla. Preparative Biochemistry 9: 157-170, 1979.

Lane, L.K., Gupte, S.S., Collins, J.H., Wallick, E.T., Johnson, J.D. and Schwartz, A.: Purification and characterization of lamb kidney Na+,K+-ATPase, In: Na+,K+-ATPase: Structure and Kinetics (Skou, J.C. and Nrby, J.G., eds.) pgs. 33-44, Academic Press, 1979.

Schwartz, A., Adams, R.J., Ball, W.J., Collins, J.H., Gupte, S.S., Lane, L.K., Reeves, A. and Wallick, E.T.: Structure, function and regulation of Na+,K+-ATPase. Int. J. Biochem. 12: 287-293, 1980.

Schwartz, A. and Collins, J.H.: Na+,K+-ATPase: Structure of the enzyme and mechanism of action of digitalis. In: Membranes and Transport (Martonosi, A., ed.), Vol. 1, pp. 521-527, Plenum, 1982.

Whitmer, K.R., Wallick, E.T., Epps, D.E., Lane, L.K., Collins, J.H. and Schwartz, A.: Effects of extracts of rat brain on the digitalis receptor. Life Sciences, 30: 2261-2275, 1982.

Munakata, H., Schmid, K., Collins, J.H., Zot, A.S., Lane, L.K. and Schwartz, A.: The alpha and beta subunits of lamb kidney Na+,K+-ATPase are both glycoproteins. Biochem. Biophys. Res. Commun. 107: 229-231, 1982.

Collins, J.H., Ball, W.J., Jr., Lane, L.K., and Zot, A.S.: Sequence studies on Na+,K+-ATPase. In: Methods in Protein Sequence Analysis (Elzinga, M., ed.), pp. 549-550, Humana, 1982.

Ball, W.J., Jr., Collins, J.H., Land, L. and Schwartz, A.: Antigenic properties of the alpha, beta and gamma subunits of Na+,K+-ATPase. In: Current Topics in Membranes and Transport Hoffman, J.F. and Forbush, B., III, eds.), Vol. 19, pp. 781-785, Academic Press, 1983.

Collins, J.H., Forbush, B., Lane, L.K., Ling, E., Schwartz, A. and Zot, A.S.: Structural Studies on Lamb Kidney Na+,K+-ATPase. In: Current Topics in Membranes and Transport (Hoffman, J.F. and Forbush, B., III, eds.), Vol. 19, pp. 131-134, Academic Press, 1983.

Collins, J.H., Zot, A.S., Ball, W.J., Jr., Lane, L.K. and Schwartz, A.: Tryptic digest of the alpha subunit of lamb kidney Na+,K+-ATPase. Biochim. Biophys. Acta 742: 358-365, 1983.

Ball, W.J., Jr., Collins, J.H., Lane, L.K. and Schwartz, A: Studies of the antigenic properties of the catalytic and glycoprotein subunits of Na+,K+-ATPase. Arch. Biochem. Biophys. 221: 371-380, 1983.

Collins, J.H. and Zot, A.S.: N-terminal sequences of the alpha and beta subunits of lamb kidney Na+,K+-ATPase. IRCS Med. Sci. 11: 299, 1983.

Jrgensen, P.L. and Collins, J.H.: Tryptic and chymotryptic cleavage sites in the sequence of the alpha subunit of Na+,K+-ATPase from outer medulla of mammalian kidney. Biochim. Biophys. Acta 860: 570-576, 1986.

Andersen, J.P., Jrgensen, P.L., and Collins, J.H.: Structural basis for E1-E2-transition accompanying active cation transport by Na+,K+-ATPase and Ca2+-ATPase. Implications for the pump mechanism. In: Perspectives of Biological Energy Transductions (Mukohata, Y., Morales, M.F., and Fleischer, S., eds.), pp. 249-255. Academic Press, 1987.

Jrgensen, P.L., and Collins, J.H.: Localization of tryptic and chymotryptic cleavage sites in the alpha subunit of Na+,K+-ATPase. In: The Na+,K+-Pump; Part A: Molecular Aspects (Skou, J.C., Nrby, J.G., Maunsbach, A.B., and Esmann, M., eds.), pp. 85-92, Alan R. Liss, 1988.

Structural studies on the gamma subunit of Na+,K+-ATPase

Reeves, A.S., Collins, J.H. and Schwartz, A.: Isolation and Characterization of the Na+,K+-ATPase Proteolipid. Biochem. Biophys. Res. Commun. 95: 1591-1598, 1980.

Collins, J.H., Forbush, B., Lane, L.K., Ling, E., Schwartz, A. and Zot, A.S.: Purification and characterization of a proteolipid component of Na+,K+-ATPase labeled with a photoaffinity derivative of ouabain. Biochim. Biophys. Acta, 686: 7-12, 1982.

Collins, J.H., and Leszyk, J.: The gamma subunit of Na+,K+-ATPase: a small, amphiphilic protein with a unique amino acid sequence. Biochemistry 26: 8665-8668, 1987.

Mercer, R.W., Biemesderfer, D., Bliss, D.P., Jr., Collins, J.H., and Forbush, B., III: Molecular cloning and immunological characterization of the gamma polypeptide, a small protein associated with the Na+,K+-ATPase. J. Cell Biol. 121: 579-586, 1993.

Structural studies on K+ channel-blocking peptide toxins

Rogowski, R.S., Krueger, B.K., Collins, J.H., and Blaustein, M.P.: Tityustoxin-Kalpha blocks voltage-gated, non-inactivating K+ channels and unblocks inactivating K+ channels blocked by alpha-dendrotoxin in synaptosomes. Proc. Natl. Acad. Sci. USA 91: 1475-1479, 1994.

Rogowski, R.S., Collins, J.H., O'Neill, T.J., Gustafson, T.A., Werkman, T.A., Rogawski, M.A., Tenenholz, T., Weber, D.J. and Blaustein, M.P.: Three new toxins from the scorpion, Pandinus imperator, selectively block certain voltage-gated K+ channels. Mol. Pharmacol. 50: 1167-1177, 1996

Tenenholz, T.C., Rogowski, R.S., Collins, J.H., Blaustein, M.P., and Weber, D.J.: Solution Structure for Pandinus Toxin K-alpha(PiTX-Kalpha), a Selective Blocker of A-Type Potassium Channels. Biochemistry 36: 2763-2771, 1997.

Studies on hemoglobin

Bucci, E., Fronticelli, C., Gryczynski, Z., Razynska, A., and Collins, J.H.: Effect of intramolecular crosslinks on the enthalpy and quaternary structure of the intermediates of oxygenation of human hemoglobin. Biochemistry 32: 3519-3526, 1993.

Razynska, A., Matheson-Urbaitis, B., Fronticelli, C., Collins, J.H., and Bucci, E.: Stabilization of the tetrameric structure of human and bovine hemoglobins by pseudocrosslinking with muconic acid. Arch. Biochem. Biophys. 326: 119-125, 1996.
Bucci, E., Razynska, A., Kwansa, H., Gryczynski, Z., Collins, J.H., Fronticelli, C., Unger, R., Braxenthaler, M., Moult, J., and Gilliland, G.: Positive and negative cooperativitites at subsequent steps of oxygenation regulate the allosteric behavior of multistate sebacylhemoglobin. Biochemistry 35: 3418-3425, 1996

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