Chou, M., Krause, K.-H., Campbell, K.P., Jensen, K.G., and Sjolund, R.D. Antibodies against the Calcium-Binding Protein Calsequestrin from Streptanthus tortuosus (Brassicaceae). Plant Physiol. 91, 1259-1261, 1989. (On Medline as “K. Campbell”).  [PDF]
Fischer, T.H., Barton, D.W., Krause, K.-H., White, T.E., Campbell, K.P., and White, G.C., II. The Identification of Sarcoplasmic Reticulum Terminal Cisternae Proteins in Platelets. Biochem. J. 263, 605-608, 1989.  [PDF]
Perez-Reyes, E., Kim, H.S., Lacerda, A.E., Horne, W., Wei, X., Rampe, D., Campbell, K.P., Brown, A.M., and Birnbaumer, L. Induction of Calcium Currents by the Expression of the a1-Subunit of the Dihydropyridine Receptor from Skeletal Muscle. Nature340, 233-236, 1989.  [PDF]
Jorgensen, A.O., Shen, A.C.-Y., Arnold, W., Leung, A.T., and Campbell, K.P. Subcellular Distribution of the 1,4-Dihydropyridine Receptor in Rabbit Skeletal Muscle In Situ: An Immunofluorescence and Immunocolloidal Gold-Labeling Study. J. Cell Biol. 109, 135-147, 1989.  [PDF]
Kutchai, H. and Campbell, K.P. Calcium Transport by Sarcoplasmic Reticulum of Skeletal Muscle Is Inhibited by Antibodies Against the 53-Kilodalton Glycoprotein of the Sarcoplasmic Reticulum Membrane. Biochemistry 28, 4830-4839, 1989.  [PDF]
Knudson, C.M. and Campbell, K.P. Albumin Is a Major Protein Component of Transverse Tubule Vesicles Isolated from Skeletal Muscle. J. Biol. Chem. 264, 10795-10798, 1989.  [PDF]
Campbell, K.P. and Kahl, S.D. Association of Dystrophin and an Integral Membrane Glycoprotein. Nature 338, 259-262, 1989.  [PDF]
Krause, K.-H., Chou, M., Thomas, M.A., Sjolund, R.D., and Campbell, K.P. Plant Cells Contain Calsequestrin. J. Biol. Chem. 264, 4269-4272, 1989.  [PDF]
Thomas, K., Navarro, J., Benson, R.J.J., Campbell, K.P., Rotundo, R.L., and Fine, R.E. Newly Synthesized Calsequestrin, Destined for the Sarcoplasmic Reticulum, Is Contained in Early/Intermediate Golgi-Derived Clathrin-Coated Vesicles. J. Biol. Chem. 264, 3140-3145, 1989.  [PDF]
Sharp, A.H. and Campbell, K.P. Characterization of the 1,4-Dihydropyridine Receptor Using Subunit-Specific Polyclonal Antibodies. Evidence for a 32,000-Da Subunit. J. Biol. Chem. 264, 2816-2825, 1989.  [PDF]
Knudson, C.M., Chaudhari, N., Sharp, A.H., Powell, J.A., Beam, K.G., and Campbell, K.P. Specific Absence of the a1 Subunit of the Dihydropyridine Receptor in Mice with Muscular Dysgenesis. J. Biol. Chem. 264, 1345-1348, 1989.  [PDF]
Block, B.A., Imagawa, T., Campbell, K.P., and Franzini-Armstrong, C. Structural Evidence for Direct Interaction between the Molecular Components of the Transverse Tubule/Sarcoplasmic Reticulum Junction in Skeletal Muscle. J. Cell Biol. 107, 2587-2600, 1988.  [PDF]
Ma, J., Fill, M., Knudson, C.M., Campbell, K.P., and Coronado, R. Ryanodine Receptor of Skeletal Muscle Is a Gap Junction-Type Channel. Science 242, 99-102, 1988.  [PDF]
Ellis, S.B., Williams, M.E., Ways, N.R., Brenner, R., Sharp, A.H., Leung, A.T., Campbell, K.P., McKenna, E., Koch, W.J., Hui, A., Schwartz, A., and Harpold, M.M. Sequence and Expression of mRNAs Encoding the a1 and a2 Subunits of a DHP-Sensitive Calcium Channel. Science 241, 1661-1664, 1988.  [PDF]
Smith, J.S., Imagawa, T., Ma, J., Fill, M., Campbell, K.P., and Coronado, R. Purified Ryanodine Receptor from Rabbit Skeletal Muscle Is the Calcium-Release Channel of Sarcoplasmic Reticulum. J. Gen. Physiol. 92, 1-26, 1988.  [PDF]
Grover, A.K., Boonstra, I., Garfield, R.E., and Campbell, K.P. Ca Pumps in Rabbit Stomach Smooth Muscle Plasma Membrane and Endoplasmic Reticulum. Biochemical Archives 4,169-179, 1988.  [PDF]
Knudson, C.M., Hoffman, E.P., Kahl, S.D., Kunkel, L.M., and Campbell, K.P. Evidence for the Association of Dystrophin with the Transverse Tubular System in Skeletal Muscle. J. Biol. Chem. 263, 8480-8484, 1988.  [PDF]
Leung, A.T., Imagawa, T., and Campbell, K.P. Monoclonal Antibody Characterization of the 1,4-Dihydropyridine Receptor of Rabbit Skeletal Muscle. Ann. N. Y. Acad. Sci. 552, 43-46, 1988.  [PDF]
Jorgensen, A.O., Arnold, W., Pepper, D.R., Kahl, S.D., Mandel F., and Campbell, K.P. A Monoclonal Antibody to the Ca2+-ATPase of Cardiac Sarcoplasmic Reticulum Cross-Reacts with Slow Type I but Not with Fast Type II Canine Skeletal Muscle Fibers: An Immunocytochemical and Immunochemical Study. Cell Motil. Cytoskeleton 9, 164-174, 1988.  [PDF]
Leung, A.T., Imagawa, T., Block, B., Franzini-Armstrong, C., and Campbell, K.P. Biochemical and Ultrastructural Characterization of the 1,4-Dihydropyridine Receptor from Rabbit Skeletal Muscle. Evidence for a 52,000-Da Subunit. J. Biol. Chem. 263, 994-1001, 1988.  [PDF]
Hoffman, E.P., Knudson, C.M., Campbell, K.P., and Kunkel, L.M. Subcellular Fractionation of Dystrophin to the Triads of Skeletal Muscle. Nature 330, 754-758, 1987.  [PDF]
Imagawa, T., Smith, J.S., Coronado, R., and Campbell, K.P. Purified Ryanodine Receptor from Skeletal Muscle Sarcoplasmic Reticulum Is the Ca2+-Permeable Pore of the Calcium Release Channel. J. Biol. Chem. 262, 16636-16643, 1987.  [PDF]
Fischer, T.H., Campbell, K.P., and White, G.C., II. An Investigation of Functional Similarities between the Sarcoplasmic Reticulum and Platelet Calcium-Dependent Adenosinetriphosphatases with the Inhibitors Quercetin and Calmidazolium. Biochemistry 26, 8024-8030, 1987.  [PDF]
Sharp, A.H. and Campbell, K.P. Affinity Purification of Antibodies Specific for 1,4-Dihydropyridine Ca2+ Channel Blockers. Circ. Res. 61(4, Suppl. I), I-37-I-45, 1987.  [PDF]
Sharp, A.H., Imagawa, T., Leung, A.T., and Campbell, K.P. Identification and Characterization of the Dihydropyridine Binding Subunit of the Skeletal Muscle Dihydropyridine Receptor. J. Biol. Chem. 262, 12309-12315, 1987.  [PDF]
Campbell, K.P., Sharp, A.H., and Kahl, S.D. Anti-Dihydropyridine Antibodies Exhibit [3H]Nitrendipine Binding Properties Similar to the Membrane Receptor for the 1,4-Dihydropyridine Ca2+ Channel Antagonists. J. Cardiovasc. Pharmacol. 9(Suppl. 4), S113-S121, 1987.  [PDF]
Imagawa, T., Leung, A.T., and Campbell, K.P. Phosphorylation of the 1,4-Dihydropyridine Receptor of the Voltage-Dependent Ca2+ Channel by an Intrinsic Protein Kinase in Isolated Triads from Rabbit Skeletal Muscle. J. Biol. Chem. 262, 8333-8339, 1987.  [PDF]
Leung, A.T., Imagawa, T., and Campbell, K.P. Structural Characterization of the 1,4-Dihydropyridine Receptor of the Voltage-Dependent Ca2+ Channel from Rabbit Skeletal Muscle. Evidence for Two Distinct High Molecular Weight Subunits. J. Biol. Chem.262, 7943-7946, 1987.  [PDF]
Campbell, K.P., Knudson, C.M., Imagawa, T., Leung, A.T., Sutko, J.L., Kahl, S.D., Raab, C.R., and Madson, L. Identification and Characterization of the High Affinity [3H]Ryanodine Receptor of the Junctional Sarcoplasmic Reticulum Ca2+ Release Channel. J. Biol. Chem. 262, 6460-6463, 1987.  [PDF]
Lattanzio, F.A., Schlatterer, R.G., Nicar, M., Campbell, K.P., and Sutko, J.L. The Effects of Ryanodine on Passive Calcium Fluxes Across Sarcoplasmic Reticulum Membranes. J. Biol. Chem. 262, 2711-2718, 1987.  [PDF]
Campbell, K.P., Sharp, A., Strom, M., and Kahl, S.D. High-Affinity Antibodies to the 1,4-Dihydropyridine Ca2+-Channel Blockers. Proc. Natl. Acad. Sci. U.S.A. 83, 2792-2796, 1986.  [PDF]
Fischer, T.H., Campbell, K.P., and White, G.C., II. Evidence That Platelet and Skeletal Sarcoplasmic Reticulum Ca2+-ATPase are Structurally Distinct. J. Biol. Chem. 260, 8996-9001, 1985.  [PDF]
Jorgensen, A.O., Shen, A.C.-Y., and Campbell, K.P. Ultrastructural Localization of Calsequestrin in Adult Rat Atrial and Ventricular Muscle Cells. J. Cell Biol. 101, 257-268, 1985.  [PDF]