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. Nature 340, 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]