Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum

[1]  V. Fülöp,et al.  N-terminal arm exchange is observed in the 2.15 A crystal structure of oxidized nitrite reductase from Pseudomonas aeruginosa. , 1997, Structure.

[2]  Yvonne M. Kobayashi,et al.  Complex Formation between Junctin, Triadin, Calsequestrin, and the Ryanodine Receptor , 1997, The Journal of Biological Chemistry.

[3]  R. Taylor,et al.  Structure of TcpG, the DsbA protein folding catalyst from Vibrio cholerae. , 1997, Journal of molecular biology.

[4]  P. Dumas,et al.  Proline-dependent oligomerization with arm exchange. , 1997, Structure.

[5]  C. Hidalgo,et al.  Protons induce calsequestrin conformational changes. , 1996, Biophysical journal.

[6]  T. Creighton,et al.  Identifying and characterizing a structural domain of protein disulfide isomerase. , 1996, Biochemistry.

[7]  D Eisenberg,et al.  3D domain swapping: A mechanism for oligomer assembly , 1995, Protein science : a publication of the Protein Society.

[8]  K. Campbell,et al.  Association of Triadin with the Ryanodine Receptor and Calsequestrin in the Lumen of the Sarcoplasmic Reticulum (*) , 1995, The Journal of Biological Chemistry.

[9]  W. Cook,et al.  Drug binding by calmodulin: crystal structure of a calmodulin-trifluoperazine complex. , 1994, Biochemistry.

[10]  E A Merritt,et al.  Raster3D Version 2.0. A program for photorealistic molecular graphics. , 1994, Acta crystallographica. Section D, Biological crystallography.

[11]  W. Diekmann,et al.  Retention and retrieval: both mechanisms cooperate to maintain calreticulin in the endoplasmic reticulum. , 1994, Journal of cell science.

[12]  M. Kasai,et al.  Regulation of calcium channel in sarcoplasmic reticulum by calsequestrin. , 1994, Biochemical and biophysical research communications.

[13]  A. Gronenborn,et al.  Solution structure of a calmodulin-target peptide complex by multidimensional NMR. , 1994, Science.

[14]  S. Baksh,et al.  Crystallization of canine cardiac calsequestrin. , 1994, Journal of molecular biology.

[15]  F A Quiocho,et al.  Modulation of calmodulin plasticity in molecular recognition on the basis of x-ray structures. , 1993, Science.

[16]  A. Dunker,et al.  Ca(2+)-induced folding and aggregation of skeletal muscle sarcoplasmic reticulum calsequestrin. The involvement of the trifluoperazine-binding site. , 1993, The Journal of biological chemistry.

[17]  John Kuriyan,et al.  Crystal structure of the DsbA protein required for disulphide bond formation in vivo , 1993, Nature.

[18]  A. Lampen,et al.  CaBP2 is a rat homolog of ERp72 with proteindisulfide isomerase activity. , 1993, European journal of biochemistry.

[19]  F A Quiocho,et al.  Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex. , 1992, Science.

[20]  S. Treves,et al.  Molecular cloning, functional expression and tissue distribution of the cDNA encoding frog skeletal muscle calsequestrin. , 1992, The Biochemical journal.

[21]  J. Lytton,et al.  Intracellular calcium: molecules and pools , 1992, Current Biology.

[22]  N. Alpert,et al.  Cloning and characterization of the gene encoding rabbit cardiac calsequestrin. , 1991, Gene.

[23]  K. Sharp,et al.  Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons , 1991, Proteins.

[24]  P. Kraulis A program to produce both detailed and schematic plots of protein structures , 1991 .

[25]  M. Ronjat,et al.  Intravesicular calcium transient during calcium release from sarcoplasmic reticulum. , 1991, Biochemistry.

[26]  K. Krause,et al.  Thermodynamics of cation binding to rabbit skeletal muscle calsequestrin. Evidence for distinct Ca(2+)- and Mg(2+)-binding sites. , 1991, The Journal of biological chemistry.

[27]  J. Zou,et al.  Improved methods for building protein models in electron density maps and the location of errors in these models. , 1991, Acta crystallographica. Section A, Foundations of crystallography.

[28]  D. Clegg,et al.  Identification and developmental expression of a chicken calsequestrin homolog. , 1990, Developmental biology.

[29]  H. Eklund,et al.  Crystal structure of thioredoxin from Escherichia coli at 1.68 A resolution. , 1990, Journal of molecular biology.

[30]  H. Willard,et al.  Characterization and localization to human chromosome 1 of human fast-twitch skeletal muscle calsequestrin gene , 1990, Somatic cell and molecular genetics.

[31]  M K Smith,et al.  Calcium/calmodulin-dependent protein kinase II. , 1989, The Biochemical journal.

[32]  T. Soderling,et al.  Regulatory interactions of the calmodulin-binding, inhibitory, and autophosphorylation domains of Ca2+/calmodulin-dependent protein kinase II. , 1988, The Journal of biological chemistry.

[33]  D. Bacon,et al.  A fast algorithm for rendering space-filling molecule pictures , 1988 .

[34]  P. Kelly,et al.  Active site-directed inhibition of Ca2+/calmodulin-dependent protein kinase type II by a bifunctional calmodulin-binding peptide. , 1988, Proceedings of the National Academy of Sciences of the United States of America.

[35]  J. H. Collins,et al.  Complete amino acid sequence of canine cardiac calsequestrin deduced by cDNA cloning. , 1988, The Journal of biological chemistry.

[36]  T. Soderling,et al.  Calcium/calmodulin-dependent protein kinase II. Characterization of distinct calmodulin binding and inhibitory domains. , 1988, The Journal of biological chemistry.

[37]  L. Fliegel,et al.  Structure of the rabbit fast-twitch skeletal muscle calsequestrin gene. , 1988, The Journal of biological chemistry.

[38]  L. Jones,et al.  Ca2+ binding effects on protein conformation and protein interactions of canine cardiac calsequestrin. , 1988, The Journal of biological chemistry.

[39]  R. Reithmeier,et al.  Fragmentation of rabbit skeletal muscle calsequestrin: spectral and ion binding properties of the carboxyl-terminal region. , 1987, Biochemistry.

[40]  C. Franzini-armstrong,et al.  The structure of calsequestrin in triads of vertebrate skeletal muscle: a deep-etch study , 1987, The Journal of cell biology.

[41]  R. Reithmeier,et al.  Amino acid sequence of rabbit fast-twitch skeletal muscle calsequestrin deduced from cDNA and peptide sequencing. , 1987, Proceedings of the National Academy of Sciences of the United States of America.

[42]  R. Williams,et al.  Secondary structure of calsequestrin in solutions and in crystals as determined by Raman spectroscopy. , 1986, The Journal of biological chemistry.

[43]  G A Petsko,et al.  Aromatic-aromatic interaction: a mechanism of protein structure stabilization. , 1985, Science.

[44]  S. Fleischer,et al.  Purification and crystallization of the calcium binding protein of sarcoplasmic reticulum from skeletal muscle. , 1985, Proceedings of the National Academy of Sciences of the United States of America.

[45]  A. Edelman,et al.  Identification of the calmodulin-binding domain of skeletal muscle myosin light chain kinase. , 1985, Proceedings of the National Academy of Sciences of the United States of America.

[46]  R. Reithmeier,et al.  Characterization of skeletal muscle calsequestrin by 1H NMR spectroscopy. , 1984, The Journal of biological chemistry.

[47]  S. Fleischer,et al.  Preparation and morphology of sarcoplasmic reticulum terminal cisternae from rabbit skeletal muscle , 1984, The Journal of cell biology.

[48]  R. Reithmeier,et al.  Size and shape of rabbit skeletal muscle calsequestrin. , 1984, The Journal of biological chemistry.

[49]  N. Thorn,et al.  Calcium/sodium exchange in purified secretory vesicles from bovine neurohypophyses. , 1983, Cell calcium.

[50]  J Gariépy,et al.  Localization of a trifluoperazine binding site on troponin C. , 1983, Biochemistry.

[51]  H. Shuman,et al.  Calcium release and ionic changes in the sarcoplasmic reticulum of tetanized muscle: an electron-probe study , 1981, The Journal of cell biology.

[52]  C. Brändén,et al.  Relation between structure and function of α/β–protejns , 1980, Quarterly Reviews of Biophysics.

[53]  B. Weiss,et al.  Binding of trifluoperazine to the calcium-dependent activator of cyclic nucleotide phosphodiesterase. , 1977, Molecular pharmacology.

[54]  D. Maclennan,et al.  Effects of cation binding on the conformation of calsequestrin and the high affinity calcium-binding protein of sarcoplasmic reticulum. , 1974, The Journal of biological chemistry.

[55]  J. Gergely,et al.  Studies on a metal-binding protein of the sarcoplasmic reticulum. , 1974, The Journal of biological chemistry.

[56]  J. Gergely,et al.  Interaction of divalent cations with the 55,000-dalton protein component of the sarcoplasmic reticulum. Studies of fluorescence and circular dichroism. , 1972, The Journal of biological chemistry.

[57]  D. Maclennan,et al.  Isolation of a calcium-sequestering protein from sarcoplasmic reticulum. , 1971, Proceedings of the National Academy of Sciences of the United States of America.

[58]  C. N. Reilley,et al.  Heat and Entropies of Formation of Metal Chelates of Polyamine and Polyaminocarboxylate Ligands. , 1965 .

[59]  W Furey,et al.  PHASES-95: a program package for processing and analyzing diffraction data from macromolecules. , 1997, Methods in enzymology.

[60]  M. James,et al.  Crystal structures of the helix-loop-helix calcium-binding proteins. , 1989, Annual review of biochemistry.

[61]  S. Fleischer,et al.  [25] Purification and crystallization of calcium-binding protein from skeletal muscle sarcoplasmic reticulum , 1988 .

[62]  E. Haber,et al.  The heart and cardiovascular system , 1986 .

[63]  B. C. Wang Resolution of phase ambiguity in macromolecular crystallography. , 1985, Methods in enzymology.

[64]  R. Hodges,et al.  CHAPTER 5 – Structural Studies on Calmodulin and Troponin C: Phenothiazine, Peptide, and Protein Interactions with Calcium-Induced Helices , 1985 .

[65]  D. Hartshorne,et al.  Calmodulin antagonists and cellular physiology , 1985 .