Calcium Determines the Shape of Fibrillin*
暂无分享,去创建一个
D. Keene | D. Reinhardt | L. Sakai | H. Bächinger | B. A. Boswell | D. Mechling | Diane E. Mechling | Bruce A. Boswell
[1] D. Reinhardt,et al. Calcium Stabilizes Fibrillin-1 against Proteolytic Degradation* , 1997, The Journal of Biological Chemistry.
[2] T. Sasaki,et al. Fibrillin-1 and Fibulin-2 Interact and Are Colocalized in Some Tissues* , 1996, The Journal of Biological Chemistry.
[3] I. Campbell,et al. Solution Structure of a Pair of Calcium-Binding Epidermal Growth Factor-like Domains: Implications for the Marfan Syndrome and Other Genetic Disorders , 1996, Cell.
[4] D. Keene,et al. Fibrillin-1: organization in microfibrils and structural properties. , 1996, Journal of molecular biology.
[5] David W. Banner,et al. The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor , 1996, Nature.
[6] P. Handford,et al. Calcium binding properties of an epidermal growth factor-like domain pair from human fibrillin-1. , 1996, Journal of Molecular Biology.
[7] D. Milewicz,et al. Fibrillin–2 (FBN2) mutations result in the Marfan–like disorder, congenital contractural arachnodactyly , 1995, Nature Genetics.
[8] H Brandstetter,et al. X-ray structure of clotting factor IXa: active site and module structure related to Xase activity and hemophilia B. , 1995, Proceedings of the National Academy of Sciences of the United States of America.
[9] H. Dietz,et al. Mutations in the human gene for fibrillin-1 (FBN1) in the Marfan syndrome and related disorders. , 1995, Human molecular genetics.
[10] P. Handford,et al. The structure of a Ca2+-binding epidermal growth factor-like domain: Its role in protein-protein interactions , 1995, Cell.
[11] M. Raghunath,et al. Truncated profibrillin of a Marfan patient is of apparent similar size as fibrillin: intracellular retention leads to over-N-glycosylation. , 1995, Journal of molecular biology.
[12] P. Handford,et al. The Calcium Binding Properties and Molecular Organization of Epidermal Growth Factor-like Domains in Human Fibrillin-1 (*) , 1995, The Journal of Biological Chemistry.
[13] J. Berg,et al. Fibrillin domain folding and calcium binding: significance to Marfan syndrome. , 1995, Chemistry and Biology.
[14] R. Glanville,et al. Calcium binding, hydroxylation, and glycosylation of the precursor epidermal growth factor-like domains of fibrillin-1, the Marfan gene protein. , 1994, The Journal of biological chemistry.
[15] L. Peltonen,et al. Analyses of truncated fibrillin caused by a 366 bp deletion in the FBN1 gene resulting in Marfan syndrome. , 1994, The Biochemical journal.
[16] M. Ullner,et al. How an epidermal growth factor (EGF)-like domain binds calcium. High resolution NMR structure of the calcium form of the NH2-terminal EGF-like domain in coagulation factor X. , 1994, The Journal of biological chemistry.
[17] R. Mecham,et al. Structure and expression of fibrillin-2, a novel microfibrillar component preferentially located in elastic matrices , 1994, The Journal of cell biology.
[18] C. Kielty,et al. The role of calcium in the organization of fibrillin microfibrils , 1993, FEBS letters.
[19] T. Sasaki,et al. Structure and expression of fibulin-2, a novel extracellular matrix protein with multiple EGF-like repeats and consensus motifs for calcium binding , 1993, The Journal of cell biology.
[20] R. Timpl,et al. Sequence of extracellular mouse protein BM-90/fibulin and its calcium-dependent binding to other basement-membrane ligands. , 1993, European journal of biochemistry.
[21] H. Dietz,et al. Fibrillin binds calcium and is coded by cDNAs that reveal a multidomain structure and alternatively spliced exons at the 5' end. , 1993, Genomics.
[22] P. Bork,et al. Epidermal growth factor-like modules , 1993 .
[23] I. Campbell,et al. Ligand requirements for Ca2+ binding to EGF-like domains. , 1992, Protein engineering.
[24] T. Drakenberg,et al. Three-dimensional structure of the apo form of the N-terminal EGF-like module of blood coagulation factor X as determined by NMR spectroscopy and simulated folding. , 1992, Biochemistry.
[25] F. Rathjen,et al. The chicken neural extracellular matrix molecule restrictin: Similarity with EGF-, fibronectin type III-, and fibrinogen-like motifs , 1992, Neuron.
[26] I. Campbell,et al. The three‐dimensional structure of the first EGF‐like module of human factor IX: Comparison with EGF and TGF‐α , 1992, Protein science : a publication of the Protein Society.
[27] J. Stenflo,et al. Structure-function relationships of epidermal growth factor modules in vitamin K-dependent clotting factors. , 1991, Blood.
[28] R. Glanville,et al. Purification and partial characterization of fibrillin, a cysteine-rich structural component of connective tissue microfibrils. , 1991, The Journal of biological chemistry.
[29] R. Glanville,et al. Partial sequence of a candidate gene for the Marfan syndrome , 1991, Nature.
[30] M. Mattei,et al. Linkage of Marfan syndrome and a phenotypically related disorder to two different fibrillin genes , 1991, Nature.
[31] I. D. Campbell,et al. Key residues involved in calcium-binding motifs in EGF-like domains , 1991, Nature.
[32] J. Gulcher,et al. The complete cDNA sequence of human hexabrachion (Tenascin). A multidomain protein containing unique epidermal growth factor repeats. , 1991, The Journal of biological chemistry.
[33] M. Somerman,et al. Fibulin is an extracellular matrix and plasma glycoprotein with repeated domain structure , 1990, The Journal of cell biology.
[34] R. J. Fleming,et al. The gene Serrate encodes a putative EGF-like transmembrane protein essential for proper ectodermal development in Drosophila melanogaster. , 1990, Genes & development.
[35] J. Stenflo,et al. sup 1 H NMR assignment and secondary structure of the Ca sup 2+ -free form of the amino-terminal epidermal growth factor like domain in coagulation factor X , 1990 .
[36] P. Handford,et al. The role of beta‐hydroxyaspartate and adjacent carboxylate residues in the first EGF domain of human factor IX. , 1988, The EMBO journal.
[37] J. Campos-Ortega,et al. The neurogenic gene Delta of Drosophila melanogaster is expressed in neurogenic territories and encodes a putative transmembrane protein with EGF‐like repeats , 1987, The EMBO journal.
[38] C. Mathews,et al. The conformation of T4 bacteriophage dihydrofolate reductase from circular dichroism. , 1987, The Journal of biological chemistry.
[39] E. Engvall,et al. Fibrillin, a new 350-kD glycoprotein, is a component of extracellular microfibrils , 1986, The Journal of cell biology.
[40] B. Dahlbäck,et al. Isolation and sequence of the cDNA for human protein S, a regulator of blood coagulation. , 1986, Proceedings of the National Academy of Sciences of the United States of America.
[41] N. Morris,et al. The tissue form of type VII collagen is an antiparallel dimer. , 1986, The Journal of biological chemistry.
[42] S. Artavanis-Tsakonas,et al. Nucleotide sequence from the neurogenic locus Notch implies a gene product that shares homology with proteins containing EGF-like repeats , 1985, Cell.
[43] L. Fessler,et al. Protein assembly of procollagen and effects of hydroxylation. , 1974, The Journal of biological chemistry.
[44] U. K. Laemmli,et al. Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.
[45] K. V. van Holde,et al. Frictional coefficients of multisubunit structures. I. Theory , 1967, Biopolymers.