The Biological and Chemical Basis for Tissue-Selective Amyloid Disease
暂无分享,去创建一个
J. Kelly | W. Balch | R. L. Wiseman | J. Matteson | P. Hammarström | Y. Sekijima | Sean R. Miller | A. Sawkar | R. Wiseman | J. Kelly
[1] J. Sacchettini,et al. Synthesis and characterization of potent bivalent amyloidosis inhibitors that bind prior to transthyretin tetramerization. , 2003, Journal of the American Chemical Society.
[2] C. Wurth,et al. The most pathogenic transthyretin variant, L55P, forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions. , 1999, Biochemistry.
[3] J. Kelly,et al. Prevention of Transthyretin Amyloid Disease by Changing Protein Misfolding Energetics , 2003, Science.
[4] F. Studier,et al. Use of T7 RNA polymerase to direct expression of cloned genes. , 1990, Methods in enzymology.
[5] Wei Zheng,et al. Establishment and characterization of an immortalized Z310 choroidal epithelial cell line from murine choroid plexus , 2002, Brain Research.
[6] J. Kelly,et al. The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid. , 1996, Biochemistry.
[7] T. Tokuda,et al. Energetic Characteristics of the New Transthyretin Variant A25T May Explain Its Atypical Central Nervous System Pathology , 2003, Laboratory Investigation.
[8] B. Wallin,et al. Clinical improvement and amyloid regression after liver transplantation in hereditary transthyretin amyloidosis , 1993, The Lancet.
[9] K. Yutani,et al. Folding mechanism of mutant human lysozyme C77/95A with increased secretion efficiency in yeast. , 1992, The Journal of biological chemistry.
[10] Fred E. Cohen,et al. Therapeutic approaches to protein-misfolding diseases , 2003, Nature.
[11] J. Menting,et al. Thyroxine transport in choroid plexus. , 1987, The Journal of biological chemistry.
[12] O. Suhr,et al. Long‐term follow‐up of survival of liver transplant recipients with familial amyloid polyneuropathy (Portuguese type) , 2002, Liver transplantation : official publication of the American Association for the Study of Liver Diseases and the International Liver Transplantation Society.
[13] J. Hamilton,et al. Transthyretin: a review from a structural perspective , 2001, Cellular and Molecular Life Sciences CMLS.
[14] K. Sletten,et al. Fibril in senile systemic amyloidosis is derived from normal transthyretin. , 1990, Proceedings of the National Academy of Sciences of the United States of America.
[15] Michel Bouvier,et al. Pharmacological chaperones: potential treatment for conformational diseases , 2004, Trends in Endocrinology & Metabolism.
[16] C. Der,et al. GTP-binding mutants of rab1 and rab2 are potent inhibitors of vesicular transport from the endoplasmic reticulum to the Golgi complex , 1992, The Journal of cell biology.
[17] A Helenius,et al. Setting the standards: quality control in the secretory pathway. , 1999, Science.
[18] Joleen T White,et al. D18G transthyretin is monomeric, aggregation prone, and not detectable in plasma and cerebrospinal fluid: a prescription for central nervous system amyloidosis? , 2003, Biochemistry.
[19] R. Webster,et al. Assembly of influenza hemagglutinin trimers and its role in intracellular transport , 1986, The Journal of cell biology.
[20] F. Garzuly. [Clinical characteristics of Hungarian-type familial meningo-cerebrovascular amyloidosis]. , 1996, Orvosi hetilap.
[21] T. Harkany,et al. Cutaneous lymphatic amyloid deposits in ‘Hungarian‐type’ familial transthyretin amyloidosis: a case report , 2002, The British journal of dermatology.
[22] Joleen T White,et al. Transthyretin aggregation under partially denaturing conditions is a downhill polymerization. , 2004, Biochemistry.
[23] U. K. Laemmli,et al. Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.
[24] J. Kelly,et al. Alternative conformations of amyloidogenic proteins govern their behavior. , 1996, Current opinion in structural biology.
[25] M. Kikuchi,et al. Behavior of cysteine mutants of human lysozyme in de novo synthesis and in vivo secretion. , 1991, European journal of biochemistry.
[26] J. Riordan,et al. COPII-dependent export of cystic fibrosis transmembrane conductance regulator from the ER uses a di-acidic exit code , 2004, The Journal of cell biology.
[27] Daniel R. Jacobson,et al. Transthyretin Pro55, a variant associated with early-onset, aggressive, diffuse amyloidosis with cardiac and neurologic involvement , 1992, Human Genetics.
[28] Scott A. Peterson,et al. Inhibiting transthyretin amyloid fibril formation via protein stabilization. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[29] M. Benson. Leptomeningeal amyloid and variant transthyretins. , 1996, The American journal of pathology.
[30] J. Kearney,et al. Posttranslational association of immunoglobulin heavy chain binding protein with nascent heavy chains in nonsecreting and secreting hybridomas , 1986, The Journal of cell biology.
[31] C. Dobson. Protein folding and misfolding , 2003, Nature.
[32] S. Gottesman,et al. Posttranslational quality control: folding, refolding, and degrading proteins. , 1999, Science.
[33] C. Lacroix,et al. Genotypic-phenotypic variations in a series of 65 patients with familial amyloid polyneuropathy , 1998, Neurology.
[34] K. Mori. Tripartite Management of Unfolded Proteins in the Endoplasmic Reticulum , 2000, Cell.
[35] Ernest Beutler,et al. Chemical chaperones increase the cellular activity of N370S β-glucosidase: A therapeutic strategy for Gaucher disease , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[36] M. Benson,et al. Polymorphism of human plasma thyroxine binding prealbumin. , 1983, Biochemical and biophysical research communications.
[37] M. Benson,et al. Biochemical and molecular genetic characterization of a new variant prealbumin associated with hereditary amyloidosis. , 1986, The Journal of clinical investigation.
[38] M. Nakazato,et al. Change in variant transthyretin levels in patients with familial amyloidotic polyneuropathy type I following liver transplantation. , 1995, Biochemical and biophysical research communications.
[39] S. Ikeda. Clinical Picture and Outcome of Transthyretin-Related Familial Amyloid Polyneuropathy (FAP) in Japanese Patients , 2002, Clinical chemistry and laboratory medicine.
[40] F. Spagnoli,et al. Identification of a Bipotential Precursor Cell in Hepatic Cell Lines Derived from Transgenic Mice Expressing Cyto-Met in the Liver , 1998, The Journal of cell biology.
[41] J. Kelly,et al. Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[42] J. Kelly,et al. Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. , 1992, Biochemistry.
[43] H. Budka,et al. Familial meningocerebrovascular amyloidosis, Hungarian type, with mutant transthyretin (TTR Asp18Gly) , 1996, Neurology.
[44] Jian‐Qiang Fan. A contradictory treatment for lysosomal storage disorders: inhibitors enhance mutant enzyme activity. , 2003, Trends in pharmacological sciences.
[45] K D Wittrup,et al. Yeast polypeptide fusion surface display levels predict thermal stability and soluble secretion efficiency. , 1999, Journal of molecular biology.
[46] H. M. Petrassi,et al. An engineered transthyretin monomer that is nonamyloidogenic, unless it is partially denatured. , 2001, Biochemistry.
[47] R. Schekman,et al. Bi-directional protein transport between the ER and Golgi. , 2004, Annual review of cell and developmental biology.
[48] W. Balch,et al. Mise en place-this bud's for the Golgi. , 2004, Molecular cell.
[49] M. Benson,et al. Primary structure of an amyloid prealbumin and its plasma precursor in a heredofamilial polyneuropathy of Swedish origin. , 1984, Proceedings of the National Academy of Sciences of the United States of America.
[50] R. Kopito,et al. Cystic fibrosis: premature degradation of mutant proteins as a molecular disease mechanism. , 2003, Methods in molecular biology.
[51] K D Wittrup,et al. Secretion efficiency in Saccharomyces cerevisiae of bovine pancreatic trypsin inhibitor mutants lacking disulfide bonds is correlated with thermodynamic stability. , 1998, Biochemistry.
[52] K D Wittrup,et al. Protein Folding Stability Can Determine the Efficiency of Escape from Endoplasmic Reticulum Quality Control* , 1998, The Journal of Biological Chemistry.
[53] B. Moss,et al. Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase. , 1986, Proceedings of the National Academy of Sciences of the United States of America.
[54] D. Goodenough,et al. Multisubunit assembly of an integral plasma membrane channel protein, gap junction connexin43, occurs after exit from the ER , 1993, Cell.