Protein misfolding and human disease.
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Søren Vang | Peter Bross | Niels Gregersen | P. Bross | N. Gregersen | J. Christensen | Jane H Christensen | Søren Vang
[1] A. Ciechanover,et al. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. , 2002, Physiological reviews.
[2] M. Masucci,et al. Endoplasmic reticulum stress compromises the ubiquitin-proteasome system. , 2005, Human molecular genetics.
[3] M. Bucciantini,et al. Insights into the molecular basis of the differing susceptibility of varying cell types to the toxicity of amyloid aggregates , 2005, Journal of Cell Science.
[4] D. Perlmutter,et al. Grp78, Grp94, and Grp170 interact with alpha1-antitrypsin mutants that are retained in the endoplasmic reticulum. , 2005, American journal of physiology. Gastrointestinal and liver physiology.
[5] A. Goldberg,et al. Cellular Defenses against Unfolded Proteins A Cell Biologist Thinks about Neurodegenerative Diseases , 2001, Neuron.
[6] L. Serrano,et al. Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations. , 2002, Journal of molecular biology.
[7] R. Ellis. The molecular chaperone concept. , 1990, Seminars in cell biology.
[8] David Murphy,et al. Autophagy is a prosurvival mechanism in cells expressing an autosomal dominant familial neurohypophyseal diabetes insipidus mutant vasopressin transgene , 2005, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.
[9] S. Packman,et al. The molecular basis of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency in compound heterozygous patients: is there correlation between genotype and phenotype? , 1997, Human molecular genetics.
[10] L. Bruijn,et al. Unraveling the mechanisms involved in motor neuron degeneration in ALS. , 2004, Annual review of neuroscience.
[11] F. Bricaire,et al. Neurodegenerative diseases and oxidative stress. , 2004, Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie.
[12] Nicholas J. Hoogenraad,et al. Molecular Chaperones Hsp90 and Hsp70 Deliver Preproteins to the Mitochondrial Import Receptor Tom70 , 2003, Cell.
[13] P. Bross,et al. Biochemical characterization of purified, human recombinant Lys304-->Glu medium-chain acyl-CoA dehydrogenase containing the common disease-causing mutation and comparison with the normal enzyme. , 1997, European journal of biochemistry.
[14] Ellis Rj. The molecular chaperone concept. , 1990 .
[15] R. Ellis,et al. Macromolecular crowding: an important but neglected aspect of the intracellular environment. , 2001, Current opinion in structural biology.
[16] M. Duchen,et al. Mitochondria, Ca2+ and neurodegenerative disease. , 2002, European journal of pharmacology.
[17] L. Bolund,et al. Misfolding, Degradation, and Aggregation of Variant Proteins , 2003, Journal of Biological Chemistry.
[18] P. Muchowski,et al. Modulation of neurodegeneration by molecular chaperones , 2005, Nature Reviews Neuroscience.
[19] T. Rapoport,et al. Retro-translocation of proteins from the endoplasmic reticulum into the cytosol , 2002, Nature Reviews Molecular Cell Biology.
[20] Milan Macek,et al. Cystic fibrosis: A worldwide analysis of CFTR mutations—correlation with incidence data and application to screening , 2002, Human mutation.
[21] D. Perlmutter. α1-Antitrypsin Deficiency , 2011 .
[22] Steven Henikoff,et al. SIFT: predicting amino acid changes that affect protein function , 2003, Nucleic Acids Res..
[23] F. Hartl,et al. An unstable transmembrane segment in the cystic fibrosis transmembrane conductance regulator , 1999, The EMBO journal.
[24] G. Petsko,et al. Misfolded Proteins Are Competent to Mediate a Subset of the Responses to Heat Shock in Saccharomyces cerevisiae * 210 , 2002, The Journal of Biological Chemistry.
[25] D. Perlmutter,et al. Accumulation of mutant alpha1-antitrypsin Z in the endoplasmic reticulum activates caspases-4 and -12, NFkappaB, and BAP31 but not the unfolded protein response. , 2005, The Journal of biological chemistry.
[26] M. Prevost,et al. A missense mutation in the αB-crystallin chaperone gene causes a desmin-related myopathy , 1998, Nature Genetics.
[27] V. Yee,et al. Characterization of Four Variant Forms of Human Propionyl-CoA Carboxylase Expressed in Escherichia coli* , 2005, Journal of Biological Chemistry.
[28] J. Wakefield,et al. Efficient Intracellular Processing of the Endogenous Cystic Fibrosis Transmembrane Conductance Regulator in Epithelial Cell Lines* , 2004, Journal of Biological Chemistry.
[29] N. Gregersen,et al. Six novel mutations in the arginine vasopressin gene in 15 kindreds with autosomal dominant familial neurohypophyseal diabetes insipidus give further insight into the pathogenesis , 2004, European Journal of Human Genetics.
[30] C. Dobson. Protein folding and misfolding , 2003, Nature.
[31] J. Frydman. Folding of newly translated proteins in vivo: the role of molecular chaperones. , 2001, Annual review of biochemistry.
[32] N. Pfanner,et al. The Protein Import Machinery of Mitochondria* , 2004, Journal of Biological Chemistry.
[33] J. Saffitz,et al. Desmin-related cardiomyopathy in transgenic mice: a cardiac amyloidosis. , 2004, Proceedings of the National Academy of Sciences of the United States of America.
[34] Fabrizio Chiti,et al. Prefibrillar Amyloid Protein Aggregates Share Common Features of Cytotoxicity* , 2004, Journal of Biological Chemistry.
[35] S. Lipton,et al. Molecular pathways to neurodegeneration , 2004, Nature Medicine.
[36] P. Stenson,et al. Human Gene Mutation Database (HGMD®): 2003 update , 2003, Human mutation.
[37] Patricia L Clark,et al. Protein folding in the cell: reshaping the folding funnel. , 2004, Trends in biochemical sciences.
[38] Modesto Orozco,et al. PMUT: a web-based tool for the annotation of pathological mutations on proteins , 2005, Bioinform..
[39] P. Csermely,et al. Aging and molecular chaperones , 2003, Experimental Gerontology.
[40] C. Richter-Landsberg,et al. Stress proteins in neural cells: functional roles in health and disease , 2003, Cellular and Molecular Life Sciences CMLS.
[41] J. Kelly,et al. The Biological and Chemical Basis for Tissue-Selective Amyloid Disease , 2005, Cell.
[42] P. Bork,et al. Human non-synonymous SNPs: server and survey. , 2002, Nucleic acids research.
[43] A. Dürr,et al. Hereditary spastic paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial chaperonin Hsp60. , 2002, American journal of human genetics.
[44] D. Perlmutter,et al. Accumulation of Mutant α1-Antitrypsin Z in the Endoplasmic Reticulum Activates Caspases-4 and -12, NFκB, and BAP31 but Not the Unfolded Protein Response* , 2005, Journal of Biological Chemistry.
[45] M. Amaral,et al. Most F508del-CFTR Is Targeted to Degradation at an Early Folding Checkpoint and Independently of Calnexin , 2005, Molecular and Cellular Biology.
[46] C. Jacob,et al. Oxidative activation of antioxidant defence. , 2005, Trends in biochemical sciences.
[47] M. Groll,et al. Molecular shredders: how proteasomes fulfill their role. , 2003, Current opinion in structural biology.
[48] R. Kaufman,et al. The mammalian unfolded protein response. , 2003, Annual review of biochemistry.
[49] M. Ryan,et al. A mitochondrial specific stress response in mammalian cells , 2002, The EMBO journal.
[50] K. Uchida,et al. 4-Hydroxy-2-nonenal: a product and mediator of oxidative stress. , 2003, Progress in lipid research.
[51] A. Ballabio,et al. Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia , 2003, The Journal of cell biology.
[52] Beate Gerstbrein,et al. Dying for a cause: invertebrate genetics takes on human neurodegeneration , 2003, Nature Reviews Genetics.
[53] C. Dobson,et al. Protein misfolding, functional amyloid, and human disease. , 2006, Annual review of biochemistry.
[54] M. Spiess,et al. Degradation of Wild-type Vasopressin Precursor and Pathogenic Mutants by the Proteasome* , 2004, Journal of Biological Chemistry.
[55] R. Kopito,et al. Impairment of the ubiquitin-proteasome system by protein aggregation. , 2001, Science.
[56] M. Ugarte,et al. Expression Analysis of Phenylketonuria Mutations , 2000, The Journal of Biological Chemistry.
[57] M. Maurizi,et al. AAA proteins: in search of a common molecular basis , 2001, EMBO reports.
[58] Daniel Kaganovich,et al. Protein quality control: chaperones culling corrupt conformations , 2005, Nature Cell Biology.
[59] J. Riordan,et al. The DeltaF508 mutation results in loss of CFTR function and mature protein in native human colon. , 2004, Gastroenterology.
[60] R. Schekman,et al. Bi-directional protein transport between the ER and Golgi. , 2004, Annual review of cell and developmental biology.
[61] I. Batinic-Haberle,et al. Oxidants, antioxidants and the ischemic brain , 2004, Journal of Experimental Biology.
[62] K. Dill. Theory for the folding and stability of globular proteins. , 1985, Biochemistry.
[63] Daniel J Klionsky,et al. Development by self-digestion: molecular mechanisms and biological functions of autophagy. , 2004, Developmental cell.
[64] E. Schon,et al. Neuronal degeneration and mitochondrial dysfunction. , 2003, The Journal of clinical investigation.
[65] R. Frizzell,et al. The role of regulated CFTR trafficking in epithelial secretion. , 2003, American journal of physiology. Cell physiology.
[66] H. Horvitz,et al. Superoxide Dismutase Concentration and Activity in Familial Amyotrophic Lateral Sclerosis , 1995, Journal of neurochemistry.
[67] J. Frydman,et al. Actin mutations in hypertrophic and dilated cardiomyopathy cause inefficient protein folding and perturbed filament formation , 2005, The FEBS journal.
[68] T. Sommer,et al. ERAD: the long road to destruction , 2005, Nature Cell Biology.
[69] J. Vasiliev,et al. Thread-grain transition of mitochondrial reticulum as a step of mitoptosis and apoptosis , 2004, Molecular and Cellular Biochemistry.
[70] C. Dobson,et al. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases , 2002, Nature.
[71] J. Christensen,et al. Autosomal dominant familial neurohypophyseal diabetes insipidus. , 2003, APMIS. Supplementum.
[72] Steven W. Taylor,et al. Global organellar proteomics. , 2003, Trends in biotechnology.
[73] D. Perlmutter. Liver injury in alpha1-antitrypsin deficiency: an aggregated protein induces mitochondrial injury. , 2002, The Journal of clinical investigation.
[74] L. Bolund,et al. Expression of three different mutations in the arginine vasopressin gene suggests genotype–phenotype correlation in familial neurohypophyseal diabetes insipidus kindreds , 2005, Clinical endocrinology.
[75] Valerie Daggett,et al. The complete folding pathway of a protein from nanoseconds to microseconds , 2003, Nature.
[76] A. Fersht,et al. Protein Folding and Unfolding at Atomic Resolution , 2002, Cell.
[77] R. Kopito,et al. Aggresomes, inclusion bodies and protein aggregation. , 2000, Trends in cell biology.
[78] C. Isidoro,et al. Autophagy‐dependent cell survival and cell death in an autosomal dominant familial neurohypophyseal diabetes insipidus in vitro model , 2005, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.
[79] Jonathan W. Yewdell,et al. Rapid degradation of a large fraction of newly synthesized proteins by proteasomes , 2000, Nature.
[80] J. Teckman,et al. Mitochondrial autophagy and injury in the liver in α1-antitrypsin deficiency , 2004 .
[81] L. Bruijn,et al. Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1. , 1998, Science.
[82] C. Levinthal. Are there pathways for protein folding , 1968 .
[83] Mark C. Field,et al. ER-associated protein degradation is a common mechanism underpinning numerous monogenic diseases including Robinow syndrome. , 2005, Human molecular genetics.
[84] P. Stenson,et al. Human Gene Mutation Database (HGMD , 2003 .
[85] D. J. Naylor,et al. Proteome-wide Analysis of Chaperonin-Dependent Protein Folding in Escherichia coli , 2005, Cell.
[86] Andrew B West,et al. Molecular pathophysiology of Parkinson's disease. , 2005, Annual review of neuroscience.
[87] F. Hartl,et al. Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein , 2002, Science.
[88] M. Stefani. Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world. , 2004, Biochimica et biophysica acta.
[89] Sergio Cocozza,et al. Spastic Paraplegia and OXPHOS Impairment Caused by Mutations in Paraplegin, a Nuclear-Encoded Mitochondrial Metalloprotease , 1998, Cell.
[90] D. Rudnick,et al. CONCISE REVIEW IN MECHANISMS OF DISEASE Alpha-1-Antitrypsin Deficiency: A New Paradigm for Hepatocellular Carcinoma in Genetic Liver Disease , 2005 .
[91] J. Jameson,et al. A murine model of autosomal dominant neurohypophyseal diabetes insipidus reveals progressive loss of vasopressin-producing neurons. , 2003, Journal of Clinical Investigation.
[92] K. Tanaka,et al. Intramitochondrial folding and assembly of medium-chain acyl-CoA dehydrogenase (MCAD). Demonstration of impaired transfer of K304E-variant MCAD from its complex with hsp60 to the native tetramer. , 1994, Journal of Biological Chemistry.
[93] M. Beal,et al. Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury , 1996, Nature Genetics.
[94] L. Bolund,et al. Effects of Two Mutations Detected in Medium Chain Acyl-CoA Dehydrogenase (MCAD)-deficient Patients on Folding, Oligomer Assembly, and Stability of MCAD Enzyme (*) , 1995, The Journal of Biological Chemistry.
[95] P. Waters. How PAH gene mutations cause hyper‐phenylalaninemia and why mechanism matters: Insights from in vitro expression , 2003, Human mutation.
[96] Carl W. Cotman,et al. Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis , 2003, Science.
[97] K. Davies,et al. Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease. , 2004, The international journal of biochemistry & cell biology.
[98] P. Lansbury,et al. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. , 2003, Annual review of neuroscience.
[99] R. Kopito,et al. Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins. , 1994, The Journal of biological chemistry.
[100] Peter Bross,et al. Genetic defects in fatty acid beta-oxidation and acyl-CoA dehydrogenases. Molecular pathogenesis and genotype-phenotype relationships. , 2004, European journal of biochemistry.
[101] Judith Frydman,et al. Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets. , 2004, Trends in cell biology.
[102] A. Tamura,et al. Formation of morphologically similar globular aggregates from diverse aggregation-prone proteins in mammalian cells. , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[103] T. Langer,et al. Protein degradation in mitochondria. , 2000, Seminars in cell & developmental biology.
[104] L. Bolund,et al. Differential cellular handling of defective arginine vasopressin (AVP) prohormones in cells expressing mutations of the AVP gene associated with autosomal dominant and recessive familial neurohypophyseal diabetes insipidus. , 2004, The Journal of clinical endocrinology and metabolism.
[105] R. Dean,et al. Recent developments in the intracellular degradation of oxidized proteins. , 2002, Free radical biology & medicine.
[106] S. Henikoff,et al. Predicting the effects of amino acid substitutions on protein function. , 2006, Annual review of genomics and human genetics.
[107] D. Lomas,et al. α1-Antitrypsin deficiency • 4: Molecular pathophysiology , 2004, Thorax.
[108] C. Anfinsen. Principles that govern the folding of protein chains. , 1973, Science.