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المؤلفون: Signorino G (1), Covaceuszach S (2), Bozzi M (1), (3), Hübner W (4), Mönkemöller V (4), Konarev PV (5), Cassetta A (2), Brancaccio A (3), (6), Sciandra F (3).
المصدر: Human mutation 39 (2018): 266–280.
info:cnr-pdr/source/autori:Signorino G (1), Covaceuszach S (2), Bozzi M (1),(3), Hübner W (4), Mönkemöller V (4), Konarev PV (5), Cassetta A (2), Brancaccio A (3),(6), Sciandra F (3)./titolo:A dystroglycan mutation (p.Cys66uPhe) associated to muscle-eye-brain disease with multicystic leukodystrophy results in ER-retention of the mutant protein/doi:/rivista:Human mutation/anno:2018/pagina_da:266/pagina_a:280/intervallo_pagine:266–280/volume:39مصطلحات موضوعية: SAXS, confocal microscopy, dystroglycan, dystroglycanopathy, endoplasmic-reticulum retention, multicystic leukodystrophy, site-directed mutagenesis, super resolution microscopy
URL الوصول: https://explore.openaire.eu/search/publication?articleId=cnr_________::adbed9846b9650783ff2d45322dc2d02
http://www.cnr.it/prodotto/i/390142 -
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المؤلفون: Gioia M (1, Fasciglione GF (1, Sbardella D (1, Sciandra F (3), Casella M (4), Camerini S (4), Crescenzi M (4), Gori A (5), Tarantino U (1), Cozza P (1), Brancaccio A (3, Coletta M (1, Bozzi M (3, 7).
المصدر: Gioia, M, Fasciglione, G F, Sbardella, D, Sciandra, F, Casella, M, Camerini, S, Crescenzi, M, Gori, A, Tarantino, U, Cozza, P, Brancaccio, A, Coletta, M & Bozzi, M 2018, ' The enzymatic processing of α-dystroglycan by MMP-2 is controlled by two anchoring sites distinct from the active site ', PLoS ONE, vol. 13, no. 2, pp. e0192651 . https://doi.org/10.1371/journal.pone.0192651
PloS one 15 (2018).
info:cnr-pdr/source/autori:Gioia M (1,2), Fasciglione GF (1,2), Sbardella D (1,2), Sciandra F (3), Casella M (4), Camerini S (4), Crescenzi M (4), Gori A (5), Tarantino U (1), Cozza P (1), Brancaccio A (3,6), Coletta M (1,2), Bozzi M (3,7)./titolo:The enzymatic processing of ?-dystroglycan by MMP-2 is controller by two anchoring sites distinct from the active site/doi:/rivista:PloS one/anno:2018/pagina_da:/pagina_a:/intervallo_pagine:/volume:15
PLoS ONE
PLoS ONE, Vol 13, Iss 2, p e0192651 (2018)
PloS one 13 (2018). doi:10.1371/journal.pone.0192651
info:cnr-pdr/source/autori:Gioia M.; Fasciglione G.F.; Sbardella D.; Sciandra F.; Casella M.; Camerini S.; Crescenzi M.; Gori A.; Tarantino U.; Cozza P.; Brancaccio A.; Coletta M.; Bozzi M./titolo:The enzymatic processing of ?-dystroglycan by MMP-2 is controlled by two anchoring sites distinct from the active site/doi:10.1371%2Fjournal.pone.0192651/rivista:PloS one/anno:2018/pagina_da:/pagina_a:/intervallo_pagine:/volume:13مصطلحات موضوعية: Metabolic Processes, 0301 basic medicine, Reversed-Phase High Performance Liquid Chromatography, lcsh:Medicine, Sequence Homology, Peptide, Protein Sequencing, Matrix metalloproteinase, Biochemistry, Database and Informatics Methods, Mice, 0302 clinical medicine, Tandem Mass Spectrometry, Catalytic Domain, Enzyme Inhibitors, lcsh:Science, Dystroglycans, Peptide sequence, Liquid Chromatography, chemistry.chemical_classification, Extracellular Matrix Proteins, Multidisciplinary, MMP-2, biology, medicine.diagnostic_test, Settore BIO/11, Chromatographic Techniques, Recombinant Proteins, Enzymes, Extracellular Matrix, Amino Acid, ?-dystroglycan (?-DG) and ?-dystroglycan (? -DG), ?-DG, 030220 oncology & carcinogenesis, Matrix Metalloproteinase 2, Thermodynamics, Cellular Structures and Organelles, Sequence Analysis, Research Article, Bioinformatics, Proteolysis, Sequence Databases, Research and Analysis Methods, allosteric inhibition, dystroglycan, 03 medical and health sciences, Amino Acid Sequence, Animals, Humans, Kinetics, Sequence Homology, Amino Acid, medicine, Dystroglycan, Extracellular, Settore BIO/10, Binding site, Molecular Biology Techniques, Sequencing Techniques, Molecular Biology, Settore BIO/10 - BIOCHIMICA, lcsh:R, Biology and Life Sciences, Proteins, Active site, Cell Biology, Reversed Phase Chromatography, High Performance Liquid Chromatography, Metabolism, Biological Databases, 030104 developmental biology, chemistry, Enzymology, biology.protein, Biophysics, lcsh:Q
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