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"count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "A novel gene overexpressed in the prostate of castrated rats: hormonal regulation, relationship to apoptosis and to acquired prostatic cell androgen independence.", "journal": "Endocrinology", "date": "1999-10", "authors": "Bruyninx M, Hennuy B, Cornet A, Houssa P, Daukandt M, Reiter E, Poncin J, Closset J, Hennen G", "reference": { "type": "PubMed", "id": "10499539", "url": "https://pubmed.ncbi.nlm.nih.gov/10499539" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "Q6P9X9-1", "protein_name": "Prostate androgen-regulated mucin-like protein 1 homolog", "gene_name": "Parm1", "tax_name": "Rat" } ], "species": [ { "name": "Rattus norvegicus", "taxid": 10116, "evidence": [ { "database": "UniProtKB", "id": "Q6P9X9", "url": "https://www.uniprot.org/uniprotkb/Q6P9X9" } ], "common_name": "Rat", "glygen_name": "Rat", "reference_species": "Rattus norvegicus [10116]" } 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J.", "date": "1999", "authors": "St-Denis JF, Cabaniols JP, Cushman SW, Roche PA", "reference": { "type": "PubMed", "id": "10051443", "url": "https://pubmed.ncbi.nlm.nih.gov/10051443" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "O70377-1", "protein_name": "Synaptosomal-associated protein 23", "gene_name": "Snap23", "tax_name": "Rat" } ], "species": [ { "name": "Rattus norvegicus", "taxid": 10116, "evidence": [ { "database": "UniProtKB", "id": "O70377", "url": "https://www.uniprot.org/uniprotkb/O70377" } ], "common_name": "Rat", "glygen_name": "Rat", "reference_species": "Rattus norvegicus [10116]" } ], "record_id": "pubmed.10051443", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 1 } ], "sort_fields": [ "uniprot_canonical_ac", "protein_name", "gene_name", "tax_name" ] }, { "table_id": 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"O70377-1", "protein_name": "Synaptosomal-associated protein 23", "gene_name": "Snap23", "tax_name": "Rat" }, { "uniprot_canonical_ac": "P60881-1", "protein_name": "Synaptosomal-associated protein 25", "gene_name": "Snap25", "tax_name": "Rat" }, { "uniprot_canonical_ac": "P32851-1", "protein_name": "Syntaxin-1A", "gene_name": "Stx1a", "tax_name": "Rat" } ], "species": [ { "name": "Rattus norvegicus", "taxid": 10116, "evidence": [ { "database": "UniProtKB", "id": "O70377", "url": "https://www.uniprot.org/uniprotkb/O70377" } ], "common_name": "Rat", "glygen_name": "Rat", "reference_species": "Rattus norvegicus [10116]" } ], "record_id": "pubmed.37057886", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 3 } ], "sort_fields": [ "uniprot_canonical_ac", "protein_name", "gene_name", "tax_name" ] }, { "table_id": "referenced_glycans", 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"gene_name": "Pvalb", "tax_name": "Rat" } ], "species": [ { "name": "Rattus norvegicus", "taxid": 10116, "evidence": [ { "database": "UniProtKB", "id": "P02625", "url": "https://www.uniprot.org/uniprotkb/P02625" } ], "common_name": "Rat", "glygen_name": "Rat", "reference_species": "Rattus norvegicus [10116]" } ], "mutagenesis": [ { "start_pos": 1, "end_pos": 37, "sequence_org": "MSMTDLLSAEDIKKAIGAFTAADSFDHKKFFQMVGLK", "sequence_mut": "", "comment": "Deletion of both A and B helices results in loss of stable apo form, in lower Ca(+) ion-binding affinity compared to wild-type, and in inability to bind Mg(2+).", "evidence": [ { "database": "UniProtKB", "id": "P02625", "url": "https://www.uniprot.org/uniprotkb/P02625" }, { "database": "PubMed", "id": "11562941", "url": "https://pubmed.ncbi.nlm.nih.gov/11562941" } ], "uniprot_canonical_ac": "P02625-1" } ], "record_id": "pubmed.11562941", "abstract": "", "glycosylation": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": 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"field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_automatic_literature_mining", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "Crystal structure of rat alpha-parvalbumin at 1.05 Angstrom resolution.", "journal": "Protein science : a publication of the Protein Society", "date": "2004-07", "authors": "Bottoms Christopher A, Schuermann Jonathan P, Agah Sayeh, Henzl Michael T, Tanner John J", "reference": { "type": "PubMed", "id": "15169955", "url": "https://pubmed.ncbi.nlm.nih.gov/15169955" }, 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"field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_predicted", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_automatic_literature_mining", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "Crystal structure of a high-affinity variant of rat alpha-parvalbumin.", "journal": "Biochemistry", "date": "2004-08-10", "authors": "Lee Yong-Hwan, Tanner John J, Larson John D, Henzl Michael T", "reference": { "type": "PubMed", "id": "15287728", "url": "https://pubmed.ncbi.nlm.nih.gov/15287728" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P02625-1", "protein_name": "Parvalbumin alpha", "gene_name": "Pvalb", "tax_name": "Rat" } ], "species": [ { "name": "Rattus norvegicus", "taxid": 10116, "evidence": [ { "database": "UniProtKB", "id": "P02625", "url": "https://www.uniprot.org/uniprotkb/P02625" } ], "common_name": "Rat", "glygen_name": "Rat", "reference_species": "Rattus norvegicus [10116]" } ], "mutagenesis": [ { "start_pos": 56, "end_pos": 56, "sequence_org": "S", "sequence_mut": "D", "comment": "Increased Ca(2+)-binding affinity in the EF-hand 1 domain probably due to the orientation of mutant D-60 side chain, which is predicted to stabilize helix D; when associated with D-60. Behaves as wild-type with identical Na(+)-binding stoichiometry and increased Ca(2+) and Mg(2+) ion-binding affinity in K(+)-containing solution; when associated with D-60.", "evidence": [ { "database": "UniProtKB", "id": "P02625", "url": "https://www.uniprot.org/uniprotkb/P02625" }, { "database": "PubMed", "id": "15287728", "url": "https://pubmed.ncbi.nlm.nih.gov/15287728" } ], "uniprot_canonical_ac": "P02625-1" }, { "start_pos": 60, "end_pos": 60, "sequence_org": "E", "sequence_mut": "D", "comment": "Increased Ca(2+)-binding affinity in the EF-hand 1 domain probably due to the orientation of mutant D-60 side chain, which is predicted to stabilize helix D; when associated with D-56. Behaves as wild-type with identical Na(+)-binding stoichiometry and increased Ca(2+) and Mg(2+) ion-binding affinity in K(+)-containing solution; when associated with D-56.", "evidence": [ { "database": "UniProtKB", "id": "P02625", "url": "https://www.uniprot.org/uniprotkb/P02625" }, { "database": "PubMed", "id": "15287728", "url": "https://pubmed.ncbi.nlm.nih.gov/15287728" } ], "uniprot_canonical_ac": "P02625-1" } ], "record_id": "pubmed.15287728", "abstract": "", "glycosylation": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 1 } ], "sort_fields": [ "uniprot_canonical_ac", "protein_name", "gene_name", "tax_name" ] }, { "table_id": "referenced_glycans", "table_stats": [ { "field": "total", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "phosphorylation", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_reported", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_reported_with_glycan", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_predicted", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_automatic_literature_mining", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "Crystal structure of the D94S/G98E variant of rat alpha-parvalbumin. An explanation for the reduced divalent ion affinity.", "journal": "Biochemistry", "date": "2005-08-23", "authors": "Tanner John J, Agah Sayeh, Lee Yong-Hwan, Henzl Michael T", "reference": { "type": "PubMed", "id": "16101280", "url": "https://pubmed.ncbi.nlm.nih.gov/16101280" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P02625-1", "protein_name": "Parvalbumin alpha", "gene_name": "Pvalb", "tax_name": "Rat" } ], "species": [ { "name": "Rattus norvegicus", "taxid": 10116, "evidence": [ { "database": "UniProtKB", "id": "P02625", "url": "https://www.uniprot.org/uniprotkb/P02625" } ], "common_name": "Rat", "glygen_name": "Rat", "reference_species": "Rattus norvegicus [10116]" } ], "mutagenesis": [ { "start_pos": 95, "end_pos": 95, "sequence_org": "D", "sequence_mut": "S", "comment": "Reduced Ca(2+)-binding affinity in the EF-hand 2 domain due to a substantial enthalpic penalty, the source of which may be steric interference between F-58 and C alpha atom of mutant E-99; when associated with E-99. No effect on the Ca(2+) or Mg(2+) ion-binding properties in either Na(+)- or K(+)-containing buffers indicating that the reduced affinity for divalent ions is not a result of heightened monovalent ion competition; when associated with E-99.", "evidence": [ { "database": "UniProtKB", "id": "P02625", "url": "https://www.uniprot.org/uniprotkb/P02625" }, { "database": "PubMed", "id": "16101280", "url": "https://pubmed.ncbi.nlm.nih.gov/16101280" } ], "uniprot_canonical_ac": "P02625-1" }, { "start_pos": 99, "end_pos": 99, "sequence_org": "G", "sequence_mut": "E", "comment": "Reduced Ca(2+)-binding affinity in the EF-hand 2 domain due to a substantial enthalpic penalty, the source of which may be steric interference between F-58 and C alpha atom of mutant E-99; when associated with S-95. No effect on the Ca(2+) or Mg(2+) ion-binding properties in either Na(+)- or K(+)-containing buffers indicating that the reduced affinity for divalent ions is not a result of heightened monovalent ion competition; when associated with S-95.", "evidence": [ { "database": "UniProtKB", "id": "P02625", "url": "https://www.uniprot.org/uniprotkb/P02625" }, { "database": "PubMed", "id": "16101280", "url": "https://pubmed.ncbi.nlm.nih.gov/16101280" } ], "uniprot_canonical_ac": "P02625-1" } ], "record_id": "pubmed.16101280", "abstract": "", "glycosylation": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 1 } ], "sort_fields": [ "uniprot_canonical_ac", "protein_name", "gene_name", "tax_name" ] }, { "table_id": "referenced_glycans", "table_stats": [ { "field": "total", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation", "table_stats": [ { "field": "total", "count": 0 }, { 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Section D, Biological crystallography", "date": "2009-08", "authors": "Hoh Fran\u00e7ois, Cav\u00e9 Adrien, Strub Marie Paule, Ban\u00e8res Jean Louis, Padilla Andr\u00e9", "reference": { "type": "PubMed", "id": "19622856", "url": "https://pubmed.ncbi.nlm.nih.gov/19622856" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P02625-1", "protein_name": "Parvalbumin alpha", "gene_name": "Pvalb", "tax_name": "Rat" } ], "species": [ { "name": "Rattus norvegicus", "taxid": 10116, "evidence": [ { "database": "UniProtKB", "id": "P02625", "url": "https://www.uniprot.org/uniprotkb/P02625" } ], "common_name": "Rat", "glygen_name": "Rat", "reference_species": "Rattus norvegicus [10116]" } ], "mutagenesis": [ { "start_pos": 76, "end_pos": 76, "sequence_org": "R", "sequence_mut": "A", "comment": "Loss of salt bridge formation with E-81. No effect in the overall structure of the protein. However, more solvent-exposed AB loop, which consists of two antiparallel helices A and B, and higher flexibility of the AB loop compared to the wild-type structure. Lower thermal stability of the calcium-loaded form of the protein than that of the wild-type, but melting temperature (Tm) value still remains quite high. Unfolded apo form at room temperature. Weaker calcium- and, to a lesser extent, magnesium-binding affinities compared to the wild-type.", "evidence": [ { "database": "UniProtKB", "id": "P02625", "url": "https://www.uniprot.org/uniprotkb/P02625" }, { "database": "PubMed", "id": "19622856", "url": "https://pubmed.ncbi.nlm.nih.gov/19622856" } ], "uniprot_canonical_ac": "P02625-1" } ], "record_id": "pubmed.19622856", "abstract": "", "glycosylation": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 1 } ], "sort_fields": [ "uniprot_canonical_ac", "protein_name", "gene_name", "tax_name" ] }, { "table_id": "referenced_glycans", "table_stats": [ { "field": "total", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": 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"field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "Chronic Stress Exposure Reduces Parvalbumin Expression in the Rat Hippocampus through an Imbalance of Redox Mechanisms: Restorative Effect of the Antipsychotic Lurasidone.", "journal": "The international journal of neuropsychopharmacology", "date": "2018", "authors": "Rossetti AC, Paladini MS, Colombo M, Gruca P, Lason-Tyburkiewicz M, Tota-Glowczyk K, Papp M, Riva MA, Molteni R", "reference": { "type": "PubMed", "id": "29788232", "url": "https://pubmed.ncbi.nlm.nih.gov/29788232" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P02625-1", "protein_name": "Parvalbumin alpha", "gene_name": "Pvalb", "tax_name": "Rat" } ], "species": [ { "name": "Rattus norvegicus", "taxid": 10116, "evidence": [ { "database": "UniProtKB", "id": "P02625", "url": "https://www.uniprot.org/uniprotkb/P02625" } ], "common_name": "Rat", "glygen_name": "Rat", 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Biol. Chem.", "date": "1986", "authors": "Epstein P, Means A R, Berchtold M W", "reference": { "type": "PubMed", "id": "3009434", "url": "https://pubmed.ncbi.nlm.nih.gov/3009434" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P02625-1", "protein_name": "Parvalbumin alpha", "gene_name": "Pvalb", "tax_name": "Rat" } ], "species": [ { "name": "Rattus norvegicus", "taxid": 10116, "evidence": [ { "database": "UniProtKB", "id": "P02625", "url": "https://www.uniprot.org/uniprotkb/P02625" } ], "common_name": "Rat", "glygen_name": "Rat", "reference_species": "Rattus norvegicus [10116]" } ], "record_id": "pubmed.3009434", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 1 } ], "sort_fields": [ "uniprot_canonical_ac", "protein_name", "gene_name", "tax_name" ] }, { "table_id": "referenced_glycans", "table_stats": 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"table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "Comprehensive analysis of the roles of 'black' and 'gray' clusters in structure and function of rat beta-parvalbumin.", "journal": "Cell calcium", "date": "2018", "authors": "Permyakov SE, Vologzhannikova AA, Khorn PA, Shevelyova MP, Kazakov AS, Emelyanenko VI, Denesyuk AI, Denessiouk K, Uversky VN, Permyakov EA", "reference": { "type": "PubMed", "id": "30176502", "url": "https://pubmed.ncbi.nlm.nih.gov/30176502" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P02625-1", "protein_name": "Parvalbumin alpha", "gene_name": "Pvalb", "tax_name": "Rat" } ], 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Identity of the zinc-binding protein with rat parathymosin.", "journal": "FEBS Lett.", "date": "1989", "authors": "Trompeter HI, Brand IA, Soling HD", "reference": { "type": "PubMed", "id": "2759245", "url": "https://pubmed.ncbi.nlm.nih.gov/2759245" }, "referenced_glycans": [], "referenced_proteins": [ { "uniprot_canonical_ac": "P04550-1", "protein_name": "Parathymosin", "gene_name": "Ptms", "tax_name": "Rat" } ], "species": [ { "name": "Rattus norvegicus", "taxid": 10116, "evidence": [ { "database": "UniProtKB", "id": "P04550", "url": "https://www.uniprot.org/uniprotkb/P04550" } ], "common_name": "Rat", "glygen_name": "Rat", "reference_species": "Rattus norvegicus [10116]" } ], "record_id": "pubmed.2759245", "abstract": "", "glycosylation": [], "mutagenesis": [], "snv": [], "phosphorylation": [], "glycation": [], "section_stats": [ { "table_id": "referenced_proteins", "table_stats": [ { "field": "total", "count": 1 } ], "sort_fields": [ "uniprot_canonical_ac", "protein_name", "gene_name", "tax_name" ] }, { "table_id": "referenced_glycans", "table_stats": [ { "field": "total", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "phosphorylation", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_reported", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_reported_with_glycan", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_predicted", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_automatic_literature_mining", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_sites", "count": 0 }, { "field": "o_linked_sites", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "o_linked_glycans", "count": 0 } ], "sort_fields": [] } ] }, { "title": "Bovine parathymosin: amino acid sequence and comparison with rat parathymosin.", "journal": "Biochem. 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