{"entity": "publications", "timestamp": "2026-04-20T02:58:40.909Z", "year": "2004", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publications/2004.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publications/2004"}}, "publications_count": 3, "full": true, "publications": [{"entity": "publication", "iuid": "1e69aba3685f454aa3bb7318c630812c", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/1e69aba3685f454aa3bb7318c630812c.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/1e69aba3685f454aa3bb7318c630812c"}}, "title": "Birth and adaptive evolution of a hominoid gene that supports high neurotransmitter flux.", "authors": [{"family": "Burki", "given": "Fabien", "initials": "F"}, {"family": "Kaessmann", "given": "Henrik", "initials": "H"}], "type": "journal article", "published": "2004-10-00", "journal": {"title": "Nat Genet", "issn": "1061-4036", "volume": "36", "issue": "10", "pages": "1061-1063", "issn-l": "1061-4036"}, "abstract": "The enzyme glutamate dehydrogenase (GDH) is important for recycling the chief excitatory neurotransmitter, glutamate, during neurotransmission. Human GDH exists in housekeeping and brain-specific isotypes encoded by the genes GLUD1 and GLUD2, respectively. Here we show that GLUD2 originated by retroposition from GLUD1 in the hominoid ancestor less than 23 million years ago. The amino acid changes responsible for the unique brain-specific properties of the enzyme derived from GLUD2 occurred during a period of positive selection after the duplication event.", "doi": "10.1038/ng1431", "pmid": "15378063", "labels": {"Fabien Burki": null, "SciLifeLab Fellow": null}, "xrefs": [{"db": "pii", "key": "ng1431"}], "notes": [], "created": "2020-09-28T12:17:41.209Z", "modified": "2022-11-07T11:31:56.981Z"}, {"entity": "publication", "iuid": "03204982ceb446069e254857db28ea9e", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/03204982ceb446069e254857db28ea9e.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/03204982ceb446069e254857db28ea9e"}}, "title": "Proton binding to proteins: pK(a) calculations with explicit and implicit solvent models.", "authors": [{"family": "Simonson", "given": "Thomas", "initials": "T"}, {"family": "Carlsson", "given": "Jens", "initials": "J"}, {"family": "Case", "given": "David A", "initials": "DA"}], "type": "journal article", "published": "2004-04-07", "journal": {"title": "J. Am. Chem. Soc.", "issn": "0002-7863", "volume": "126", "issue": "13", "pages": "4167-4180", "issn-l": null}, "abstract": "Ionizable residues play important roles in protein structure and activity, and proton binding is a valuable reporter of electrostatic interactions in these systems. We use molecular dynamics free energy simulations (MDFE) to compute proton pKa shifts, relative to a model compound in solution, for three aspartate side chains in two proteins. Simulations with explicit solvent and with an implicit, dielectric continuum solvent are reported. The implicit solvent simulations use the generalized Born (GB) model, which provides an approximate, analytical solution to Poisson's equation. With explicit solvent, the direction of the pKa shifts is correct in all three cases with one force field (AMBER) and in two out of three cases with another (CHARMM). For two aspartates, the dielectric response to ionization is found to be linear, even though the separate protein and solvent responses can be nonlinear. For thioredoxin Asp26, nonlinearity arises from the presence of two substates that correspond to the two possible orientations of the protonated carboxylate. For this side chain, which is partly buried and has a large pKa upshift, very long simulations are needed to correctly sample several slow degrees of freedom that reorganize in response to the ionization. Thus, nearby Lys57 rotates to form a salt bridge and becomes buried, while three waters intercalate along the opposite edge of Asp26. Such strong and anisotropic reorganization is very difficult to predict with Poisson-Boltzmann methods that only consider electrostatic interactions and employ a single protein structure. In contrast, MDFE with a GB dielectric continuum solvent, used for the first time for pKa calculations, can describe protein reorganization accurately and gives encouraging agreement with experiment and with the explicit solvent simulations.", "doi": "10.1021/ja039788m", "pmid": "15053606", "labels": {"Jens Carlsson": null, "SciLifeLab Fellow": null}, "xrefs": [], "notes": [], "created": "2020-09-29T13:52:57.378Z", "modified": "2022-11-07T11:33:17.833Z"}, {"entity": "publication", "iuid": "31ea995fbcb4484faffde8700c8b629f", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/31ea995fbcb4484faffde8700c8b629f.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/31ea995fbcb4484faffde8700c8b629f"}}, "title": "Capacity ofSalvinia minima Baker to Tolerate and Accumulate As and Pb", "authors": [{"family": "Hoffmann", "given": "T", "initials": "T"}, {"family": "Kutter", "given": "C", "initials": "C"}, {"family": "Santamar\u00eda", "given": "J", "initials": "J"}], "type": "journal-article", "published": "2004-02-05", "journal": {"title": "Eng. Life Sci.", "issn": "1618-0240", "volume": "4", "issue": "1", "pages": "61-65", "issn-l": null}, "abstract": null, "doi": "10.1002/elsc.200400008", "pmid": null, "labels": {"Claudia Kutter": null, "SciLifeLab Fellow": null}, "xrefs": [], "notes": [], "created": "2020-09-25T14:39:42.266Z", "modified": "2022-11-07T11:30:38.652Z"}]}