M
Melanie R. Nelson
Researcher at Scripps Research Institute
Publications - 15
Citations - 4133
Melanie R. Nelson is an academic researcher from Scripps Research Institute. The author has contributed to research in topics: CellML & Calmodulin. The author has an hindex of 12, co-authored 15 publications receiving 3934 citations. Previous affiliations of Melanie R. Nelson include Science Applications International Corporation & Princeton University.
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Journal ArticleDOI
The systems biology markup language (SBML): a medium for representation and exchange of biochemical network models.
Michael Hucka,Andrew Finney,Herbert M. Sauro,Hamid Bolouri,Hamid Bolouri,John Doyle,Hiroaki Kitano,Adam P. Arkin,Benjamin Bornstein,Dennis Bray,Athel Cornish-Bowden,Autumn A. Cuellar,S. Dronov,E. D. Gilles,Martin Ginkel,V. Gor,Igor Goryanin,W. J. Hedley,T. C. Hodgman,J.-H.S. Hofmeyr,Peter Hunter,Nick Juty,J. L. Kasberger,Andreas Kremling,Ursula Kummer,N Le Novère,Leslie M. Loew,D. Lucio,Pedro Mendes,E. Minch,Eric Mjolsness,Yoichi Nakayama,Melanie R. Nelson,Poul M. F. Nielsen,T. Sakurada,James C. Schaff,Bruce E. Shapiro,Thomas S. Shimizu,H. D. Spence,Jörg Stelling,Koichi Takahashi,Masaru Tomita,John Wagner,J. Wang +43 more
TL;DR: This work summarizes the Systems Biology Markup Language (SBML) Level 1, a free, open, XML-based format for representing biochemical reaction networks, a software-independent language for describing models common to research in many areas of computational biology.
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Structures of EF-hand Ca(2+)-binding proteins: diversity in the organization, packing and response to Ca2+ binding.
TL;DR: The classical picture of calcium sensors and calcium signal modulators is presented, along with variants on the basic theme and new structural paradigms.
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An interaction‐based analysis of calcium‐induced conformational changes in Ca2+ sensor proteins
TL;DR: Insight is provided into the structural basis for these changes and into the differential response to calcium binding of various members of the EF‐hand calcium‐binding protein family, including a new hypothesis that critical hydrophobic interactions stabilize the open conformation in Ca2+ sensors, but are absent in “non‐sensor” proteins that remain closed upon Ca2-binding.
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Incorporating Protein Environments in Density Functional Theory: A Self-Consistent Reaction Field Calculation of Redox Potentials of [2Fe2S] Clusters in Ferredoxin and Phthalate Dioxygenase Reductase
TL;DR: In this paper, an approach to calculate molecular electronic structures of active-site clusters in the presence of protein environments has been developed, where the active site cluster is treated by density functional theory.
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A short introduction to CellML
TL;DR: CellML as mentioned in this paper is an XML-based language designed to facilitate the exchange of biological models across the World Wide Web, which is used to describe models as a collection of discrete components linked by connections to form a network.