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Journal of Molecular Biology|January 12, 2002
Why are proteins so robust to site mutations?Darin M Taverna, Richard A GoldsteinMethods in Molecular Biology (Clifton, N.J.)|January 5, 2011
Technological issues and experimental design of gene association studiesJohanna K Distefano, Darin M TavernaJournal of Pharmacological and Toxicological Methods|November 16, 2020
Use of computed tomography to assess subcutaneous drug dispersion with recombinant human hyaluronidase PH20 in a swine modelRobert J Connor, Darin M Taverna, Karla Thrall, et al.Proteins|February 22, 2011
The evolution and evolutionary consequences of marginal thermostability in proteinsRichard A GoldsteinToxicologic Pathology|November 23, 2017
Skeletal Muscle Injury Biomarkers: Assay Qualification Efforts and Translation to the ClinicRichard A GoldsteinGenome Biology and Evolution|July 26, 2013
Population size dependence of fitness effect distribution and substitution rate probed by biophysical model of protein thermostabilityRichard A GoldsteinCurrent Opinion in Structural Biology|March 11, 2008
The structure of protein evolution and the evolution of protein structureRichard A GoldsteinOrigins of Life and Evolution of the Biosphere : the Journal of the International Society for the Study of the Origin of Life|September 15, 2006
Emergent robustness in competition between autocatalytic chemical networksRichard A GoldsteinProtein Science : a Publication of the Protein Society|September 4, 2007
Amino-acid interactions in psychrophiles, mesophiles, thermophiles, and hyperthermophiles: insights from the quasi-chemical approximationRichard A GoldsteinPageof 8