Steven R. Van Doren

University of Missouri - Columbia, Columbia, MO, United States 
"Steven Van Doren"
Mean distance: 9953.25
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Prior SH, Byrne TS, Tokmina-Roszyk D, et al. (2016) Path to Collagenolysis: Collagen V Triple-Helix Model Bound Productively and in Encounters by Matrix Metalloproteinase-12. The Journal of Biological Chemistry
Prior SH, Fulcher YG, Koppisetti RK, et al. (2015) Charge-Triggered Membrane Insertion of Matrix Metalloproteinase-7, Supporter of Innate Immunity and Tumors. Structure (London, England : 1993). 23: 2099-110
Zhao Y, Marcink TC, Sanganna Gari RR, et al. (2015) Transient collagen triple helix binding to a key metalloproteinase in invasion and development. Structure (London, England : 1993). 23: 257-69
Xu J, Lee Y, Beamer LJ, et al. (2015) Phosphorylation in the catalytic cleft stabilizes and attracts domains of a phosphohexomutase. Biophysical Journal. 108: 325-37
Van Doren SR. (2015) Matrix metalloproteinase interactions with collagen and elastin. Matrix Biology : Journal of the International Society For Matrix Biology. 44: 224-31
Koppisetti RK, Fulcher YG, Jurkevich A, et al. (2014) Ambidextrous binding of cell and membrane bilayers by soluble matrix metalloproteinase-12. Nature Communications. 5: 5552
Fulcher YG, Sanganna Gari RR, Frey NC, et al. (2014) Heparinoids activate a protease, secreted by mucosa and tumors, via tethering supplemented by allostery. Acs Chemical Biology. 9: 957-66
Lauer JL, Bhowmick M, Tokmina-Roszyk D, et al. (2014) The role of collagen charge clusters in the modulation of matrix metalloproteinase activity. The Journal of Biological Chemistry. 289: 1981-92
Wei Y, Marcink TC, Xu J, et al. (2014) Chemical shift assignments of domain 4 from the phosphohexomutase from Pseudomonas aeruginosa suggest that freeing perturbs its coevolved domain interface. Biomolecular Nmr Assignments. 8: 329-33
Sarma AV, Anbanandam A, Kelm A, et al. (2012) Solution NMR of a 463-residue phosphohexomutase: domain 4 mobility, substates, and phosphoryl transfer defect. Biochemistry. 51: 807-19
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