Arcus VL - Search Results

1

Change in heat capacity for enzyme catalysis determines temperature dependence of enzyme catalyzed rates.

Hobbs JK, Jiao W, Easter AD, Parker EJ, Schipper LA, Arcus VL. Hobbs JK, et al. Among authors: arcus vl. ACS Chem Biol. 2013 Nov 15;8(11):2388-93. doi: 10.1021/cb4005029. Epub 2013 Sep 17. ACS Chem Biol. 2013. PMID: 24015933

2

On the origin and evolution of thermophily: reconstruction of functional precambrian enzymes from ancestors of Bacillus.

Hobbs JK, Shepherd C, Saul DJ, Demetras NJ, Haaning S, Monk CR, Daniel RM, Arcus VL. Hobbs JK, et al. Among authors: arcus vl. Mol Biol Evol. 2012 Feb;29(2):825-35. doi: 10.1093/molbev/msr253. Epub 2011 Oct 13. Mol Biol Evol. 2012. PMID: 21998276

3

Thermodynamic theory explains the temperature optima of soil microbial processes and high Q10 values at low temperatures.

Schipper LA, Hobbs JK, Rutledge S, Arcus VL. Schipper LA, et al. Among authors: arcus vl. Glob Chang Biol. 2014 Nov;20(11):3578-86. doi: 10.1111/gcb.12596. Epub 2014 May 26. Glob Chang Biol. 2014. PMID: 24706438 Free article.

4

Toward more accurate ancestral protein genotype-phenotype reconstructions with the use of species tree-aware gene trees.

Groussin M, Hobbs JK, Szöllősi GJ, Gribaldo S, Arcus VL, Gouy M. Groussin M, et al. Among authors: arcus vl. Mol Biol Evol. 2015 Jan;32(1):13-22. doi: 10.1093/molbev/msu305. Epub 2014 Nov 4. Mol Biol Evol. 2015. PMID: 25371435 Free PMC article.

5

Change in heat capacity accurately predicts vibrational coupling in enzyme catalyzed reactions.

Arcus VL, Pudney CR. Arcus VL, et al. FEBS Lett. 2015 Aug 4;589(17):2200-6. doi: 10.1016/j.febslet.2015.06.042. Epub 2015 Jul 11. FEBS Lett. 2015. PMID: 26172507 Free article.

6

Reconstructed Ancestral Enzymes Impose a Fitness Cost upon Modern Bacteria Despite Exhibiting Favourable Biochemical Properties.

Hobbs JK, Prentice EJ, Groussin M, Arcus VL. Hobbs JK, et al. Among authors: arcus vl. J Mol Evol. 2015 Oct;81(3-4):110-20. doi: 10.1007/s00239-015-9697-5. Epub 2015 Sep 9. J Mol Evol. 2015. PMID: 26349578

7

On the Temperature Dependence of Enzyme-Catalyzed Rates.

Arcus VL, Prentice EJ, Hobbs JK, Mulholland AJ, Van der Kamp MW, Pudney CR, Parker EJ, Schipper LA. Arcus VL, et al. Biochemistry. 2016 Mar 29;55(12):1681-8. doi: 10.1021/acs.biochem.5b01094. Epub 2016 Mar 8. Biochemistry. 2016. PMID: 26881922

8

Interdomain Conformational Changes Provide Allosteric Regulation en Route to Chorismate.

Nazmi AR, Lang EJM, Bai Y, Allison TM, Othman MH, Panjikar S, Arcus VL, Parker EJ. Nazmi AR, et al. Among authors: arcus vl. J Biol Chem. 2016 Oct 14;291(42):21836-21847. doi: 10.1074/jbc.M116.741637. Epub 2016 Aug 8. J Biol Chem. 2016. PMID: 27502275 Free PMC article.

9

Heat Capacity Changes for Transition-State Analogue Binding and Catalysis with Human 5'-Methylthioadenosine Phosphorylase.

Firestone RS, Cameron SA, Karp JM, Arcus VL, Schramm VL. Firestone RS, et al. Among authors: arcus vl. ACS Chem Biol. 2017 Feb 17;12(2):464-473. doi: 10.1021/acschembio.6b00885. Epub 2016 Dec 27. ACS Chem Biol. 2017. PMID: 28026167 Free PMC article.

10

Change in Heat Capacity for Enzyme Catalysis Determines Temperature Dependence of Enzyme Catalyzed Rates.

Hobbs JK, Jiao W, Easter AD, Parker EJ, Schipper LA, Arcus VL. Hobbs JK, et al. Among authors: arcus vl. ACS Chem Biol. 2017 Mar 17;12(3):868. doi: 10.1021/acschembio.7b00065. Epub 2017 Feb 21. ACS Chem Biol. 2017. PMID: 28221017 No abstract available.

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