Darrell Cockburn Pennsylvania State University
1 protocol

Nicole Koropatkin
  • Department of Microbiology and Immunology, University of Michigan Medical School, USA
  • 1 Author merit

Education

Ph.D. in Biochemistry / Crystallography, University of Wisconsin, Madison, WI, 2014

Current position

Assistant Professor, Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, MI (2014 – present)

Publications

  1. Cockburn, D. W., Orlovsky, N. I., Foley, M. H., Kwiatkowski, K. J., Bahr, C. M., Maynard, M., Demeler, B. and Koropatkin, N. M. (2015). Molecular details of a starch utilization pathway in the human gut symbiont Eubacterium rectale. Mol Microbiol 95(2): 209-230.
  2. Karunatilaka, K. S., Cameron, E. A., Martens, E. C., Koropatkin, N. M. and Biteen, J. S. (2014). Superresolution imaging captures carbohydrate utilization dynamics in human gut symbionts. MBio 5(6): e02172.
  3. Larsbrink, J., Rogers, T. E., Hemsworth, G. R., McKee, L. S., Tauzin, A. S., Spadiut, O., Klinter, S., Pudlo, N. A., Urs, K., Koropatkin, N. M., Creagh, A. L., Haynes, C. A., Kelly, A. G., Cederholm, S. N., Davies, G. J., Martens, E. C. and Brumer, H. (2014). A discrete genetic locus confers xyloglucan metabolism in select human gut Bacteroidetes. Nature 506(7489): 498-502.
  4. Rogers, T. E., Pudlo, N. A., Koropatkin, N. M., Bell, J. S., Moya Balasch, M., Jasker, K. and Martens, E. C. (2013). Dynamic responses of Bacteroides thetaiotaomicron during growth on glycan mixtures. Mol Microbiol 88(5): 876-890.
  5. Bolam, D. N. and Koropatkin, N. M. (2012). Glycan recognition by the Bacteroidetes Sus-like systems. Curr Opin Struct Biol 22(5): 563-569.
  6. Cameron, E. A., Maynard, M. A., Smith, C. J., Smith, T. J., Koropatkin, N. M. and Martens, E. C. (2012). Multidomain Carbohydrate-binding Proteins Involved in Bacteroides thetaiotaomicron Starch Metabolism. J Biol Chem 287(41): 34614-34625.
  7. Koropatkin, N. M., Cameron, E. A. and Martens, E. C. (2012). How glycan metabolism shapes the human gut microbiota. Nat Rev Microbiol 10(5): 323-335.
  8. Morgan, S. J., Felek, S., Gadwal, S., Koropatkin, N. M., Perry, J. W., Bryson, A. B. and Krukonis, E. S. (2011). The two faces of ToxR: activator of ompU, co-regulator of toxT in Vibrio cholerae. Mol Microbiol 81(1): 113-128.
  9. Koropatkin, N. M. and Smith, T. J. (2010). SusG: a unique cell-membrane-associated alpha-amylase from a prominent human gut symbiont targets complex starch molecules. Structure 18(2): 200-215.
  10. Koropatkin, N., Martens, E. C., Gordon, J. I. and Smith, T. J. (2009). Structure of a SusD Homologue, BT1043, Involved in Mucin O-Glycan Utilization in a Prominent Human Gut Symbiont†,‡. Biochemistry 48(7): 1532-1542.
  11. Martens, E. C., Koropatkin, N. M., Smith, T. J. and Gordon, J. I. (2009). Complex glycan catabolism by the human gut microbiota: the Bacteroidetes Sus-like paradigm. J Biol Chem 284(37): 24673-24677.
  12. Koropatkin, N. M.*#, Martens, E. C., Gordon, J. I. and Smith, T. J. (2008). Starch catabolism by a prominent human gut symbiont is directed by the recognition of amylose helices. Structure 16(7): 1105-1115. (*Cover art, #Featured in “Editors Choice” Science)
  13. Koropatkin, N. M., Koppenaal, D. W., Pakrasi, H. B. and Smith, T. J. (2007). The structure of a cyanobacterial bicarbonate transport protein, CmpA. J Biol Chem 282(4): 2606-2614.
  14. Koropatkin, N. M.$, Pakrasi, H. B. and Smith, T. J. (2006). Atomic structure of a nitrate-binding protein crucial for photosynthetic productivity. Proc Natl Acad Sci U S A 103(26): 9820-9825.( $Selected for faculty of 1000)
  15. Koropatkin, N. M. and Holden, H. M. (2005). Structure of CDP-D-glucose 4,6-dehydratase from Salmonella typhi complexed with CDP-D-xylose. Acta Crystallogr D Biol Crystallogr 61(Pt 4): 365-373.
  16. Koropatkin, N. M., Cleland, W. W. and Holden, H. M. (2005). Kinetic and structural analysis of alpha-D-Glucose-1-phosphate cytidylyltransferase from Salmonella typhi. J Biol Chem 280(11): 10774-10780.
  17. Koropatkin, N. M. and Holden, H. M. (2004). Molecular structure of alpha-D-glucose-1-phosphate cytidylyltransferase from Salmonella typhi. J Biol Chem 279(42): 44023-44029.
  18. Koropatkin, N. M., Liu, H. W. and Holden, H. M. (2003). High resolution x-ray structure of tyvelose epimerase from Salmonella typhi. J Biol Chem 278(23): 20874-20881.
1 Protocol published
Product Analysis of Starch Active Enzymes by TLC
Authors:  Darrell Cockburn and Nicole Koropatkin, date: 10/20/2015, view: 5073, Q&A: 0
Thin layer chromatography (TLC) is a useful technique for detecting the presence of monosaccharides through to oligosaccharides, though it needs to be optimized for the specific sugars that are analyzed. Here we present a method for visualizing the ...
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