Kakalis LT - Search Results

1

Characterization of the calcium-binding sites of calcineurin B.

Kakalis LT, Kennedy M, Sikkink R, Rusnak F, Armitage IM. Kakalis LT, et al. FEBS Lett. 1995 Mar 27;362(1):55-8. doi: 10.1016/0014-5793(95)00207-p. FEBS Lett. 1995. PMID: 7698353 Free article.

2

Expression of human cyclophilin-40 and the effect of the His141-->Trp mutation on catalysis and cyclosporin A binding.

Hoffmann K, Kakalis LT, Anderson KS, Armitage IM, Handschumacher RE. Hoffmann K, et al. Among authors: kakalis lt. Eur J Biochem. 1995 Apr 1;229(1):188-93. doi: 10.1111/j.1432-1033.1995.tb20454.x. Eur J Biochem. 1995. PMID: 7744028 Free article.

3

Solution conformation of a cyclophilin-bound proline isomerase substrate.

Kakalis LT, Armitage IM. Kakalis LT, et al. Biochemistry. 1994 Feb 15;33(6):1495-501. doi: 10.1021/bi00172a028. Biochemistry. 1994. PMID: 8312269

4

HIV protease substrate conformation: modulation by cyclophilin A.

McCornack MA, Kakalis LT, Caserta C, Handschumacher RE, Armitage IM. McCornack MA, et al. Among authors: kakalis lt. FEBS Lett. 1997 Sep 1;414(1):84-8. doi: 10.1016/s0014-5793(97)00974-5. FEBS Lett. 1997. PMID: 9305737 Free article.

5

Identification of transient intermediates in the bisphosphatase reaction of rat liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase by 31P-NMR spectroscopy.

Okar DA, Kakalis LT, Narula SS, Armitage IM, Pilkis SJ. Okar DA, et al. Among authors: kakalis lt. Biochem J. 1995 May 15;308 ( Pt 1)(Pt 1):189-95. doi: 10.1042/bj3080189. Biochem J. 1995. PMID: 7755565 Free PMC article.

6

Impact of angiotensin-converting enzyme substrate conformation on fractional hydrolysis in lung.

Merker MP, Armitage IM, Audi SH, Kakalis LT, Linehan JH, Maehl JR, Roerig DL, Dawson CA. Merker MP, et al. Among authors: kakalis lt. Am J Physiol. 1996 Feb;270(2 Pt 1):L251-9. doi: 10.1152/ajplung.1996.270.2.L251. Am J Physiol. 1996. PMID: 8779994

7

Defining critical residues for substrate binding to 1-deoxy-D-xylulose 5-phosphate synthase--active site substitutions stabilize the predecarboxylation intermediate C2α-lactylthiamin diphosphate.

Basta LAB, Patel H, Kakalis L, Jordan F, Meyers CLF. Basta LAB, et al. FEBS J. 2014 Jun;281(12):2820-2837. doi: 10.1111/febs.12823. Epub 2014 May 12. FEBS J. 2014. PMID: 24767541 Free PMC article.

8

Electronic and nuclear magnetic resonance spectroscopic features of the 1',4'-iminopyrimidine tautomeric form of thiamin diphosphate, a novel intermediate on enzymes requiring this coenzyme.

Baykal AT, Kakalis L, Jordan F. Baykal AT, et al. Biochemistry. 2006 Jun 20;45(24):7522-8. doi: 10.1021/bi060395k. Biochemistry. 2006. PMID: 16768448 Free PMC article.

9

Determination of pre-steady-state rate constants on the Escherichia coli pyruvate dehydrogenase complex reveals that loop movement controls the rate-limiting step.

Balakrishnan A, Nemeria NS, Chakraborty S, Kakalis L, Jordan F. Balakrishnan A, et al. J Am Chem Soc. 2012 Nov 14;134(45):18644-55. doi: 10.1021/ja3062375. Epub 2012 Nov 2. J Am Chem Soc. 2012. PMID: 23088422 Free PMC article.

10

Nuclear magnetic resonance evidence for the role of the flexible regions of the E1 component of the pyruvate dehydrogenase complex from gram-negative bacteria.

Song J, Park YH, Nemeria NS, Kale S, Kakalis L, Jordan F. Song J, et al. J Biol Chem. 2010 Feb 12;285(7):4680-94. doi: 10.1074/jbc.M109.082842. Epub 2009 Dec 7. J Biol Chem. 2010. PMID: 19996100 Free PMC article.

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