Tawfik DS - Search Results

1

The moderately efficient enzyme: evolutionary and physicochemical trends shaping enzyme parameters.

Bar-Even A, Noor E, Savir Y, Liebermeister W, Davidi D, Tawfik DS, Milo R. Bar-Even A, et al. Among authors: tawfik ds. Biochemistry. 2011 May 31;50(21):4402-10. doi: 10.1021/bi2002289. Epub 2011 May 4. Biochemistry. 2011. PMID: 21506553

2

Detection of catalytic monoclonal antibodies.

Tawfik DS, Green BS, Eshhar Z. Tawfik DS, et al. Anal Biochem. 1992 Apr;202(1):35-9. doi: 10.1016/0003-2697(92)90201-h. Anal Biochem. 1992. PMID: 1621985

3

Efficient and selective p-nitrophenyl-ester-hydrolyzing antibodies elicited by a p-nitrobenzyl phosphonate hapten.

Tawfik DS, Lindner AB, Chap R, Eshhar Z, Green BS. Tawfik DS, et al. Eur J Biochem. 1997 Mar 1;244(2):619-26. doi: 10.1111/j.1432-1033.1997.00619.x. Eur J Biochem. 1997. PMID: 9119032 Free article.

4

Directed evolution of the promiscuous esterase activity of carbonic anhydrase II.

Gould SM, Tawfik DS. Gould SM, et al. Among authors: tawfik ds. Biochemistry. 2005 Apr 12;44(14):5444-52. doi: 10.1021/bi0475471. Biochemistry. 2005. PMID: 15807537

5

High-throughput screens and selections of enzyme-encoding genes.

Aharoni A, Griffiths AD, Tawfik DS. Aharoni A, et al. Among authors: tawfik ds. Curr Opin Chem Biol. 2005 Apr;9(2):210-6. doi: 10.1016/j.cbpa.2005.02.002. Curr Opin Chem Biol. 2005. PMID: 15811807 Review.

6

Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase.

Khersonsky O, Tawfik DS. Khersonsky O, et al. Among authors: tawfik ds. Biochemistry. 2005 Apr 26;44(16):6371-82. doi: 10.1021/bi047440d. Biochemistry. 2005. PMID: 15835926

7

High affinity, stability, and lactonase activity of serum paraoxonase PON1 anchored on HDL with ApoA-I.

Gaidukov L, Tawfik DS. Gaidukov L, et al. Among authors: tawfik ds. Biochemistry. 2005 Sep 6;44(35):11843-54. doi: 10.1021/bi050862i. Biochemistry. 2005. PMID: 16128586

8

Shared promiscuous activities and evolutionary features in various members of the amidohydrolase superfamily.

Roodveldt C, Tawfik DS. Roodveldt C, et al. Among authors: tawfik ds. Biochemistry. 2005 Sep 27;44(38):12728-36. doi: 10.1021/bi051021e. Biochemistry. 2005. PMID: 16171387

9

Enzyme promiscuity: evolutionary and mechanistic aspects.

Khersonsky O, Roodveldt C, Tawfik DS. Khersonsky O, et al. Among authors: tawfik ds. Curr Opin Chem Biol. 2006 Oct;10(5):498-508. doi: 10.1016/j.cbpa.2006.08.011. Epub 2006 Aug 30. Curr Opin Chem Biol. 2006. PMID: 16939713 Review.

10

The latent promiscuity of newly identified microbial lactonases is linked to a recently diverged phosphotriesterase.

Afriat L, Roodveldt C, Manco G, Tawfik DS. Afriat L, et al. Among authors: tawfik ds. Biochemistry. 2006 Nov 21;45(46):13677-86. doi: 10.1021/bi061268r. Biochemistry. 2006. PMID: 17105187

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