You are here

Found 8 results

Sort by:[Year][Author]
Filters: author is Haikal  [Clear All Filters]
1998
ZegersI, LorisR, DehollanderG, FattahHaikal A, PoortmansF, SteyaertJ, WynsL.  1998.  Hydrolysis of a slow cyclic thiophosphate substrate of RNase T1 analyzed by time-resolved crystallography. 5(4):280-283. Abstract
ZegersI, LorisR, DehollanderG, FattahHaikal A, PoortmansF, SteyaertJ, WynsL.  1998.  Hydrolysis of a slow cyclic thiophosphate substrate of RNase T1 analyzed by time-resolved crystallography. 5(4):280-283. Abstract
1994
SteyaertJ, HaikalAF, WynsL.  1994.  Investigation of the functional interplay between the primary site and the subsite of RNase T1: kinetic analysis of single and multiple mutants for modified substrates. 18(4):318-323. Abstract
SteyaertJ, HaikalAF, WynsL.  1994.  Investigation of the functional interplay between the primary site and the subsite of RNase T1: kinetic analysis of single and multiple mutants for modified substrates. 18(4):318-323. Abstract
ZegersI, HaikalAF, PalmerR, WynsL.  1994.  Crystal structure of RNase T1 with 3'-guanylic acid and guanosine. 269(1):127-133. Abstract
1992
SteyaertJ, HaikalAF, StanssensP, WynsL.  1992.  Dissection of the ribonuclease T1 subsite. The transesterification kinetics of Asn36Ala and Asn98Ala ribonuclease T1 for minimal dinucleoside phosphates. 203(3):551-555. Abstract
SteyaertJ, HaikalAF, StanssensP, WynsL.  1992.  Dissection of the ribonuclease T1 subsite. The transesterification kinetics of Asn36Ala and Asn98Ala ribonuclease T1 for minimal dinucleoside phosphates. 203(3):551-555. Abstract
1991
SteyaertJ, HaikalAF, WynsL, StanssensP.  1991.  Subsite interactions of ribonuclease T1: Asn36 and Asn98 accelerate GpN transesterification through interactions with the leaving nucleoside N. Biochemistry. 30(35):8666-8670. Abstract

Publications on

Most recent publications