about
Rational design of a new Trypanosoma rangeli trans-sialidase for efficient sialylation of glycansA Pasteurella multocida sialyltransferase displaying dual trans-sialidase activities for production of 3'-sialyl and 6'-sialyl glycans.Modulating the regioselectivity of a Pasteurella multocida sialyltransferase for biocatalytic production of 3'- and 6'-sialyllactose.Identification of the methyltransferase targeting C2499 in Deinococcus radiodurans 23S ribosomal RNA.Distinction between the Cfr methyltransferase conferring antibiotic resistance and the housekeeping RlmN methyltransferase.Recognition of guanosine by dissimilar tRNA methyltransferases.Enzyme catalysed production of sialylated human milk oligosaccharides and galactooligosaccharides by Trypanosoma cruzi trans-sialidase.Automated N-glycan profiling of a mutant Trypanosoma rangeli sialidase expressed in Pichia pastoris, using tandem mass spectrometry and bioinformatics.Identification of 5-hydroxycytidine at position 2501 concludes characterization of modified nucleotides in E. coli 23S rRNA.Mapping of ribosomal 23S ribosomal RNA modifications in Clostridium sporogenesDetection of internal N7-methylguanosine (m7G) RNA modifications by mutational profiling sequencingThe human methyltransferase ZCCHC4 catalyses N6-methyladenosine modification of 28S ribosomal RNAExcision of uracil from DNA by hSMUG1 includes strand incision and processing
P50
Q28538298-3B2CA1DB-AFF6-4117-9123-FD01038EFBDCQ35056940-B4EC16D7-0DB6-4B9A-8E7E-FCB2C3F2FABDQ38297395-CD25557E-CE3D-4128-BCAA-1C225F92D403Q40293449-978235B3-7B4D-42F5-8F14-317AAEE7E2A8Q41774206-65D75811-19AE-482B-B648-FF560F53F546Q42288537-F458F235-560F-45B3-AE21-C286E8836C8AQ46864086-358074D8-9116-4151-B6C9-ECFF56E55266Q51795991-413C4ACE-5B61-440C-A145-010085C2F971Q54357985-FFCE6FFC-E224-4015-AEF4-08E7FC8A1966Q89276276-E43708C5-38FB-445C-9A10-0A5FB16293B1Q90029388-1FCF59C4-42CB-4118-B7AB-406BDFB1161FQ91678562-00B39898-86DF-4FCF-AECC-4799C4C75753Q93367769-CA06D74A-E77D-499D-944D-81830FFCA3B7
P50
description
investigador
@es
researcher
@en
name
Finn Kirpekar
@en
type
label
Finn Kirpekar
@en
prefLabel
Finn Kirpekar
@en
P31
P496
0000-0003-1901-2266