about
Lesion processing by a repair enzyme is severely curtailed by residues needed to prevent aberrant activity on undamaged DNASwitching DNA-binding specificity by unnatural amino acid substitution.Simultaneous inhibition of key growth pathways in melanoma cells and tumor regression by a designed bidentate constrained helical peptideE2-mediated small ubiquitin-like modifier (SUMO) modification of thymine DNA glycosylase is efficient but not selective for the enzyme-product complex.Lesion search and recognition by thymine DNA glycosylase revealed by single molecule imaging.Divergent mechanisms for enzymatic excision of 5-formylcytosine and 5-carboxylcytosine from DNA.Mechanisms for enzymatic cleavage of the N-glycosidic bond in DNA.How a mismatch repair enzyme balances the needs for efficient lesion processing and minimal action on undamaged DNA.Crystal structure of the catalytic domain of HIV-1 restriction factor APOBEC3G in complex with ssDNA.
P50
Q24319667-77AAE691-39BC-4F21-A405-DE79C9C52C16Q24813825-B88167F7-E28C-463B-BBED-11FF8B9718DBQ33934743-EDA1406D-864E-4D5B-8FAC-2BFF8F94A32CQ34076047-3FEE3502-5817-4A40-B2AB-9D9EE82ACF8EQ35171647-285683C2-05DE-4D41-AB22-3D8241F6D1A4Q37595036-8EBC67DB-84D8-4BA3-B693-C71F44C4BCF1Q38245504-14C5E321-83E8-47ED-8CFE-B0F2C6FF4B01Q42445136-61C0ED9D-F04B-418C-B208-D16E9825B755Q55289251-7F99FBFF-DC5A-4A54-BECA-17B46A5193DF
P50
description
investigador
@es
researcher
@en
wetenschapper
@nl
name
Atanu Maiti
@en
Atanu Maiti
@nl
type
label
Atanu Maiti
@en
Atanu Maiti
@nl
prefLabel
Atanu Maiti
@en
Atanu Maiti
@nl
P31
P496
0000-0002-9080-1025