Results 151 to 160 of about 124,916 (340)
Recognition and Cleavage of Human tRNA Methyltransferase TRMT1 by the SARS‐CoV‐2 Main Protease
Angel D′Oliviera +2 more
openalex +2 more sources
Structure, activity and function of the lysine methyltransferase SETD5 [PDF]
Mingyang Li +7 more
openalex +1 more source
Development of Dimethylsulfonium Probes for Broad Profiling of Methyllysine Reader Proteins
Development of oligoglycine‐based dimethylsulfonium probes for unbiased crosslinking to methyllysine readers. The general probe facilitates profiling of site‐specific methyllysine readers, evaluation of selectivity and activity of reader inhibitors, and global profiling of methyllysine readers.
Jinyu Yang +3 more
wiley +1 more source
A substrate promiscuous and regioselective O‐methyltransferase, SmOMT, is functionally and structurally characterized. A double mutant, SmOMTE152A/I306A, exhibited enhanced catalytic activity. By coupling this mutant with a mutant halide methyltransferase, AtHMTV140T, for SAM regeneration, a superior artificial fusion enzyme, AtHMTV140T‐L95‐SmOMTE152A ...
Xiran Xiong +11 more
wiley +1 more source
Abstract Background and Aims Intrahepatic cholangiocarcinoma (ICC) is a deadly but poorly understood disease, and its treatment options are very limited. The aim of this study was to identify the molecular drivers of ICC and search for therapeutic targets.
Yuto Shiode +16 more
wiley +1 more source
Generating Dynamic Structures Through Physics‐Based Sampling of Predicted Inter‐Residue Geometries
While static structure prediction has been revolutionized, modeling protein dynamics remains elusive. trRosettaX2‐Dynamics is presented to address this challenge. This framework leverages a Transformer‐based network to predict inter‐residue geometric constraints, guiding conformation generation via physics‐based iterative sampling. The resulting method
Chenxiao Xiang +3 more
wiley +1 more source
Recent advances in developing degraders & inhibitors of lysine methyltransferases [PDF]
Julia Velez +2 more
openalex +1 more source

