Methyltransferase-like protein is a ubiquitous enzyme-like protein in the human body, with binding domains for nucleic acids, proteins and other small molecules, and plays an important role in a variety of biological behaviours in normal organisms and diseases, characterised by the presence of a me...
During the movement of ATFS-1 to the nucleus, ubiquitin-like protein 5 (UBL-5) is upregulated with the assistance of ATFS-1 and defective proventriculus homolog protein (DVE-1) [22]. Subsequently, UBL-5 and DVE-1 form a complex that interacts with the promoters of UPRmt-related genes ...
Mechanistically, UNC-51-like kinase 1, a core autophagy protein, can phosphorylate the key glycolytic enzyme lactate dehydrogenase A (LDHA) and increase its enzyme activity, then promoting the production of lactate, which drives the Kla of vacuolar protein sorting 34 (Vps34). Vps34 Kla can not...
The methylation modification of m6A has been confirmed to be dynamic and reversible, involving methyltransferase “writers”, demethylase “erasers” and methylated reading protein “readers” [4]. For example, methyltransferase-like 3 (METTL3) and METTL14 can form a steady heterodimer complex. They ...
folding and isolation processes of eEF2 [20]. Furthermore, crystal structure comparisons reveal gross conformational changes in eEF2 upon binding to ribosomes. Within each super-domain grouping, the second super-domain is observed to exhibit a hinge-like motion, which induces a ratchet-like ...
Protein kinase RNA-like ER kinase (PERK) utilizes its intrinsic lipid kinase activity to generate phosphatidic acid, mediates Akt activation, and promotes adipocyte differentiation. PERK can promote adipocyte differentiation through activation of Akt [167]. Activating transcription factor 6 (ATF6) α ...
et al. Discovery of a drug-like G-quadruplex binding ligand by high-throughput docking. Chemmedchem 3, 881–884 (2008). 41. Totrov, M. & Abagyan, R. Flexible protein-ligand docking by global energy optimization in internal coordinates. Proteins 215–220 (1997). 42. Lee, K. et al....
The plastid-encoded Tic214(YCF1)/YCF2/FtsHi complex emerged early in chlorophyte evolution, too, maybe through the duplication of an early Tic20-like protein (Wunder et al., 2007, Kikuchi et al., 2018). The components of this complex are highly diverse, except for a C-terminal motif, ...
folding and isolation processes of eEF2 [20]. Furthermore, crystal structure comparisons reveal gross conformational changes in eEF2 upon binding to ribosomes. Within each super-domain grouping, the second super-domain is observed to exhibit a hinge-like motion, which induces a ratchet-like ...
A.k.a. RIPK6 and RIPK7 as well as proteins of the ROCO family —ROCO1 and ROCO2 — characterized by the presence of a Ras GTPase-like domain ROC (Ras of complex protein) immediately followed by a COR (C-terminal of ROC) domain. ...