{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Vaughan RM"],"funding":["NCI NIH HHS"],"pagination":["7106-7113"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12069652"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["43(13)"],"pubmed_abstract":["Kinase domains are highly conserved within proteins in both sequence and structure. Many factors, including phosphorylation, amino acid substitutions or mutations, and small molecule inhibitor binding, influence conformations of the kinase domain and enzymatic activity. ULK1 and ULK2 are serine/threonine kinases that serve important roles in autophagy, an intracellular recycling process capable of degrading proteins and organelles <i>via</i> fusion with lysosomes. ULK1/2 are emerging as therapeutic targets in human cancer, particularly KRAS-driven malignancies. Here, we performed molecular dynamics (MD) simulations to hypothesize bound poses for the ULK1/2 small molecule inhibitor, ULK-101. We observed stable bound states for ULK-101 to the adenosine triphosphate (ATP)-binding site of ULK2"],"journal":["Journal of biomolecular structure & dynamics"],"pubmed_title":["Molecular dynamics simulations provide insights into ULK-101 potency and selectivity toward autophagic kinases ULK1/2."],"pmcid":["PMC12069652"],"funding_grant_id":["R21 CA270588","R21 CA252430","R21 CA263133","K00 CA245821"],"pubmed_authors":["Vaughan RM","Martin KR","Dickson BM","MacKeigan JP"],"additional_accession":[]},"is_claimable":false,"name":"Molecular dynamics simulations provide insights into ULK-101 potency and selectivity toward autophagic kinases ULK1/2.","description":"Kinase domains are highly conserved within proteins in both sequence and structure. Many factors, including phosphorylation, amino acid substitutions or mutations, and small molecule inhibitor binding, influence conformations of the kinase domain and enzymatic activity. ULK1 and ULK2 are serine/threonine kinases that serve important roles in autophagy, an intracellular recycling process capable of degrading proteins and organelles <i>via</i> fusion with lysosomes. ULK1/2 are emerging as therapeutic targets in human cancer, particularly KRAS-driven malignancies. Here, we performed molecular dynamics (MD) simulations to hypothesize bound poses for the ULK1/2 small molecule inhibitor, ULK-101. We observed stable bound states for ULK-101 to the adenosine triphosphate (ATP)-binding site of ULK2","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Aug","modification":"2026-06-05T14:56:56.355Z","creation":"2026-05-18T03:13:08.992Z"},"accession":"S-EPMC12069652","cross_references":{"pubmed":["39535169"],"doi":["10.1080/07391102.2024.2425833"]}}