Zobrazeno 1 - 10
of 43
pro vyhledávání: '"Stephen G. Aller"'
Publikováno v:
Toxins, Vol 16, Iss 9, p 406 (2024)
ABC toxin complexes are a class of protein toxin translocases comprised of a multimeric assembly of protein subunits. Each subunit displays a unique composition, contributing to the formation of a syringe-like nano-machine with natural cargo carrying
Externí odkaz:
https://doaj.org/article/31655fa251874995a8fdc5a21890d089
Autor:
Evan J. Brettrager, Selma M. Cuya, Zachary E. Tibbs, Jun Zhang, Charles N. Falany, Stephen G. Aller, Robert C. A. M. van Waardenburg
Publikováno v:
Scientific Reports, Vol 13, Iss 1, Pp 1-12 (2023)
Abstract Tyrosyl-DNA phosphodiesterase I (Tdp1) hydrolyzes phosphodiester-linked adducts from both ends of DNA. This includes the topoisomerase I (TOP1)-DNA covalent reaction intermediate that is the target of the camptothecin class of chemotherapeut
Externí odkaz:
https://doaj.org/article/8d1bf68e18c94921a249cac7993ebd2a
Autor:
Jere P. Segrest, Chongren Tang, Hyun D. Song, Martin K. Jones, W. Sean Davidson, Stephen G. Aller, Jay W. Heinecke
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-12 (2022)
ATP-binding cassette transporter A1 (ABCA1) drives phospholipid (PL) from the plasma membrane into extracellular apolipoprotein A-I, for the production of high density lipoprotein (HDL). Here, the authors use simulations to assess the mechanism of AB
Externí odkaz:
https://doaj.org/article/fabaa2042cb346d69e7b13267b43befc
Autor:
Shimpi Bedi, Jamie Morris, Amy Shah, Rachel C. Hart, W. Gray Jerome, Stephen G. Aller, Chongren Tang, Tomas Vaisar, Karin E. Bornfeldt, Jere P. Segrest, Jay W. Heinecke, W. Sean Davidson
Publikováno v:
Journal of Lipid Research, Vol 63, Iss 3, Pp 100168- (2022)
Because of its critical role in HDL formation, significant efforts have been devoted to studying apolipoprotein A-I (APOA1) structural transitions in response to lipid binding. To assess the requirements for the conformational freedom of its termini
Externí odkaz:
https://doaj.org/article/85e2394e2ac54dddbe32143770942ea7
Publikováno v:
IUCrJ, Vol 7, Iss 4, Pp 663-672 (2020)
The multidrug transporter P-glycoprotein (Pgp)/ABCB1/MDR1 plays an important role in multidrug resistance (MDR) and detoxification owing to its ability to efflux an unusually large and chemically diverse set of substrates. Previous phenylalanine-to-a
Externí odkaz:
https://doaj.org/article/035d72c230004e189c973ae54b8a6e60
Publikováno v:
IUCrJ
IUCrJ, Vol 7, Iss 4, Pp 663-672 (2020)
IUCrJ, Vol 7, Iss 4, Pp 663-672 (2020)
Polyspecific ligand recognition by P-glycoprotein includes compensatory mechanisms in the form of ligand-binding shifts when ligand-interacting residues are challenged by mutagenesis. Point mutations of ligand-interacting phenylalanine residues to al
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a8dba44872c58702b65306958f158d7
https://doi.org/10.1107/s2052252520005709
https://doi.org/10.1107/s2052252520005709
Autor:
Kenneth L. Martin, Mark Turlington, Jake E. Doiron, Stephen G. Aller, Gary W. Breton, John Bacsa, Christina A. Le
Publikováno v:
ChemMedChem. 15:1720-1730
Although the 1,2,3-triazole is a commonly used amide bioisostere in medicinal chemistry, the structural implications of this replacement have not been fully studied. Employing X-ray crystallography and computational studies, we report the spatial and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb48cfb8491ca9fda7b1fe09420a98b8
https://doi.org/10.1002/cmdc.202000220
https://doi.org/10.1002/cmdc.202000220
Autor:
Jere P. Segrest, Chongren Tang, Hyun D. Song, Martin K. Jones, W. Sean Davidson, Stephen G. Aller, Jay W. Heinecke
Publikováno v:
Nature communications. 13(1)
Production of high density lipoprotein (HDL) requires ATP-binding cassette transporter A1 (ABCA1) to drive phospholipid (PL) from the plasma membrane into extracellular apolipoprotein A-I. Here, we use simulations to show that domains of ABCA1 within
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff66f22f9d9ac4151942eb3b127559bb
https://pubmed.ncbi.nlm.nih.gov/35974019
https://pubmed.ncbi.nlm.nih.gov/35974019
Publikováno v:
Acta Crystallographica. Section D, Structural Biology
A cluster A-I substrate-binding protein reveals conformational changes, including an asymmetric rigid-body rotation of the flexible lobe, the reordering of a mobile helix and a spring-hammer mechanism.
In the structural biology of bacterial subs
In the structural biology of bacterial subs
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b3f7e022e04724250e590eac02ad401
http://europepmc.org/articles/PMC6719664
http://europepmc.org/articles/PMC6719664
Site 2 of the Yersinia pestis substrate-binding protein YfeA is a dynamic surface metal-binding site
Autor:
Christopher D. Radka, Stephen G. Aller
Publikováno v:
Acta Crystallographica. Section F, Structural Biology Communications
The Yersinia pestis substrate-binding protein YfeA contains two polyspecific metal-binding sites, and site 2 is capable of collaborating with other protein molecules for inter-protein metal coordination. The inter-protein metal coordination can occur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4cce60654669f2ea329a4b211e1034e2
https://pubmed.ncbi.nlm.nih.gov/34473105
https://pubmed.ncbi.nlm.nih.gov/34473105