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1دورية أكاديمية
المؤلفون: Kaczmarczyk, Artur P., Déclais, Anne-Cécile, Newton, Matthew D., Boulton, Simon J., Lilley, David M. J., Rueda, David S.
المصدر: Kaczmarczyk , A P , Déclais , A-C , Newton , M D , Boulton , S J , Lilley , D M J & Rueda , D S 2022 , ' Search and processing of Holliday junctions within long DNA by junction-resolving enzymes ' , Nature Communications , vol. 13 , 5921 . https://doi.org/10.1038/s41467-022-33503-6Test
مصطلحات موضوعية: DNA/metabolism, DNA, Cruciform, Deoxyribonuclease I/metabolism, Endodeoxyribonucleases/metabolism, Endonucleases/metabolism, Holliday Junction Resolvases/metabolism, Nucleic Acid Conformation, /dk/atira/pure/subjectarea/asjc/1000, name=General, /dk/atira/pure/subjectarea/asjc/3100/3100, name=General Physics and Astronomy, /dk/atira/pure/subjectarea/asjc/1600/1600, name=General Chemistry, /dk/atira/pure/subjectarea/asjc/1300/1300, name=General Biochemistry,Genetics and Molecular Biology
وصف الملف: application/pdf
الإتاحة: https://doi.org/10.1038/s41467-022-33503-6Test
https://discovery.dundee.ac.uk/en/publications/d9a29e50-70ce-4f71-8000-0d02793bd0e6Test
https://discovery.dundee.ac.uk/ws/files/87730471/s41467_022_33503_6.pdfTest
http://www.scopus.com/inward/record.url?scp=85139571965&partnerID=8YFLogxKTest -
2دورية أكاديمية
المصدر: Bueren-Calabuig , J , Bage , M , Cowling , V & Pisliakov , A 2019 , ' Mechanism of allosteric activation of human mRNA cap methyltransferase (RNMT) by RAM : Insights from accelerated molecular dynamics simulations ' , Nucleic Acids Research , vol. 47 , no. 16 , gkz613 , pp. 8675-8692 . https://doi.org/10.1093/nar/gkz613Test
مصطلحات موضوعية: RNMT, allosteric activation, accelerated molecular dynamics, conformational selection, mRNA cap, Allosteric Regulation, Humans, Substrate Specificity, RNA Caps/chemistry, Recombinant Proteins/chemistry, Thermodynamics, RNA Polymerase II/genetics, Methyltransferases/chemistry, S-Adenosylmethionine/chemistry, Cloning, Molecular, Transcription, Genetic, Protein Interaction Domains and Motifs, Binding Sites, Genetic Vectors/chemistry, Amino Acid Sequence, Protein Conformation, alpha-Helical, Gene Expression, RNA-Binding Proteins/chemistry, S-Adenosylhomocysteine/chemistry, Escherichia coli/genetics, Molecular Dynamics Simulation, Sequence Homology
وصف الملف: application/pdf
الإتاحة: https://doi.org/10.1093/nar/gkz613Test
https://discovery.dundee.ac.uk/en/publications/c67a2e6b-59db-400c-804f-6d913de05201Test
https://discovery.dundee.ac.uk/ws/files/36653182/gkz613.pdfTest
http://www.scopus.com/inward/record.url?scp=85073307093&partnerID=8YFLogxKTest -
3دورية أكاديمية
المؤلفون: Vickery, Owen, Carvalheda Dos Santos, Catarina, Zaidi, Saheem A., Pisliakov, Andrei, Katritch, Vsevolod, Zachariae, Ulrich
المصدر: Vickery , O , Carvalheda Dos Santos , C , Zaidi , S A , Pisliakov , A , Katritch , V & Zachariae , U 2018 , ' Intracellular Transfer of Na+ in an Active State G Protein Coupled Receptor ' , Structure , vol. 26 , no. 1 , pp. 171-180.e2 . https://doi.org/10.1016/j.str.2017.11.013Test
مصطلحات موضوعية: free energy profiles, GPCR, GPCR activation, ion channels, membrane surface receptors, pK, polar network, protonation state, signal transduction, sodium, Humans, Cations, Monovalent, Thermodynamics, Ion Transport, Protein Interaction Domains and Motifs, Binding Sites, Protein Conformation, alpha-Helical, Static Electricity, Molecular Dynamics Simulation, Amino Acid Motifs, Receptor, Muscarinic M2/chemistry, Sodium/chemistry, Carbachol/chemistry, Phosphatidylcholines/chemistry, Hydrophobic and Hydrophilic Interactions, Protein Binding, Ligands
وصف الملف: application/pdf
الإتاحة: https://doi.org/10.1016/j.str.2017.11.013Test
https://discovery.dundee.ac.uk/en/publications/cb2828ea-82fc-42c4-834f-e43545d90f81Test
https://discovery.dundee.ac.uk/ws/files/41826641/Vickeryet_al_Final_submission_09_11.pdfTest
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5805466Test/ -
4دورية أكاديمية
المصدر: Shi , X , Huang , L , Lilley , D M J , Harbury , P B & Herschlag , D 2016 , ' The solution structural ensembles of RNA kink-turn motifs and their protein complexes ' , Nature Chemical Biology , vol. 12 , no. 3 , pp. 146-152 . https://doi.org/10.1038/nchembio.1997Test
مصطلحات موضوعية: Base sequence, Interferometry, Molecular dynamics simulation, Molecular sequence data, Nucleic acid conformation, Nucleotide motifs, RNA, Scattering, Radiation, X-Rays, Journal article, Research support, N.I.H., Extramural, Non-U.S. Gov't
وصف الملف: application/pdf
الإتاحة: https://doi.org/10.1038/nchembio.1997Test
https://discovery.dundee.ac.uk/en/publications/c9fd8da4-b54b-405e-b312-ea0026b53ea5Test
https://discovery.dundee.ac.uk/ws/files/9708336/main_text_LH_10_22_2105E.pdfTest -
5دورية أكاديمية
المؤلفون: Moynié, Lucile, Hope, Anthony G., Finzel, Kara, Schmidberger, Jason, Leckie, Stuart M., Schneider, Gunter, Burkart, Michael D., Smith, Andrew D., Gray, David W., Naismith, James H.
المصدر: Moynié , L , Hope , A G , Finzel , K , Schmidberger , J , Leckie , S M , Schneider , G , Burkart , M D , Smith , A D , Gray , D W & Naismith , J H 2016 , ' A substrate mimic allows high-throughput assay of the FabA protein and consequently the identification of a novel inhibitor of Pseudomonas aeruginosa FabA ' , Journal of Molecular Biology , vol. 428 , no. 1 , pp. 108-120 . https://doi.org/10.1016/j.jmb.2015.10.027Test
مصطلحات موضوعية: Crystallography, X-Ray, Cysteamine, Enzyme Inhibitors, Escherichia coli, Fatty Acid Synthase, Type II, High-Throughput Screening Assays, Models, Molecular, Protein Conformation, Pseudomonas aeruginosa
وصف الملف: application/pdf
الإتاحة: https://doi.org/10.1016/j.jmb.2015.10.027Test
https://discovery.dundee.ac.uk/en/publications/e9dc0cc2-8783-4970-9944-5d05bc3b56c4Test
https://discovery.dundee.ac.uk/ws/files/9378432/1_s2.0_S002228361500621X_main.pdfTest -
6دورية أكاديمية
المؤلفون: O'Rourke, Patrick E. F., Kalinowska-Tłuścik, Justyna, Fyfe, Paul K., Dawson, Alice, Hunter, William N.
المصدر: O'Rourke , P E F , Kalinowska-Tłuścik , J , Fyfe , P K , Dawson , A & Hunter , W N 2014 , ' Crystal structures of IspF from Plasmodium falciparum and Burkholderia cenocepacia : comparisons inform antimicrobial drug target assessment ' BMC Structural Biology , vol 14 , 1 . DOI:10.1186/1472-6807-14-1
مصطلحات موضوعية: Amino Acid Sequence, Burkholderia cenocepacia, Catalytic Domain, Citric Acid, Crystallography, X-Ray, Erythritol, Models, Molecular, Phosphorus-Oxygen Lyases, Plasmodium falciparum, Protein Conformation, Protein Structure, Secondary, Recombinant Proteins, Sequence Alignment, Substrate Specificity, Sugar Phosphates, Zinc
الإتاحة: https://doi.org/10.1186/1472-6807-14-1Test
http://discovery.dundee.ac.uk/portal/en/research/crystal-structures-of-ispf-from-plasmodium-falciparum-and-burkholderia-cenocepaciaTest(572de141-f602-433c-b294-fd7b39c87ab4).html
http://hdl.handle.net/10588/572de141-f602-433c-b294-fd7b39c87ab4Test -
7دورية أكاديمية
المؤلفون: Bowman, Lisa, Flanagan, Lindsey, Fyfe, Paul K., Parkin, Alison, Hunter, William N., Sargent, Frank
المصدر: Bowman , L , Flanagan , L , Fyfe , P K , Parkin , A , Hunter , W N & Sargent , F 2014 , ' How the structure of the large subunit controls function in an oxygen-tolerant [NiFe]-hydrogenase ' Biochemical Journal , vol 458 , no. 3 , pp. 449-458 . DOI:10.1042/BJ20131520
مصطلحات موضوعية: Bacterial Proteins, Catalysis, Crystallography, X-Ray, Genetic Engineering, Glutamic Acid, Histidine, Hydrogen, Hydrogenase, Oxygen, Protein Conformation, Protein Subunits, Salmonella enterica
وصف الملف: application/pdf
الإتاحة: https://doi.org/10.1042/BJ20131520Test
http://discovery.dundee.ac.uk/portal/en/research/how-the-structure-of-the-large-subunit-controls-function-in-an-oxygentolerant-nifehydrogenaseTest(ace6225e-a4ea-4187-8e6f-5771d9b2057f).html
http://hdl.handle.net/10588/ace6225e-a4ea-4187-8e6f-5771d9b2057fTest
http://discovery.dundee.ac.uk/ws/files/8021631/449.full_1_.pdfTest
http://www.biochemj.org/bjTest/ -
8دورية أكاديمية
المؤلفون: Lucas, Xavier, Simon, Silke, Schubert, Rolf, Günther, Stefan
المصدر: Lucas , X , Simon , S , Schubert , R & Günther , S 2013 , ' Discovery of the inhibitory effect of a phosphatidylinositol derivative on P-glycoprotein by virtual screening followed by in vitro cellular studies ' , PLoS ONE , vol. 8 , no. 4 , e60679 . https://doi.org/10.1371/journal.pone.0060679Test
مصطلحات موضوعية: Biological transport, Caco-2 cells, Cell line, Chemistry, Pharmaceutical, Cryoelectron microscopy, Digoxin, Drug discovery, Drug resistance, Multiple, Fluoresceins, Humans, Molecular docking simulation, P-Glycoproteins, Permeability, Phosphatidylinositols, Phospholipids, Protein binding, Protein conformation, Journal article, Research support, Non-U.S. Gov't
وصف الملف: application/pdf
الإتاحة: https://doi.org/10.1371/journal.pone.0060679Test
https://discovery.dundee.ac.uk/en/publications/e17e9424-5420-47b0-bb5f-764362e56380Test
https://discovery.dundee.ac.uk/ws/files/10641939/journal.pone.0060679.PDFTest -
9دورية أكاديمية
المؤلفون: Dawson, Alice, Gibellini, Federica, Sienkiewicz, Natasha, Tulloch, Lindsay B., Fyfe, Paul K., McLuskey, Karen, Fairlamb, Alan H., Hunter, William N.
المصدر: Dawson , A , Gibellini , F , Sienkiewicz , N , Tulloch , L B , Fyfe , P K , McLuskey , K , Fairlamb , A H & Hunter , W N 2006 , ' Structure and reactivity of Trypanosoma brucei pteridine reductase : inhibition by the archetypal antifolate methotrexate ' , Molecular Microbiology , vol. 61 , no. 6 , pp. 1457-1468 . https://doi.org/10.1111/j.1365-2958.2006.05332.xTest
مصطلحات موضوعية: Amino Acid Sequence, Animals, Binding Sites, Catalytic Domain, Crystallography, X-Ray, Folic Acid Antagonists/pharmacology, Methotrexate/pharmacology, Molecular Sequence Data, Oxidoreductases/antagonists & inhibitors, Protein Conformation, Protozoan Proteins/antagonists & inhibitors, Trypanosoma brucei brucei/enzymology
وصف الملف: application/pdf
الإتاحة: https://doi.org/10.1111/j.1365-2958.2006.05332.xTest
https://discovery.dundee.ac.uk/en/publications/cc8f4567-cceb-43d7-aaf4-e3d0bc5b9641Test
https://discovery.dundee.ac.uk/ws/files/35647144/Dawson_et_al_2006_Molecular_Microbiology.pdfTest -
10دورية أكاديمية
المؤلفون: Raghava, G P S, Barton, Geoffrey J
المصدر: Raghava , G P S & Barton , G J 2006 , ' Quantification of the variation in percentage identity for protein sequence alignments ' , BMC Bioinformatics , vol. 7 , pp. 415 . https://doi.org/10.1186/1471-2105-7-415Test
مصطلحات موضوعية: Algorithms, Amino Acid Sequence, Computational Biology, Databases, Protein, Protein Conformation, Proteins, Sequence Alignment, Software
وصف الملف: application/pdf
الإتاحة: https://doi.org/10.1186/1471-2105-7-415Test
https://discovery.dundee.ac.uk/en/publications/fa19dec6-dab9-4e51-9af4-93b32caebb7aTest
https://discovery.dundee.ac.uk/ws/files/9223181/art_3A10.1186_2F1471_2105_7_415.pdfTest