{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,9,25]],"date-time":"2025-09-25T00:14:00Z","timestamp":1758759240287,"version":"3.44.0"},"reference-count":29,"publisher":"Springer Science and Business Media LLC","issue":"5","license":[{"start":{"date-parts":[[2024,11,8]],"date-time":"2024-11-08T00:00:00Z","timestamp":1731024000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2024,11,8]],"date-time":"2024-11-08T00:00:00Z","timestamp":1731024000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"funder":[{"name":"Researchers Supporting project, King Saud University, Riyadh,\u00a0Saudi\u00a0Arabia","award":["RSP 2024R122"],"award-info":[{"award-number":["RSP 2024R122"]}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Mol Divers"],"published-print":{"date-parts":[[2025,10]]},"DOI":"10.1007\/s11030-024-11020-6","type":"journal-article","created":{"date-parts":[[2024,11,8]],"date-time":"2024-11-08T02:16:14Z","timestamp":1731032174000},"page":"4083-4095","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Phytosterols as inhibitors of New Delhi metallo-\u03b2-lactamase (NDM-1): an in silico study"],"prefix":"10.1007","volume":"29","author":[{"given":"Mashihur","family":"Rahman","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mohd","family":"Ahsan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Md Tabish","family":"Rehman","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mohamed F.","family":"AlAjmi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Md. Khurshid Alam","family":"Khan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2024,11,8]]},"reference":[{"key":"11020_CR1","volume-title":"Antimicrobial resistance: global report on surveillance","author":"W.H.O.","year":"2014","unstructured":"W.H.O. (2014) Antimicrobial resistance: global report on surveillance. World Health Organisation, Geneva"},{"key":"11020_CR2","volume-title":"Global action plan on antimicrobial resistance","author":"W.H.O.","year":"2015","unstructured":"W.H.O. (2015) Global action plan on antimicrobial resistance. World Health Organisation, Geneva"},{"issue":"3","key":"11020_CR3","doi-asserted-by":"publisher","first-page":"969","DOI":"10.1128\/AAC.01009-09","volume":"54","author":"K Bush","year":"2010","unstructured":"Bush K, Jacoby GA (2010) Updated functional classification of beta-lactamases. Antimicrob Agents Chemother 54(3):969\u2013976. https:\/\/doi.org\/10.1128\/AAC.01009-09","journal-title":"Antimicrob Agents Chemother"},{"issue":"1036","key":"11020_CR4","doi-asserted-by":"publisher","first-page":"321","DOI":"10.1098\/rstb.1980.0049","volume":"289","author":"RP Ambler","year":"1980","unstructured":"Ambler RP (1980) The structure of beta-lactamases. Philos Trans R Soc Lond B 289(1036):321\u2013331. https:\/\/doi.org\/10.1098\/rstb.1980.0049","journal-title":"Philos Trans R Soc Lond B"},{"issue":"12","key":"11020_CR5","doi-asserted-by":"publisher","first-page":"5046","DOI":"10.1128\/AAC.00774-09","volume":"53","author":"D Yong","year":"2009","unstructured":"Yong D, Toleman MA, Giske CG, Cho HS, Sundman K, Lee K et al (2009) Characterization of a new metallo-beta-lactamase gene, bla(NDM-1), and a novel erythromycin esterase gene carried on a unique genetic structure in Klebsiella pneumoniae sequence type 14 from India. Antimicrob Agents Chemother 53(12):5046\u20135054. https:\/\/doi.org\/10.1128\/AAC.00774-09","journal-title":"Antimicrob Agents Chemother"},{"issue":"12","key":"11020_CR6","doi-asserted-by":"publisher","first-page":"588","DOI":"10.1016\/j.tim.2011.09.005","volume":"19","author":"P Nordmann","year":"2011","unstructured":"Nordmann P, Poirel L, Walsh TR, Livermore DM (2011) The emerging NDM carbapenemases. Trends Microbiol 19(12):588\u2013595. https:\/\/doi.org\/10.1016\/j.tim.2011.09.005","journal-title":"Trends Microbiol"},{"issue":"4","key":"11020_CR7","doi-asserted-by":"publisher","first-page":"2184","DOI":"10.1128\/AAC.05961-11","volume":"56","author":"P Nordmann","year":"2012","unstructured":"Nordmann P, Boulanger AE, Poirel L (2012) NDM-4 metallo-beta-lactamase with increased carbapenemase activity from Escherichia coli. Antimicrob Agents Chemother 56(4):2184\u20132186. https:\/\/doi.org\/10.1128\/AAC.05961-11","journal-title":"Antimicrob Agents Chemother"},{"issue":"2","key":"11020_CR8","doi-asserted-by":"publisher","first-page":"100","DOI":"10.1089\/mdr.2012.0063","volume":"19","author":"BA Rogers","year":"2013","unstructured":"Rogers BA, Sidjabat HE, Silvey A, Anderson TL, Perera S, Li J et al (2013) Treatment options for New Delhi metallo-beta-lactamase-harboring enterobacteriaceae. Microb Drug Resist 19(2):100\u2013103. https:\/\/doi.org\/10.1089\/mdr.2012.0063","journal-title":"Microb Drug Resist"},{"key":"11020_CR9","doi-asserted-by":"publisher","DOI":"10.1021\/acsinfecdis.8b00247","author":"P Linciano","year":"2018","unstructured":"Linciano P, Cendron L, Gianquinto E, Spyrakis F, Tondi D (2018) Ten Years with New Delhi Metallo-beta-lactamase-1 (NDM-1): from structural insights to inhibitor design. ACS Infect Dis. https:\/\/doi.org\/10.1021\/acsinfecdis.8b00247","journal-title":"ACS Infect Dis"},{"issue":"4","key":"11020_CR10","doi-asserted-by":"publisher","first-page":"819","DOI":"10.3390\/ijms20040819","volume":"20","author":"MT Rehman","year":"2019","unstructured":"Rehman MT, AlAjmi MF, Hussain A, Rather GM, Khan MA (2019) High-throughput virtual screening, molecular dynamics simulation, and enzyme kinetics identified ZINC84525623 as a potential inhibitor of NDM-1. Int J Mol Sci 20(4):819. https:\/\/doi.org\/10.3390\/ijms20040819","journal-title":"Int J Mol Sci"},{"key":"11020_CR11","doi-asserted-by":"publisher","DOI":"10.1016\/j.ejmech.2021.113667","volume":"223","author":"T Wang","year":"2021","unstructured":"Wang T, Xu K, Zhao L, Tong R, Xiong L, Shi J (2021) Recent research and development of NDM-1 inhibitors. Eur J Med Chem 223:113667. https:\/\/doi.org\/10.1016\/j.ejmech.2021.113667","journal-title":"Eur J Med Chem"},{"issue":"5","key":"11020_CR12","doi-asserted-by":"publisher","first-page":"384","DOI":"10.1007\/s13238-011-1055-9","volume":"2","author":"Y Guo","year":"2011","unstructured":"Guo Y, Wang J, Niu G, Shui W, Sun Y, Zhou H et al (2011) A structural view of the antibiotic degradation enzyme NDM-1 from a superbug. Protein Cell 2(5):384\u2013394. https:\/\/doi.org\/10.1007\/s13238-011-1055-9","journal-title":"Protein Cell"},{"issue":"1","key":"11020_CR13","doi-asserted-by":"publisher","first-page":"142","DOI":"10.1128\/AAC.01335-15","volume":"60","author":"J Brem","year":"2016","unstructured":"Brem J, van Berkel SS, Zollman D, Lee SY, Gileadi O, McHugh PJ et al (2016) Structural basis of metallo-beta-lactamase inhibition by captopril stereoisomers. Antimicrob Agents Chemother 60(1):142\u2013150. https:\/\/doi.org\/10.1128\/AAC.01335-15","journal-title":"Antimicrob Agents Chemother"},{"issue":"16","key":"11020_CR14","doi-asserted-by":"publisher","first-page":"2785","DOI":"10.1002\/jcc.21256","volume":"30","author":"GM Morris","year":"2009","unstructured":"Morris GM, Huey R, Lindstrom W, Sanner MF, Belew RK, Goodsell DS et al (2009) AutoDock4 and AutoDockTools4: automated docking with selective receptor flexibility. J Comput Chem 30(16):2785\u20132791. https:\/\/doi.org\/10.1002\/jcc.21256","journal-title":"J Comput Chem"},{"key":"11020_CR15","volume-title":"AMBER 2016","author":"DA Case","year":"2016","unstructured":"Case DA, Betz RM, Cerutti DS, Cheatham TE III, Darden TA, Duke RE et al (2016) AMBER 2016. University of California, San Francisco"},{"issue":"36","key":"11020_CR16","doi-asserted-by":"publisher","first-page":"3316","DOI":"10.1021\/acs.biochem.0c00341","volume":"59","author":"M Ahsan","year":"2020","unstructured":"Ahsan M, Pindi C, Senapati S (2020) Electrostatics plays a crucial role in HIV-1 protease substrate binding, drugs fail to take advantage. Biochemistry 59(36):3316\u20133331. https:\/\/doi.org\/10.1021\/acs.biochem.0c00341","journal-title":"Biochemistry"},{"issue":"2","key":"11020_CR17","doi-asserted-by":"publisher","first-page":"926","DOI":"10.1063\/1.445869","volume":"79","author":"WL Jorgensen","year":"1983","unstructured":"Jorgensen WL, Chandrasekhar J, Madura JD, Impey RW, Klein ML (1983) Comparison of simple potential functions for simulating liquid water. J Chem Phys 79(2):926\u2013935. https:\/\/doi.org\/10.1063\/1.445869","journal-title":"J Chem Phys"},{"issue":"19","key":"11020_CR18","doi-asserted-by":"publisher","first-page":"8577","DOI":"10.1063\/1.470117","volume":"103","author":"U Essmann","year":"1995","unstructured":"Essmann U, Perera L, Berkowitz ML, Darden T, Lee H, Pedersen LG (1995) A smooth particle mesh Ewald method. J Chem Phys 103(19):8577\u20138593. https:\/\/doi.org\/10.1063\/1.470117","journal-title":"J Chem Phys"},{"issue":"7","key":"11020_CR19","doi-asserted-by":"publisher","first-page":"2093","DOI":"10.1080\/07391102.2019.1627248","volume":"38","author":"M Rahman","year":"2020","unstructured":"Rahman M, Khan MKA (2020) In silico based unraveling of New Delhi metallo-beta-lactamase (NDM-1) inhibitors from natural compounds: a molecular docking and molecular dynamics simulation study. J Biomol Struct Dyn 38(7):2093\u20132103. https:\/\/doi.org\/10.1080\/07391102.2019.1627248","journal-title":"J Biomol Struct Dyn"},{"issue":"4","key":"11020_CR20","doi-asserted-by":"publisher","first-page":"337","DOI":"10.1016\/j.ddtec.2004.11.007","volume":"1","author":"CA Lipinski","year":"2004","unstructured":"Lipinski CA (2004) Lead- and drug-like compounds: the rule-of-five revolution. Drug Discov Today Technol 1(4):337\u2013341. https:\/\/doi.org\/10.1016\/j.ddtec.2004.11.007","journal-title":"Drug Discov Today Technol"},{"key":"11020_CR21","doi-asserted-by":"publisher","DOI":"10.3389\/fphar.2020.599959","volume":"11","author":"B Salehi","year":"2020","unstructured":"Salehi B, Quispe C, Sharifi-Rad J, Cruz-Martins N, Nigam M, Mishra AP et al (2020) Phytosterols: from preclinical evidence to potential clinical applications. Front Pharmacol 11:599959. https:\/\/doi.org\/10.3389\/fphar.2020.599959","journal-title":"Front Pharmacol"},{"key":"11020_CR22","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1007\/978-1-61779-012-6_1","volume":"716","author":"YT Tang","year":"2011","unstructured":"Tang YT, Marshall GR (2011) Virtual screening for lead discovery. Methods Mol Biol 716:1\u201322. https:\/\/doi.org\/10.1007\/978-1-61779-012-6_1","journal-title":"Methods Mol Biol"},{"issue":"11","key":"11020_CR23","doi-asserted-by":"publisher","first-page":"10","DOI":"10.1128\/AAC.01579-18","volume":"62","author":"H Zhang","year":"2018","unstructured":"Zhang H, Ma G, Zhu Y, Zeng L, Ahmad A, Wang C et al (2018) Active-site conformational fluctuations promote the enzymatic activity of NDM-1. Antimicrob Agents Chemother 62(11):10\u20131128. https:\/\/doi.org\/10.1128\/AAC.01579-18","journal-title":"Antimicrob Agents Chemother"},{"issue":"9","key":"11020_CR24","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0024621","volume":"6","author":"Y Kim","year":"2011","unstructured":"Kim Y, Tesar C, Mire J, Jedrzejczak R, Binkowski A, Babnigg G et al (2011) Structure of apo- and monometalated forms of NDM-1\u2013a highly potent carbapenem-hydrolyzing metallo-beta-lactamase. PLoS ONE 6(9):e24621. https:\/\/doi.org\/10.1371\/journal.pone.0024621","journal-title":"PLoS ONE"},{"issue":"9","key":"11020_CR25","doi-asserted-by":"publisher","first-page":"1484","DOI":"10.1002\/pro.697","volume":"20","author":"D King","year":"2011","unstructured":"King D, Strynadka N (2011) Crystal structure of New Delhi metallo-beta-lactamase reveals molecular basis for antibiotic resistance. Protein Sci 20(9):1484\u20131491. https:\/\/doi.org\/10.1002\/pro.697","journal-title":"Protein Sci"},{"issue":"8","key":"11020_CR26","doi-asserted-by":"publisher","first-page":"2574","DOI":"10.1096\/fj.11-184036","volume":"25","author":"H Zhang","year":"2011","unstructured":"Zhang H, Hao Q (2011) Crystal structure of NDM-1 reveals a common beta-lactam hydrolysis mechanism. FASEB J 25(8):2574\u20132582. https:\/\/doi.org\/10.1096\/fj.11-184036","journal-title":"FASEB J"},{"issue":"5","key":"11020_CR27","doi-asserted-by":"publisher","first-page":"445","DOI":"10.1007\/s00249-016-1188-0","volume":"46","author":"L Karami","year":"2017","unstructured":"Karami L, Saboury AA, Rezaee E, Tabatabai SA (2017) Investigation of the binding mode of 1, 3, 4-oxadiazole derivatives as amide-based inhibitors for soluble epoxide hydrolase (sEH) by molecular docking and MM-GBSA. Eur Biophys J 46(5):445\u2013459. https:\/\/doi.org\/10.1007\/s00249-016-1188-0","journal-title":"Eur Biophys J"},{"issue":"1","key":"11020_CR28","doi-asserted-by":"publisher","first-page":"78","DOI":"10.1080\/07391102.2019.1568306","volume":"38","author":"S Sadeghi-Kaji","year":"2020","unstructured":"Sadeghi-Kaji S, Shareghi B, Saboury AA, Farhadian S (2020) Spermine as a porcine pancreatic elastase activator: spectroscopic and molecular simulation studies. J Biomol Struct Dyn 38(1):78\u201388. https:\/\/doi.org\/10.1080\/07391102.2019.1568306","journal-title":"J Biomol Struct Dyn"},{"key":"11020_CR29","volume-title":"Phytosterols as functional food components and nutraceuticals. Nutraceutical science and technology series","author":"PC Dutta","year":"2004","unstructured":"Dutta PC (2004) Phytosterols as functional food components and nutraceuticals. Nutraceutical science and technology series. Marcel Dekker, New York"}],"container-title":["Molecular Diversity"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s11030-024-11020-6.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s11030-024-11020-6\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s11030-024-11020-6.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,9,24]],"date-time":"2025-09-24T13:12:43Z","timestamp":1758719563000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s11030-024-11020-6"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,11,8]]},"references-count":29,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2025,10]]}},"alternative-id":["11020"],"URL":"https:\/\/doi.org\/10.1007\/s11030-024-11020-6","relation":{},"ISSN":["1381-1991","1573-501X"],"issn-type":[{"type":"print","value":"1381-1991"},{"type":"electronic","value":"1573-501X"}],"subject":[],"published":{"date-parts":[[2024,11,8]]},"assertion":[{"value":"23 August 2024","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"14 October 2024","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"8 November 2024","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"The authors declare no competing interests.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Conflict of interest"}}]}}