{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,16]],"date-time":"2026-07-16T12:09:14Z","timestamp":1784203754524,"version":"3.55.0"},"reference-count":123,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,7,1]],"date-time":"2026-07-01T00:00:00Z","timestamp":1782864000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,7,1]],"date-time":"2026-07-01T00:00:00Z","timestamp":1782864000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,5,14]],"date-time":"2026-05-14T00:00:00Z","timestamp":1778716800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/100007675","name":"International Center for Genetic Engineering and Biotechnology","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100007675","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001411","name":"Indian Council of Medical Research","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001411","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001688","name":"International Centre for Genetic Engineering and Biotechnology","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001688","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100008605","name":"Indian National Science Academy","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100008605","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100012306","name":"Universit\u00e0 degli Studi di Trieste","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100012306","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100016281","name":"Sharda University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100016281","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100014836","name":"AICS","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100014836","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["clinicalkey.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Microbiological Methods"],"published-print":{"date-parts":[[2026,7]]},"DOI":"10.1016\/j.mimet.2026.107549","type":"journal-article","created":{"date-parts":[[2026,5,12]],"date-time":"2026-05-12T23:08:53Z","timestamp":1778627333000},"page":"107549","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"special_numbering":"C","title":["Exploiting selected Mur enzyme characteristics for antibacterial drug design"],"prefix":"10.1016","volume":"246","author":[{"given":"Gizachew Muluneh","family":"Amera","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Giulia","family":"Canarutto","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Monika","family":"Jain","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rashmi Prabha","family":"Singh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gedefaw","family":"Wubie","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mussa","family":"Adal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jayaraman","family":"Muthukumaran","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Amit Kumar","family":"Singh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Silvano","family":"Piazza","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.mimet.2026.107549_bb0005","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1016\/j.jmgm.2017.07.024","article-title":"Binding mode analysis, dynamic simulation and binding free energy calculations of the MurF ligase from Acinetobacter baumannii","volume":"77","author":"Ahmad","year":"2017","journal-title":"J. Mol. Graph. Model."},{"key":"10.1016\/j.mimet.2026.107549_bb0010","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/j.molliq.2019.02.051","article-title":"Blocking the catalytic mechanism of MurC ligase enzyme from Acinetobacter baumannii: An in silico guided study towards the discovery of natural antibiotics","volume":"281","author":"Ahmad","year":"2019","journal-title":"J. Mol. Liq."},{"key":"10.1016\/j.mimet.2026.107549_bb0015","doi-asserted-by":"crossref","first-page":"8919","DOI":"10.1021\/bi8006274","article-title":"Active site mapping of MraY, a member of the Polyprenyl-phosphate N-Acetylhexosamine 1-phosphate transferase superfamily, catalyzing the first membrane step of peptidoglycan biosynthesis","volume":"47","author":"Al-Dabbagh","year":"2008","journal-title":"Biochemistry"},{"key":"10.1016\/j.mimet.2026.107549_bb0025","doi-asserted-by":"crossref","first-page":"3389","DOI":"10.1093\/nar\/25.17.3389","article-title":"Gapped BLAST and PSI-BLAST: A New Generation of Protein Database Search","volume":"25","author":"Altschul","year":"1997","journal-title":"Programs. Nucleic Acids Res."},{"key":"10.1016\/j.mimet.2026.107549_bb0030","doi-asserted-by":"crossref","DOI":"10.1016\/j.imu.2019.100216","article-title":"Structure based in-silico study on UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-2,6-diaminopimelate ligase (MurE) from Acinetobacter baumannii as a drug target against nosocomial infections","volume":"16","author":"Amera","year":"2019","journal-title":"Inform Med Unlocked"},{"key":"10.1016\/j.mimet.2026.107549_bb0035","first-page":"18","article-title":"Prioritization of Mur family drug targets against a. baumannii and identification of their homologous proteins through molecular phylogeny, primary sequence, and structural analysis","author":"Amera","year":"2020","journal-title":"J. Genetic Eng. Biotechnol."},{"key":"10.1016\/j.mimet.2026.107549_bb0040","first-page":"100","article-title":"Structure based drug designing and discovery of promising lead molecules against UDP-N-acetylenolpyruvoylglucosamine reductase (MurB): a potential drug target in multi-drug resistant Acinetobacter baumannii","author":"Amera","year":"2020","journal-title":"J. Mol. Graph. Model."},{"key":"10.1016\/j.mimet.2026.107549_bb0045","doi-asserted-by":"crossref","first-page":"5230","DOI":"10.1080\/07391102.2019.1700167","article-title":"Screening of promising molecules against MurG as drug target in multi-drug-resistant-Acinetobacter baumannii - insights from comparative protein modeling, molecular docking and molecular dynamics simulation","volume":"38","author":"Amera","year":"2020","journal-title":"J. Biomol. Struct. Dyn."},{"key":"10.1016\/j.mimet.2026.107549_bb0050","doi-asserted-by":"crossref","DOI":"10.1016\/j.micpath.2020.104205","article-title":"Computer aided ligand based screening for identification of promising molecules against enzymes involved in peptidoglycan biosynthetic pathway from Acinetobacter baumannii","volume":"147","author":"Amera","year":"2020","journal-title":"Microb. Pathog."},{"key":"10.1016\/j.mimet.2026.107549_bb0055","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/j.compbiolchem.2017.05.004","article-title":"Extra precision docking, free energy calculation and molecular dynamics studies on glutamic acid derivatives as MurD inhibitors","volume":"69","author":"Azam","year":"2017","journal-title":"Comput. Biol. Chem."},{"key":"10.1016\/j.mimet.2026.107549_bb0060","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1111\/j.1574-6976.2008.00104.x","article-title":"Cytoplasmic steps of peptidoglycan biosynthesis","volume":"32","author":"Barreteau","year":"2008","journal-title":"FEMS Microbiol. Rev."},{"key":"10.1016\/j.mimet.2026.107549_bb0065","doi-asserted-by":"crossref","first-page":"1011","DOI":"10.1007\/s13238-010-0132-9","article-title":"Essential residues for the enzyme activity of ATP-dependent MurE ligase from mycobacterium tuberculosis","volume":"1","author":"Basavannacharya","year":"2010","journal-title":"Protein Cell"},{"key":"10.1016\/j.mimet.2026.107549_bb0070","doi-asserted-by":"crossref","first-page":"254","DOI":"10.1016\/j.jprot.2016.11.005","article-title":"A glimpse into the modulation of post-translational modifications of human-colonizing bacteria","volume":"152","author":"Bastos","year":"2017","journal-title":"J. Proteomics"},{"key":"10.1016\/j.mimet.2026.107549_bb0075","doi-asserted-by":"crossref","first-page":"4420","DOI":"10.1128\/AAC.00845-07","article-title":"A MurF inhibitor that disrupts cell wall biosynthesis in Escherichia coli","volume":"51","author":"Baum","year":"2007","journal-title":"Antimicrob. Agents Chemother"},{"key":"10.1016\/j.mimet.2026.107549_bb0080","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/S0969-2126(96)00008-1","article-title":"The structure of the substrate-free form of MurB, an essential enzyme for the synthesis of bacterial cell walls","volume":"4","author":"Benson","year":"1996","journal-title":"Structure"},{"key":"10.1016\/j.mimet.2026.107549_bb0085","doi-asserted-by":"crossref","first-page":"3416","DOI":"10.1093\/emboj\/16.12.3416","article-title":"Crystal structure of UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase from Escherichia coli and D-alanine:D-alanine ligase (DD-ligase) from E.Coli","volume":"16","author":"Bertrand","year":"1997","journal-title":"The EMBO Journal"},{"key":"10.1016\/j.mimet.2026.107549_bb0090","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1006\/jmbi.1999.2800","article-title":"Determination of the MurD Mechanism Through Crystallographic Analysis of Enzyme Complexes","volume":"289","author":"Bertrand","year":"1999","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.mimet.2026.107549_bb0095","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1002\/prot.24167","article-title":"3Drefine: consistent protein structure refinement by optimizing hydrogen bonding network and atomic-level energy minimization","volume":"81","author":"Bhattacharya","year":"2013","journal-title":"Proteins: Struct. Funct. Bioinformat."},{"key":"10.1016\/j.mimet.2026.107549_bb0100","doi-asserted-by":"crossref","first-page":"11556","DOI":"10.1021\/bi970797f","article-title":"Invariant Amino Acids in the Mur Peptide Synthetases of Bacterial Peptidoglycan Synthesis and their Modification by Site-Directed Mutagenesis in the UDP-MurNAc:L-Alanine Ligase from Escherichia coli","volume":"36","author":"Bouhss","year":"1997","journal-title":".Biochemistry"},{"key":"10.1016\/j.mimet.2026.107549_bb0105","doi-asserted-by":"crossref","first-page":"576","DOI":"10.1046\/j.1365-2958.1999.01623.x","article-title":"Topological analysis of the MraY protein catalysing the first membrane step of peptidoglycan synthesis","volume":"34","author":"Bouhss","year":"1999","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.mimet.2026.107549_bb0110","doi-asserted-by":"crossref","first-page":"29974","DOI":"10.1074\/jbc.M314165200","article-title":"Purification and characterization of the bacterial MraY translocase catalyzing the first membrane step of peptidoglycan biosynthesis","volume":"279","author":"Bouhss","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mimet.2026.107549_bb0115","doi-asserted-by":"crossref","first-page":"873","DOI":"10.1016\/S0960-894X(02)01076-4","article-title":"Discovery of the first antibacterial small molecule inhibitors of MurB","volume":"13","author":"Bronson","year":"2003","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.mimet.2026.107549_bb0120","doi-asserted-by":"crossref","first-page":"85","DOI":"10.2174\/187152606784112128","article-title":"Phospho-MurNAc-Pentapeptide translocase (MraY) as a target for antibacterial agents and antibacterial proteins","volume":"6","author":"Bugg","year":"2006","journal-title":"Infectious disorders drug targets"},{"key":"10.1016\/j.mimet.2026.107549_bb0125","doi-asserted-by":"crossref","first-page":"6340","DOI":"10.1016\/j.bmc.2016.03.018","article-title":"Inhibition of phospho-MurNAc-pentapeptide translocase (MraY) by nucleoside natural product antibiotics, bacteriophage \u03c6X174 lysis protein E, and cationic antibacterial peptides","volume":"24","author":"Bugg","year":"2016","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.mimet.2026.107549_bb0130","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/j.jprot.2013.08.012","article-title":"Beyond gene expression: the impact of protein post-translational modifications in bacteria","volume":"97","author":"Cain","year":"2014","journal-title":"J. Proteomics"},{"key":"10.1016\/j.mimet.2026.107549_bb0135","doi-asserted-by":"crossref","first-page":"1045","DOI":"10.1016\/j.bbrc.2014.06.108","article-title":"ATP-binding mode including a carbamoylated lysine and two Mg2+ ions, and substrate-binding mode in Acinetobacter baumannii MurF","volume":"450","author":"Cha","year":"2014","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.mimet.2026.107549_bb0145","doi-asserted-by":"crossref","first-page":"e40155","DOI":"10.1371\/journal.pone.0040155","article-title":"GlycoPP: a webserver for prediction of N- and O-glycosites in prokaryotic protein sequences","volume":"7","author":"Chauhan","year":"2012","journal-title":"PloS One"},{"key":"10.1016\/j.mimet.2026.107549_bb0150","article-title":"Substrate Channel flexibility in Pseudomonas aeruginosa MurB accommodates two distinct substrates","volume":"8","author":"Chen","year":"2013","journal-title":"PloS One"},{"key":"10.1016\/j.mimet.2026.107549_bb0160","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1038\/nature17636","article-title":"Structural insights into inhibition of lipid i production in bacterial cell wall synthesis","volume":"533","author":"Chung","year":"2016","journal-title":"Nature"},{"key":"10.1016\/j.mimet.2026.107549_bb0155","first-page":"1012","article-title":"Crystal structure of MraY, an essential membrane enzyme for bacterial cell wall synthesis","author":"Chung","year":"2013","journal-title":"Science 341,"},{"key":"10.1016\/j.mimet.2026.107549_bb0165","doi-asserted-by":"crossref","first-page":"7693","DOI":"10.1021\/bi060652l","article-title":"Dynamic coupling and allosteric behavior in a nonallosteric protein","volume":"45","author":"Clarkson","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.mimet.2026.107549_bb0170","doi-asserted-by":"crossref","first-page":"1511","DOI":"10.1002\/pro.5560020916","article-title":"Verification of protein structures: patterns of nonbonded atomic interactions","volume":"2","author":"Colovos","year":"1993","journal-title":"Protein Sci."},{"key":"10.1016\/j.mimet.2026.107549_bb0175","doi-asserted-by":"crossref","first-page":"D523","DOI":"10.1093\/nar\/gkac1052","article-title":"UniProt: the universal protein knowledgebase in 2023","volume":"51","author":"Consortium TU","year":"2023","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.mimet.2026.107549_bb0180","doi-asserted-by":"crossref","first-page":"617","DOI":"10.1002\/cbic.200800678","article-title":"Specific labeling of peptidoglycan precursors as a tool for bacterial Cell Wall studies","volume":"10","author":"van Dam","year":"2009","journal-title":"ChemBioChem"},{"key":"10.1016\/j.mimet.2026.107549_bb0185","doi-asserted-by":"crossref","DOI":"10.1099\/00221287-145-11-3177","article-title":"Alteration of a single amino acid residue reverses fosfomycin resistance of recombinant MurA from mycobacterium tuberculosis","author":"De Smet","year":"1999","journal-title":"Microbiology"},{"key":"10.1016\/j.mimet.2026.107549_bb0195","doi-asserted-by":"crossref","first-page":"2051","DOI":"10.3389\/fmicb.2019.02051","article-title":"Editorial: bacterial Cell Wall structure and dynamics","volume":"10","author":"D\u00f6rr","year":"2019","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.mimet.2026.107549_bb0200","doi-asserted-by":"crossref","first-page":"4735","DOI":"10.1073\/pnas.1523573113","article-title":"Dynamical network of residue-residue contacts reveals coupled allosteric effects in recognition, catalysis, and mutation","volume":"113","author":"Doshi","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.mimet.2026.107549_bb0205","doi-asserted-by":"crossref","first-page":"1098","DOI":"10.1021\/ar500351b","article-title":"Fluctuations within folded proteins: implications for thermodynamic and allosteric regulation","volume":"48","author":"DuBay","year":"2015","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.mimet.2026.107549_bb0210","doi-asserted-by":"crossref","first-page":"7264","DOI":"10.1021\/bi970266r","article-title":"Evaluation of the kinetic mechanism of Escherichia coli uridine diphosphate-N-acetylmuramate:l-alanine ligase","volume":"36","author":"Emanuele","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/j.mimet.2026.107549_bb0215","doi-asserted-by":"crossref","first-page":"2399","DOI":"10.1080\/07391102.2015.1117397","article-title":"A comparative modeling and molecular docking study on mycobacterium tuberculosis targets involved in peptidoglycan biosynthesis","volume":"34","author":"Fakhar","year":"2016","journal-title":"J. Biomol. Struct. Dyn."},{"key":"10.1016\/j.mimet.2026.107549_bb0220","doi-asserted-by":"crossref","first-page":"3218","DOI":"10.1111\/1462-2920.12171","article-title":"MreB and MurG as scaffolds for the cytoplasmic steps of peptidoglycan biosynthesis","volume":"15","author":"Favini-Stabile","year":"2013","journal-title":"Environ. Microbiol."},{"key":"10.1016\/j.mimet.2026.107549_bb0225","doi-asserted-by":"crossref","first-page":"36553","DOI":"10.1074\/jbc.M807175200","article-title":"The MurC ligase essential for peptidoglycan biosynthesis is regulated by the serine\/threonine protein kinase PknA in Corynebacterium glutamicum","volume":"283","author":"Fiuza","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mimet.2026.107549_bb0235","article-title":"Arming the Troops: Post-Translational Modification of Extracellular Bacterial Proteins","volume":"103","author":"Forrest","year":"2020","journal-title":"Sci\u00a0 Prog."},{"key":"10.1016\/j.mimet.2026.107549_bb0240","series-title":"Protein Identification and Analysis Tools on the ExPASy Server. In: Walker JM, editor. The Proteomics Protocols Handbook [Internet]","first-page":"571","author":"Gasteiger","year":"2005"},{"key":"10.1016\/j.mimet.2026.107549_bb0245","doi-asserted-by":"crossref","DOI":"10.1016\/j.crphar.2022.100137","article-title":"Recent developments on UDP-N-acetylmuramoyl-L-alanine-D-gutamate ligase (Mur D) enzyme for antimicrobial drug development: An emphasis on in-silico approaches","author":"Gaur","year":"2022","journal-title":"Curr. Res. Pharmacol. Drug Disc. Elsevier B.V."},{"key":"10.1016\/j.mimet.2026.107549_bb0255","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1016\/j.sbi.2006.02.003","article-title":"Comparative modeling for protein structure prediction","author":"Ginalski","year":"2006","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.mimet.2026.107549_bb0260","doi-asserted-by":"crossref","first-page":"500","DOI":"10.3389\/fmicb.2015.00500","article-title":"Regulatory potential of post-translational modifications in bacteria","volume":"6","author":"Grangeasse","year":"2015","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.mimet.2026.107549_bb0265","doi-asserted-by":"crossref","first-page":"2101","DOI":"10.1093\/jac\/dkq313","article-title":"Anti-tubercular screening of natural products from Colombian plants: 3-methoxynordomesticine, an inhibitor of MurE ligase of mycobacterium tuberculosis","volume":"65","author":"Guzman","year":"2010","journal-title":"J. Antimicrobial Chemotherapy."},{"key":"10.1016\/j.mimet.2026.107549_bb0270","doi-asserted-by":"crossref","first-page":"1045","DOI":"10.1110\/ps.9.6.1045","article-title":"The 1.9 \u00c5 crystal structure of Escherichia coli MurG, a membrane-associated glycosyltransferase involved in peptidoglycan biosynthesis","volume":"9","author":"Ha","year":"2000","journal-title":"Protein Sci."},{"key":"10.1016\/j.mimet.2026.107549_bb0520","doi-asserted-by":"crossref","first-page":"1045","DOI":"10.1110\/ps.9.6.1045","article-title":"The 1.9 A crystal structure of Escherichia coli MurG, a membrane-associated glycosyltransferase involved in peptidoglycan biosynthesis","volume":"9","author":"Ha","year":"2000","journal-title":"Protein Sci."},{"key":"10.1016\/j.mimet.2026.107549_bb0275","first-page":"9,","article-title":"Computational identification of microbial phosphorylation sites by the enhanced characteristics of sequence information","author":"Hasan","year":"2019","journal-title":"Sci. Rep."},{"key":"10.1016\/j.mimet.2026.107549_bb0280","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1039\/a804532a","article-title":"Recent advances in the formation of the bacterial peptidoglycan monomer unit","volume":"18","author":"van Heijenoort","year":"2001","journal-title":"Nat. Prod. Rep."},{"key":"10.1016\/j.mimet.2026.107549_bb0285","doi-asserted-by":"crossref","first-page":"11168","DOI":"10.1021\/ja036494s","article-title":"Identification of active-site inhibitors of MurG using a generalizable, high-throughput glycosyltransferase screen","volume":"125","author":"Helm","year":"2003","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.mimet.2026.107549_bb0290","doi-asserted-by":"crossref","first-page":"964","DOI":"10.1038\/nature06522","article-title":"Dynamic Personalities of Proteins","volume":"450","author":"Henzler-Wildman","year":"2007","journal-title":"Nature"},{"key":"10.1016\/j.mimet.2026.107549_bb0295","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1016\/j.bioorg.2014.03.008","article-title":"Inhibitors of the peptidoglycan biosynthesis enzymes MurA-F","volume":"55","author":"Hrast","year":"2014","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.mimet.2026.107549_bb0300","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1016\/j.chembiol.2004.02.024","article-title":"Identification of selective inhibitors for the glycosyltransferase MurG via high-throughput screening","volume":"11","author":"Hu","year":"2004","journal-title":"Chem. Biol."},{"key":"10.1016\/j.mimet.2026.107549_bb0305","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1016\/j.compbiolchem.2018.11.002","article-title":"Homology modeling and molecular dynamic simulation of UDP-N-acetylmuramoyl-L-alanine-D-glutamate ligase (MurD) from mycobacterium tuberculosis H37Rv using in silico approach","volume":"78","author":"Isa","year":"2019","journal-title":"Comput. Biol. Chem."},{"key":"10.1016\/j.mimet.2026.107549_bb0020","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1016\/j.imu.2018.06.007","article-title":"Molecular modelling and dynamic simulation of UDP-N-acetylglucosamine 1-carboxyvinyltransferase (MurA) from mycobacterium tuberculosis using in silico approach","volume":"12","author":"Isa","year":"2018","journal-title":"Inform Med Unlocked."},{"key":"10.1016\/j.mimet.2026.107549_bb0310","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1007\/s00894-020-04557-4","article-title":"Identification of promising molecules against MurD ligase from Acinetobacter baumannii: insights from comparative protein modelling, virtual screening, molecular dynamics simulations and MM\/PBSA analysis","volume":"26","author":"Jha","year":"2020","journal-title":"J. Mol. Model."},{"key":"10.1016\/j.mimet.2026.107549_bb0315","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1002\/1873-3468.14007","article-title":"Wide-open conformation of UDP-MurNAc-tripeptide ligase revealed by the substrate-free structure of MurE from Acinetobacter baumannii","volume":"595","author":"Jung","year":"2021","journal-title":"FEBS Lett."},{"key":"10.1016\/j.mimet.2026.107549_bb0320","doi-asserted-by":"crossref","first-page":"574","DOI":"10.1107\/S2052252521003729","article-title":"Putative hexameric glycosyltransferase functional unit revealed by the crystal structure of Acinetobacter baumannii MurG","volume":"8","author":"Jung","year":"2021","journal-title":"IUCrJ."},{"key":"10.1016\/j.mimet.2026.107549_bb0325","doi-asserted-by":"crossref","first-page":"4923","DOI":"10.1021\/bi952937w","article-title":"Characterization of a Cys115 to asp substitution in the Escherichia coli Cell Wall biosynthetic enzyme UDP-GlcNAc Enolpyruvyl transferase (MurA) that confers resistance to inactivation by the antibiotic Fosfomycin","volume":"35","author":"Kim","year":"1996","journal-title":"Biochemistry"},{"key":"10.1016\/j.mimet.2026.107549_bb0330","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/j.jmb.2007.04.048","article-title":"Structural and functional characterization of enantiomeric glutamic acid derivatives as potential transition state analogue inhibitors of MurD ligase","volume":"370","author":"Kotnik","year":"2007","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.mimet.2026.107549_bb0340","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1111\/mmi.12758","article-title":"The biology of Mur ligases as an antibacterial target","author":"Kouidmi","year":"2014","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.mimet.2026.107549_bb0345","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1002\/prot.22570","article-title":"Improving physical realism, stereochemistry, and side-chain accuracy in homology modeling: four approaches that performed well in CASP8","author":"Krieger","year":"2009","journal-title":"Proteins: Struct., Funct., Bioinf"},{"key":"10.1016\/j.mimet.2026.107549_bb0350","doi-asserted-by":"crossref","first-page":"8996","DOI":"10.1080\/07391102.2024.2325661","article-title":"In silico strategies for identifying therapeutic candidates against Acinetobacter baumannii: spotlight on the UDP-N-acetylmuramoyl-L-alanine-D-glutamate:meso-diaminopimelate ligase (MurE)","volume":"43","author":"Kumar","year":"2025","journal-title":"J. Biomol. Struct. Dyn."},{"key":"10.1016\/j.mimet.2026.107549_bb0355","doi-asserted-by":"crossref","first-page":"1547","DOI":"10.1093\/molbev\/msy096","article-title":"MEGA X: molecular evolutionary genetics analysis across computing platforms","volume":"35","author":"Kumar","year":"2018","journal-title":"Mol. Biol. Evol."},{"key":"10.1016\/j.mimet.2026.107549_bb0360","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1002\/pro.3289","article-title":"PDBsum: structural summaries of PDB entries","volume":"27","author":"Laskowski","year":"2018","journal-title":"Protein Sci."},{"key":"10.1016\/j.mimet.2026.107549_bb0365","doi-asserted-by":"crossref","first-page":"818","DOI":"10.1016\/j.bbrc.2006.08.199","article-title":"Prediction of N\u03b5-acetylation on internal lysines implemented in Bayesian discriminant method","volume":"350","author":"Li","year":"2006","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.mimet.2026.107549_bb0370","doi-asserted-by":"crossref","first-page":"D912","DOI":"10.1093\/nar\/gkab1107","article-title":"VFDB 2022: a general classification scheme for bacterial virulence factors","volume":"50","author":"Liu","year":"2022","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/j.mimet.2026.107549_bb0375","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1002\/cbic.200300557","article-title":"Acceptor specificity and inhibition of the bacterial Cell-Wall glycosyltransferase MurG","volume":"4","author":"Liu","year":"2003","journal-title":"ChemBioChem"},{"key":"10.1016\/j.mimet.2026.107549_bb0380","doi-asserted-by":"crossref","first-page":"28","DOI":"10.3390\/antibiotics5030028","article-title":"The membrane steps of bacterial cell wall synthesis as antibiotic targets","volume":"5","author":"Liu","year":"2016","journal-title":"Antibiotics"},{"key":"10.1016\/j.mimet.2026.107549_bb0385","doi-asserted-by":"crossref","first-page":"1747","DOI":"10.1128\/JB.186.6.1747-1757.2004","article-title":"Phospho-N-acetyl-Muramyl-Pentapeptide translocase from Escherichia coli: catalytic role of conserved aspartic acid residues","volume":"186","author":"Lloyd","year":"2004","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.mimet.2026.107549_bb0390","doi-asserted-by":"crossref","first-page":"D677","DOI":"10.1093\/nar\/gkaa917","article-title":"DEG 15, an update of the database of essential genes that includes built-in analysis tools","volume":"49","author":"Luo","year":"2021","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/j.mimet.2026.107549_bb0395","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1038\/356083a0","article-title":"Assessment of protein models with three-dimensional profiles","volume":"356","author":"L\u00fcthy","year":"1992","journal-title":"Nature"},{"key":"10.1016\/j.mimet.2026.107549_bb0400","doi-asserted-by":"crossref","first-page":"784923","DOI":"10.3389\/fmicb.2021.784923","article-title":"Post-translational modifications in Oral Bacteria and their functional impact","volume":"12","author":"Ma","year":"2021","journal-title":"Front. Microbiol"},{"key":"10.1016\/j.mimet.2026.107549_bb0405","doi-asserted-by":"crossref","first-page":"W521","DOI":"10.1093\/nar\/gkae241","article-title":"The EMBL-EBI job dispatcher sequence analysis tools framework in 2024","volume":"52","author":"Madeira","year":"2024","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.mimet.2026.107549_bb0410","doi-asserted-by":"crossref","first-page":"1414","DOI":"10.1002\/cmdc.200700094","article-title":"Naphthyl tetronic acids as multi-target inhibitors of bacterial peptidoglycan biosynthesis","volume":"2","author":"Mansour","year":"2007","journal-title":"ChemMedChem"},{"key":"10.1016\/j.mimet.2026.107549_bb0415","doi-asserted-by":"crossref","first-page":"12207","DOI":"10.1021\/bi015567m","article-title":"Biochemical characterization of a Phosphinate inhibitor of Escherichia coli MurC","volume":"40","author":"Marmor","year":"2001","journal-title":"Biochemistry"},{"key":"10.1016\/j.mimet.2026.107549_bb0420","doi-asserted-by":"crossref","first-page":"10646","DOI":"10.1021\/bi00201a011","article-title":"Kinetics, stoichiometry, and identification of the reactive thiolate in the inactivation of UDP-GlcNAc Enolpyruvoyl transferase by the antibiotic Fosfomycin","volume":"33","author":"Marquardt","year":"1994","journal-title":"Biochemistry"},{"key":"10.1016\/j.mimet.2026.107549_bb0425","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1016\/j.sbi.2010.09.014","article-title":"Bridging cell wall biosynthesis and bacterial morphogenesis","author":"Matte\u00ef","year":"2010","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.mimet.2026.107549_bb0430","doi-asserted-by":"crossref","first-page":"580","DOI":"10.1016\/j.coph.2009.08.004","article-title":"Novel trends in high-throughput screening","volume":"9","author":"Mayr","year":"2009","journal-title":"Curr. Opin. Pharmacol."},{"key":"10.1016\/j.mimet.2026.107549_bb0435","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1016\/j.cobme.2019.08.007","article-title":"Single-molecule FRET methods to study the dynamics of proteins at work","volume":"12","author":"Mazal","year":"2019","journal-title":"Curr. Opin. Biomed. Eng."},{"key":"10.1016\/j.mimet.2026.107549_bb0440","doi-asserted-by":"crossref","first-page":"1218","DOI":"10.1128\/JB.185.4.1218-1228.2003","article-title":"In vitro and in vivo functional activity of Chlamydia MurA, a UDP-N-acetylglucosamine enolpyruvyl transferase involved in peptidoglycan synthesis and fosfomycin resistance","volume":"185","author":"McCoy","year":"2003","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.mimet.2026.107549_bb0445","doi-asserted-by":"crossref","first-page":"17909","DOI":"10.1073\/pnas.0608643103","article-title":"L,L-diaminopimelate aminotransferase, a trans-kingdom enzyme shared by Chlamydia and plants for synthesis of diaminopimelate\/lysine","volume":"103","author":"Mccoy","year":"2006","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.mimet.2026.107549_bb0450","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0066458","article-title":"Biochemical characterization of UDP-N-acetylmuramoyl-L-alanyl-D-glutamate: Meso-2,6-diaminopimelate ligase (MurE) from Verrucomicrobium spinosum DSM 4136T","volume":"8","author":"McGroty","year":"2013","journal-title":"PloS One"},{"key":"10.1016\/j.mimet.2026.107549_bb0455","doi-asserted-by":"crossref","first-page":"4566","DOI":"10.1016\/j.bmc.2014.07.035","article-title":"Identification of novel inhibitors of phospho-MurNAc-pentapeptide translocase MraY from library screening: Isoquinoline alkaloid michellamine B and xanthene dye phloxine B","volume":"22","author":"Mihalyi","year":"2014","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.mimet.2026.107549_bb0460","first-page":"131","article-title":"Aminoalkylphosphinate inhibitors of D-ala-D-ala adding enzyme","volume":"1","author":"Miller","year":"2010","journal-title":"J. Chem. Soc., Perkin Trans."},{"key":"10.1016\/j.mimet.2026.107549_bb0465","doi-asserted-by":"crossref","first-page":"2566","DOI":"10.1093\/jac\/dkq349","article-title":"Benzothioxalone derivatives as novel inhibitors of UDP-N-acetylglucosamine enolpyruvyl transferases (MurA and MurZ)","volume":"65","author":"Miller","year":"2010","journal-title":"J. Antimicrob. Chemother."},{"key":"10.1016\/j.mimet.2026.107549_bb0470","doi-asserted-by":"crossref","first-page":"4152","DOI":"10.1128\/JB.185.14.4152-4162.2003","article-title":"Crystal structures of active fully assembled substrate- and product-bound complexes of UDP-N-acetylmuramic acid:L-alanine ligase (MurC) from Haemophilus influenzae","volume":"185","author":"Mol","year":"2003","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.mimet.2026.107549_bb0480","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/j.tube.2015.01.006","article-title":"Structural and functional features of enzymes of Mycobacterium tuberculosis peptidoglycan biosynthesis as targets for drug development","volume":"95","author":"Moraes","year":"2015","journal-title":"Tuberculosis"},{"key":"10.1016\/j.mimet.2026.107549_bb0485","doi-asserted-by":"crossref","first-page":"362","DOI":"10.3389\/fmicb.2016.00362","article-title":"Identification and partial characterization of a novel UDP-N-acetylenolpyruvoylglucosamine reductase\/UDP-N-acetylmuramate: L-alanine ligase fusion enzyme from Verrucomicrobium spinosum DSM 4136(T)","volume":"7","author":"Naqvi","year":"2016","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.mimet.2026.107549_bb0490","doi-asserted-by":"crossref","first-page":"4294","DOI":"10.1093\/nar\/29.21.4294","article-title":"On the molecular discrimination between adenine and guanine by proteins","volume":"29","author":"Nobeli","year":"2001","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/j.mimet.2026.107549_bb0495","doi-asserted-by":"crossref","first-page":"eadg9091","DOI":"10.1126\/science.adg9091","article-title":"The mechanism of the phage-encoded protein antibiotic from \u03a6X174","volume":"381","author":"Orta","year":"2023","journal-title":"Science"},{"key":"10.1016\/j.mimet.2026.107549_bb0500","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1042\/BJ20081395","article-title":"Pseudomonas aeruginosa MurE amide ligase: enzyme kinetics and peptide inhibitor","volume":"421","author":"Paradis-Bleau","year":"2009","journal-title":"Biochem. J."},{"key":"10.1016\/j.mimet.2026.107549_bb0505","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1007\/s10822-015-9843-6","article-title":"Furan-based benzene mono- and dicarboxylic acid derivatives as multiple inhibitors of the bacterial Mur ligases (MurC-MurF): experimental and computational characterization","volume":"29","author":"Perdih","year":"2015","journal-title":"J. Comput. Aided Mol. Des."},{"key":"10.1016\/j.mimet.2026.107549_bb0510","doi-asserted-by":"crossref","DOI":"10.1016\/j.molbiopara.2021.111427","article-title":"Computational screening of potential inhibitors targeting MurF of Brugia malayi Wolbachia through multi-scale molecular docking, molecular dynamics and MM-GBSA analysis","volume":"246","author":"Poopandi","year":"2021","journal-title":"Mol. Biochem. Parasitol."},{"key":"10.1016\/j.mimet.2026.107549_bb0515","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1111\/j.1465-0691.2004.1006.x","article-title":"Antibacterial drug discovery: Is it all Downhill from here?","volume":"10","author":"Projan","year":"2004","journal-title":"Clinical Microbiology and Infection"},{"key":"10.1016\/j.mimet.2026.107549_bb0525","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1002\/prot.22879","article-title":"Automated minimization of steric clashes in protein structures","volume":"79","author":"Ramachandran","year":"2011","journal-title":"Proteins: Struct. Funct. Bioinformat."},{"key":"10.1016\/j.mimet.2026.107549_bb0530","doi-asserted-by":"crossref","first-page":"1451","DOI":"10.1016\/S0960-894X(01)00251-7","article-title":"Inhibitors of the bacterial cell wall biosynthesis enzyme MurC","volume":"11","author":"Reck","year":"2001","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.mimet.2026.107549_bb0535","doi-asserted-by":"crossref","first-page":"276","DOI":"10.1016\/S0168-9525(00)02024-2","article-title":"EMBOSS: the European molecular biology open software suite","volume":"16","author":"Rice","year":"2000","journal-title":"Trends Genet."},{"key":"10.1016\/j.mimet.2026.107549_bb0540","doi-asserted-by":"crossref","first-page":"33439","DOI":"10.1074\/jbc.M113.508135","article-title":"Specificity determinants for lysine incorporation in Staphylococcus aureus peptidoglycan as revealed by the structure of a MurE enzyme ternary complex","volume":"288","author":"Ruane","year":"2013","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mimet.2026.107549_bb0545","doi-asserted-by":"crossref","first-page":"3164","DOI":"10.2174\/1381612823666170214115048","article-title":"Mur ligase inhibitors as anti-bacterials: a comprehensive review","volume":"23","author":"Sangshetti","year":"2017","journal-title":"Curr. Pharm. Des."},{"key":"10.1016\/j.mimet.2026.107549_bb0550","doi-asserted-by":"crossref","first-page":"6133","DOI":"10.1073\/pnas.1017311108","article-title":"Mapping Allostery Through the Covariance Analysis of NMR Chemical Shifts","volume":"108","author":"Selvaratnam","year":"2011","journal-title":"PNAS"},{"key":"10.1016\/j.mimet.2026.107549_bb0555","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1016\/S0960-894X(01)00832-0","article-title":"Benzylidene Rhodanines as novel inhibitors of UDP-N-Acetylmuramate\/l-alanine ligase","volume":"12","author":"Sim","year":"2002","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.mimet.2026.107549_bb0560","doi-asserted-by":"crossref","first-page":"2572","DOI":"10.1021\/bi9722608","volume":"37","author":"Skarzynski","year":"1998","journal-title":"Biochemistry"},{"key":"10.1016\/j.mimet.2026.107549_bb0565","doi-asserted-by":"crossref","first-page":"640","DOI":"10.1016\/j.jmb.2006.07.066","article-title":"Structure, function and dynamics in the mur family of bacterial Cell Wall ligases","volume":"362","author":"Smith","year":"2006","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.mimet.2026.107549_bb0570","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/j.jprot.2014.03.009","article-title":"Ser\/Thr\/Tyr phosphoproteome characterization of Acinetobacter baumannii: comparison between a reference strain and a highly invasive multidrug-resistant clinical isolate","volume":"102","author":"Soares","year":"2014","journal-title":"J. Proteomics"},{"key":"10.1016\/j.mimet.2026.107549_bb0575","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1016\/j.ijbiomac.2016.12.082","article-title":"UDP-N-Acetylglucosamine enolpyruvyl transferase (MurA) of Acinetobacter baumannii (AbMurA): structural and functional properties","volume":"97","author":"Sonkar","year":"2017","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.mimet.2026.107549_bb0580","doi-asserted-by":"crossref","first-page":"1279","DOI":"10.1086\/420937","article-title":"Trends in Antimicrobial Drug Development: Implications for the Future","volume":"38","author":"Spellberg","year":"2004","journal-title":"Clinical Infectious Diseases"},{"key":"10.1016\/j.mimet.2026.107549_bb0585","doi-asserted-by":"crossref","first-page":"626","DOI":"10.1021\/ml300047h","article-title":"Dual inhibitor of MurD and MurE ligases from escherichia coli and staphylococcus aureus","volume":"3","author":"Toma\u0161i\u0107","year":"2012","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/j.mimet.2026.107549_bb0590","doi-asserted-by":"crossref","first-page":"D439","DOI":"10.1093\/nar\/gkab1061","article-title":"AlphaFold protein structure database: massively expanding the structural coverage of protein-sequence space with high-accuracy models","volume":"50","author":"Varadi","year":"2022","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.mimet.2026.107549_bb0595","doi-asserted-by":"crossref","first-page":"775","DOI":"10.1038\/35021219","article-title":"Molecular mechanisms that confer antibacterial drug resistance","volume":"406","author":"Walsh","year":"2000","journal-title":"Nature"},{"key":"10.1016\/j.mimet.2026.107549_bb0600","doi-asserted-by":"crossref","first-page":"5.6.1","DOI":"10.1002\/cpbi.3","article-title":"Comparative protein structure modeling using MODELLER","volume":"54","author":"Webb","year":"2016","journal-title":"Curr. Protoc. Bioinformatics"},{"key":"10.1016\/j.mimet.2026.107549_bb0605","doi-asserted-by":"crossref","first-page":"W407","DOI":"10.1093\/nar\/gkm290","article-title":"ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins","volume":"35","author":"Wiederstein","year":"2007","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/j.mimet.2026.107549_bb0610","doi-asserted-by":"crossref","first-page":"2525","DOI":"10.1016\/j.bpj.2011.10.024","article-title":"Improving the physical realism and structural accuracy of protein models by a two-step atomic-level energy minimization","volume":"101","author":"Xu","year":"2011","journal-title":"Biophys. J."},{"key":"10.1016\/j.mimet.2026.107549_bb0615","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1006\/jmbi.2000.4215","article-title":"Crystal structure of Escherichia coli UDPMurNAc-tripeptide D-alanyl-D-alanine-adding enzyme (MurF) at 2.3 \u00c5 resolution","volume":"304","author":"Yan","year":"2000","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.mimet.2026.107549_bb0620","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1080\/07391102.2013.770372","article-title":"Protein dynamics and motions in relation to their functions: several case studies and the underlying mechanisms","volume":"32","author":"Yang","year":"2014","journal-title":"J. Biomol. Struct. Dyn."},{"key":"10.1016\/j.mimet.2026.107549_bb0625","series-title":"Methods in Enzymology","first-page":"15","article-title":"A beginner\u2019s guide to molecular dynamics simulations and the identification of cross-correlation networks for enzyme engineering","author":"Yu","year":"2020"},{"key":"10.1016\/j.mimet.2026.107549_bb0630","doi-asserted-by":"crossref","first-page":"168444","DOI":"10.1016\/j.jmb.2024.168444","article-title":"Leucine motifs stabilize residual helical structure in disordered proteins","volume":"436","author":"Zavrtanik","year":"2024","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.mimet.2026.107549_bb0635","doi-asserted-by":"crossref","first-page":"2009","DOI":"10.1016\/j.bpj.2021.03.017","article-title":"Energetics and structure of alanine-rich \u03b1-helices via adaptive steered molecular dynamics","volume":"120","author":"Zhuang","year":"2021","journal-title":"Biophys. J."},{"key":"10.1016\/j.mimet.2026.107549_bb0640","doi-asserted-by":"crossref","first-page":"1079","DOI":"10.1016\/j.jmb.2007.01.051","article-title":"Propagation of dynamic changes in Barnase upon binding of Barstar: An NMR and computational study","volume":"367","author":"Zhuravleva","year":"2007","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.mimet.2026.107549_bb0645","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1046\/j.1432-1327.1998.2540154.x","article-title":"Molecular characterization of cyanophycin synthetase, the enzyme catalyzing the biosynthesis of the cyanobacterial reserve material multi- L-arginyl-poly- L-aspartate (cyanophycin)","volume":"254","author":"Ziegler","year":"1998","journal-title":"Eur. J. Biochem."}],"container-title":["Journal of Microbiological Methods"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0167701226001612?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0167701226001612?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,7,16]],"date-time":"2026-07-16T11:43:45Z","timestamp":1784202225000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0167701226001612"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,7]]},"references-count":123,"alternative-id":["S0167701226001612"],"URL":"https:\/\/doi.org\/10.1016\/j.mimet.2026.107549","relation":{},"ISSN":["0167-7012"],"issn-type":[{"value":"0167-7012","type":"print"}],"subject":[],"published":{"date-parts":[[2026,7]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Exploiting selected Mur enzyme characteristics for antibacterial drug design","name":"articletitle","label":"Article Title"},{"value":"Journal of Microbiological Methods","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.mimet.2026.107549","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 The Authors. Published by Elsevier B.V.","name":"copyright","label":"Copyright"}],"article-number":"107549"}}