{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,26]],"date-time":"2026-09-26T21:15:48Z","timestamp":1790457348310,"version":"4.1.0"},"reference-count":88,"publisher":"Elsevier BV","issue":"8","license":[{"start":{"date-parts":[[2019,8,1]],"date-time":"2019-08-01T00:00:00Z","timestamp":1564617600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2019,8,1]],"date-time":"2019-08-01T00:00:00Z","timestamp":1564617600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"content-domain":{"domain":["bmn.com","cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Trends in Biochemical Sciences"],"published-print":{"date-parts":[[2019,8]]},"DOI":"10.1016\/j.tibs.2019.03.007","type":"journal-article","created":{"date-parts":[[2019,4,27]],"date-time":"2019-04-27T11:07:01Z","timestamp":1556363221000},"page":"701-715","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":25,"title":["Targeting Lipoprotein Biogenesis: Considerations towards Antimicrobials"],"prefix":"10.1016","volume":"44","author":[{"given":"Toufic","family":"El Arnaout","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tewfik","family":"Soulimane","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.tibs.2019.03.007_bb0005","doi-asserted-by":"crossref","first-page":"5560","DOI":"10.1016\/j.bmcl.2009.08.045","article-title":"Using the golden triangle to optimize clearance and oral absorption","volume":"19","author":"Johnson","year":"2009","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.tibs.2019.03.007_bb0010","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/S0169-409X(00)00129-0","article-title":"Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings","volume":"46","author":"Lipinski","year":"2001","journal-title":"Adv. Drug Deliv. Rev."},{"key":"10.1016\/j.tibs.2019.03.007_bb0015","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1016\/j.tibs.2018.11.008","article-title":"Hitting undruggable targets: viewing stabilized peptide development through the lens of quantitative systems pharmacology","volume":"44","author":"Atangcho","year":"2019","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.tibs.2019.03.007_bb0020","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1002\/med.20163","article-title":"Falcipain-2 inhibitors","volume":"30","author":"Ettari","year":"2010","journal-title":"Med. Res. Rev."},{"key":"10.1016\/j.tibs.2019.03.007_bb0025","doi-asserted-by":"crossref","first-page":"3049","DOI":"10.2174\/0929867311320250003","article-title":"Development of Plasmodium falciparum protease inhibitors in the past decade (2002\u20132012)","volume":"20","author":"Perez","year":"2013","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.tibs.2019.03.007_bb0030","doi-asserted-by":"crossref","first-page":"1409","DOI":"10.4155\/fmc.12.93","article-title":"Macrocycles in new drug discovery","volume":"4","author":"Mallinson","year":"2012","journal-title":"Future Med. Chem."},{"key":"10.1016\/j.tibs.2019.03.007_bb0035","doi-asserted-by":"crossref","DOI":"10.1038\/ncomms10198","article-title":"Crystal structure of E. coli lipoprotein diacylglyceryl transferase","volume":"7","author":"Mao","year":"2016","journal-title":"Nat. Commun."},{"key":"10.1016\/j.tibs.2019.03.007_bb0040","doi-asserted-by":"crossref","first-page":"876","DOI":"10.1126\/science.aad3747","article-title":"Structural basis of lipoprotein signal peptidase II action and inhibition by the antibiotic globomycin","volume":"351","author":"Vogeley","year":"2016","journal-title":"Science"},{"key":"10.1016\/j.tibs.2019.03.007_bb0045","doi-asserted-by":"crossref","first-page":"E6044","DOI":"10.1073\/pnas.1707813114","article-title":"Structural insights into lipoprotein N-acylation by Escherichia coli apolipoprotein N-acyltransferase","volume":"114","author":"Noland","year":"2017","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.tibs.2019.03.007_bb0050","doi-asserted-by":"crossref","first-page":"15948","DOI":"10.1038\/ncomms15948","article-title":"Crystal structure of E. coli apolipoprotein N-acyl transferase","volume":"8","author":"Lu","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.tibs.2019.03.007_bb0055","doi-asserted-by":"crossref","DOI":"10.1038\/ncomms15952","article-title":"Structural insights into the mechanism of the membrane integral N-acyltransferase step in bacterial lipoprotein synthesis","volume":"8","author":"Wiktor","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.tibs.2019.03.007_bb0060","series-title":"bioRxiv","article-title":"Conformational changes in apolipoprotein N-acyltransferase (Lnt)","author":"Wiseman","year":"2018"},{"key":"10.1016\/j.tibs.2019.03.007_bb0065","doi-asserted-by":"crossref","first-page":"19701","DOI":"10.1016\/S0021-9258(17)32077-X","article-title":"Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol","volume":"269","author":"Sankaran","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tibs.2019.03.007_bb0070","doi-asserted-by":"crossref","first-page":"1705","DOI":"10.1128\/JB.02414-14","article-title":"Revisiting the Gram-negative lipoprotein paradigm","volume":"197","author":"LoVullo","year":"2015","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.tibs.2019.03.007_bb0075","doi-asserted-by":"crossref","first-page":"1547","DOI":"10.1099\/mic.0.000726","article-title":"The apolipoprotein N-acyl transferase Lnt is dispensable for growth in Acinetobacter species","volume":"164","author":"Gwin","year":"2018","journal-title":"Microbiology"},{"key":"10.1016\/j.tibs.2019.03.007_bb0080","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1111\/j.1574-6976.2009.00194.x","article-title":"Extracellular biology of Myxococcus xanthus","volume":"34","author":"Konovalova","year":"2010","journal-title":"FEMS Microbiol. Rev."},{"key":"10.1016\/j.tibs.2019.03.007_bb0085","doi-asserted-by":"crossref","first-page":"3800","DOI":"10.1002\/1873-3468.12273","article-title":"Mycobacterium tuberculosis lipoproteins in virulence and immunity \u2013 fighting with a double-edged sword","volume":"590","author":"Becker","year":"2016","journal-title":"FEBS Lett."},{"key":"10.1016\/j.tibs.2019.03.007_bb0090","series-title":"Bacterial Secreted Proteins: Secretory Mechanisms and Role in Pathogenesis","author":"Wooldridge","year":"2009"},{"key":"10.1016\/j.tibs.2019.03.007_bb0095","doi-asserted-by":"crossref","first-page":"1562","DOI":"10.1016\/j.chembiol.2015.10.006","article-title":"Quantitative lipoproteomics in Clostridium difficile reveals a role for lipoproteins in sporulation","volume":"22","author":"Charlton","year":"2015","journal-title":"Chem. Biol."},{"key":"10.1016\/j.tibs.2019.03.007_bb0100","doi-asserted-by":"crossref","first-page":"1395","DOI":"10.1111\/j.1365-2958.2011.07656.x","article-title":"Dissecting the complete lipoprotein biogenesis pathway in Streptomyces scabies","volume":"80","author":"Widdick","year":"2011","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.tibs.2019.03.007_bb0105","doi-asserted-by":"crossref","first-page":"8406","DOI":"10.1074\/jbc.M809618200","article-title":"The triacylated ATP binding cluster transporter substrate-binding lipoprotein of Staphylococcus aureus functions as a native ligand for Toll-like receptor 2","volume":"284","author":"Kurokawa","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tibs.2019.03.007_bb0110","doi-asserted-by":"crossref","DOI":"10.1155\/2010\/410975","article-title":"Mutational and bioinformatic analysis of haloarchaeal lipobox-containing proteins","volume":"2010","author":"Storf","year":"2010","journal-title":"Archaea"},{"key":"10.1016\/j.tibs.2019.03.007_bb0115","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1128\/JB.00976-06","article-title":"Inactivation of Lgt allows systematic characterization of lipoproteins from Listeria monocytogenes","volume":"189","author":"Baumgartner","year":"2007","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.tibs.2019.03.007_bb0120","doi-asserted-by":"crossref","DOI":"10.1128\/JB.00099-17","article-title":"Identification of the lyso-form N-acyl intramolecular transferase in low-GC Firmicutes","volume":"199","author":"Armbruster","year":"2017","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.tibs.2019.03.007_bb0125","doi-asserted-by":"crossref","first-page":"13170","DOI":"10.1074\/jbc.M111.292235","article-title":"Novel bacterial lipoprotein structures conserved in low-GC content Gram-positive bacteria are recognized by Toll-like receptor 2","volume":"287","author":"Kurokawa","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tibs.2019.03.007_bb0130","doi-asserted-by":"crossref","first-page":"1110","DOI":"10.1021\/bi101923r","article-title":"Molecular mechanism by which palmitate inhibits PKR autophosphorylation","volume":"50","author":"Cho","year":"2011","journal-title":"Biochemistry"},{"key":"10.1016\/j.tibs.2019.03.007_bb0135","doi-asserted-by":"crossref","first-page":"29941","DOI":"10.1074\/jbc.M111.245225","article-title":"Crystal structure of H2O2-dependent cytochrome P450SPalpha with its bound fatty acid substrate: insight into the regioselective hydroxylation of fatty acids at the alpha position","volume":"286","author":"Fujishiro","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tibs.2019.03.007_bb0140","doi-asserted-by":"crossref","first-page":"1432","DOI":"10.1002\/pro.2327","article-title":"Crystal structures of alpha-dioxygenase from Oryza sativa: insights into substrate binding and activation by hydrogen peroxide","volume":"22","author":"Zhu","year":"2013","journal-title":"Protein Sci."},{"key":"10.1016\/j.tibs.2019.03.007_bb0145","series-title":"Advances in Membrane Proteins. Part I: Mass Processing and Transportation","first-page":"77","article-title":"Membrane phospholipid biosynthesis in bacteria","author":"Tang","year":"2018"},{"key":"10.1016\/j.tibs.2019.03.007_bb0150","doi-asserted-by":"crossref","first-page":"7636","DOI":"10.1073\/pnas.1403097111","article-title":"Crystal structure of lipid phosphatase Escherichia coli phosphatidylglycerophosphate phosphatase B","volume":"111","author":"Fan","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.tibs.2019.03.007_bb0155","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.09248","article-title":"Large-scale determination of previously unsolved protein structures using evolutionary information","volume":"4","author":"Ovchinnikov","year":"2015","journal-title":"eLife"},{"key":"10.1016\/j.tibs.2019.03.007_bb0160","doi-asserted-by":"crossref","first-page":"18342","DOI":"10.1074\/jbc.M116.737874","article-title":"Structural insight into substrate selection and catalysis of lipid phosphate phosphatase PgpB in the cell membrane","volume":"291","author":"Tong","year":"2016","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tibs.2019.03.007_bb0165","doi-asserted-by":"crossref","first-page":"1691","DOI":"10.1038\/s41467-017-01821-9","article-title":"Structural insights into the committed step of bacterial phospholipid biosynthesis","volume":"8","author":"Li","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.tibs.2019.03.007_bb0170","doi-asserted-by":"crossref","first-page":"410","DOI":"10.7164\/antibiotics.31.410","article-title":"Globomycin, a new peptide antibiotic with spheroplast-forming activity. I. Taxonomy of producing organisms and fermentation","volume":"31","author":"Inukai","year":"1978","journal-title":"J Antibiot. (Tokyo)"},{"key":"10.1016\/j.tibs.2019.03.007_bb0175","doi-asserted-by":"crossref","first-page":"83","DOI":"10.7164\/antibiotics.32.83","article-title":"Isolation and structure of SF-1902 A5, a new globomycin analogue","volume":"32","author":"Omoto","year":"1979","journal-title":"J Antibiot. (Tokyo)"},{"key":"10.1016\/j.tibs.2019.03.007_bb0180","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1128\/jb.145.1.657-660.1981","article-title":"Globomycin sensitivity of Escherichia coli and Salmonella typhimurium: effects of mutations affecting structures of murein lipoprotein","volume":"145","author":"Lai","year":"1981","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.tibs.2019.03.007_bb0185","doi-asserted-by":"crossref","first-page":"1416","DOI":"10.7164\/antibiotics.34.1416","article-title":"Studies on SF-1902 A2~A5, minor components of SF-1902 (globomycin)","volume":"34","author":"Omoto","year":"1981","journal-title":"J. Antibiot."},{"key":"10.1016\/j.tibs.2019.03.007_bb0190","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1111\/j.1747-0285.2010.00972.x","article-title":"Non-competitive inhibition by active site binders","volume":"75","author":"Blat","year":"2010","journal-title":"Chem. Biol. Drug Des."},{"key":"10.1016\/j.tibs.2019.03.007_bb0195","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1016\/j.chembiol.2017.12.011","article-title":"Lipoprotein signal peptidase inhibitors with antibiotic properties identified through design of a robust in vitro HT platform","volume":"25","author":"Kitamura","year":"2018","journal-title":"Cell Chem. Biol."},{"key":"10.1016\/j.tibs.2019.03.007_bb0200","doi-asserted-by":"crossref","first-page":"5891","DOI":"10.1016\/S0021-9258(18)88911-6","article-title":"Inhibition of prolipoprotein signal peptidase by globomycin","volume":"260","author":"Dev","year":"1985","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tibs.2019.03.007_bb0205","doi-asserted-by":"crossref","first-page":"1741","DOI":"10.1110\/ps.0305203","article-title":"Atomic resolution analysis of the catalytic site of an aspartic proteinase and an unexpected mode of binding by short peptides","volume":"12","author":"Erskine","year":"2003","journal-title":"Protein Sci."},{"key":"10.1016\/j.tibs.2019.03.007_bb0210","doi-asserted-by":"crossref","first-page":"25529","DOI":"10.1074\/jbc.273.40.25529","article-title":"The low barrier hydrogen bond in enzymatic catalysis","volume":"273","author":"Cleland","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tibs.2019.03.007_bb0215","doi-asserted-by":"crossref","first-page":"4582","DOI":"10.1074\/jbc.M210471200","article-title":"Kinetic studies on \u03b2-site amyloid precursor protein-cleaving enzyme (BACE): confirmation of an iso-mechanism","volume":"278","author":"Toulokhonova","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tibs.2019.03.007_bb0220","doi-asserted-by":"crossref","first-page":"2315","DOI":"10.1016\/S0960-894X(03)00432-3","article-title":"Synthesis and antimicrobial activity of novel globomycin analogues","volume":"13","author":"Kiho","year":"2003","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.tibs.2019.03.007_bb0225","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1016\/j.bmc.2003.10.055","article-title":"Structure\u2013activity relationships of globomycin analogues as antibiotics","volume":"12","author":"Kiho","year":"2004","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.tibs.2019.03.007_bb0230","doi-asserted-by":"crossref","first-page":"1597","DOI":"10.1111\/j.1365-2958.2007.06034.x","article-title":"Haloferax volcanii twin-arginine translocation substates include secreted soluble, C-terminally anchored and lipoproteins","volume":"66","author":"Gim\u00e9nez","year":"2007","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.tibs.2019.03.007_bb0235","doi-asserted-by":"crossref","first-page":"414","DOI":"10.1093\/jac\/dkm223","article-title":"LspA-independent action of globomycin on Mycobacterium tuberculosis","volume":"60","author":"Banaiee","year":"2007","journal-title":"J. Antimicrob. Chemother."},{"key":"10.1016\/j.tibs.2019.03.007_bb0240","unstructured":"Wolan, D.W. and Owensby, A. Scripps Research Institute. Methods for identifying novel antibiotics and related compositions, WO2017040762A2"},{"key":"10.1016\/j.tibs.2019.03.007_bb0245","first-page":"424","article-title":"Autocides and a paracide, antibiotic TA, produced by Myxococcus xanthus","volume":"17","author":"Rosenberg","year":"1996","journal-title":"J. Ind. Microbiol."},{"key":"10.1016\/j.tibs.2019.03.007_bb0250","doi-asserted-by":"crossref","first-page":"2014","DOI":"10.1128\/AAC.06148-11","article-title":"Myxobacterium-produced antibiotic TA (myxovirescin) inhibits type II signal peptidase","volume":"56","author":"Xiao","year":"2012","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.tibs.2019.03.007_bb0255","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1128\/AAC.4.5.507","article-title":"Bactericidal action of an antibiotic produced by Myxococcus xanthus","volume":"4","author":"Rosenberg","year":"1973","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.tibs.2019.03.007_bb0260","unstructured":"Rosenberg, E. Ramot University Authority. Antibacterial agent, US5532231A"},{"key":"10.1016\/j.tibs.2019.03.007_bb0265","series-title":"Structure\u2013Function Studies of the Prolipoprotein Signal Peptidase, LspA","author":"El Arnaout","year":"2013"},{"key":"10.1016\/j.tibs.2019.03.007_bb0270","doi-asserted-by":"crossref","first-page":"11114","DOI":"10.1016\/S0021-9258(18)90629-0","article-title":"Rapid assay and purification of a unique signal peptidase that processes the prolipoprotein from Escherichia coli B","volume":"259","author":"Dev","year":"1984","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tibs.2019.03.007_bb0275","first-page":"291","article-title":"Cathepsin D inhibitors","volume":"45","author":"Gacko","year":"2007","journal-title":"Folia Histochem. Cytobiol."},{"key":"10.1016\/j.tibs.2019.03.007_bb0280","doi-asserted-by":"crossref","first-page":"3423","DOI":"10.1016\/S0968-0896(03)00312-2","article-title":"New inhibitors of the malaria aspartyl proteases plasmepsin I and II","volume":"11","author":"Dahlgren","year":"2003","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.tibs.2019.03.007_bb0285","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1107\/S0907444999016376","article-title":"Structural study of the complex between human pepsin and a phosphorus-containing peptidic\u00adtransition-state analog","volume":"56","author":"Masao","year":"2000","journal-title":"Acta Crystallogr. Sect. D"},{"key":"10.1016\/j.tibs.2019.03.007_bb0290","doi-asserted-by":"crossref","first-page":"3586","DOI":"10.1016\/j.bmcl.2017.05.027","article-title":"Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity","volume":"27","author":"Takagi","year":"2017","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.tibs.2019.03.007_bb0295","doi-asserted-by":"crossref","first-page":"726","DOI":"10.1016\/j.tibs.2018.06.009","article-title":"The rhomboid superfamily: structural mechanisms and chemical biology opportunities","volume":"43","author":"Tich\u00e1","year":"2018","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.tibs.2019.03.007_bb0300","doi-asserted-by":"crossref","DOI":"10.1186\/gb-2001-2-1-reviews0001","article-title":"The nitrilase superfamily: classification, structure and function","volume":"2","author":"Pace","year":"2001","journal-title":"Genome Biol."},{"key":"10.1016\/j.tibs.2019.03.007_bb0305","doi-asserted-by":"crossref","first-page":"5761","DOI":"10.1128\/AEM.00312-11","article-title":"Biochemical and mutational studies of the Bacillus cereus CECT 5050T formamidase support the existence of a C-E-E-K tetrad in several members of the nitrilase superfamily","volume":"77","author":"Soriano-Maldonado","year":"2011","journal-title":"Appl. Environ. Microbiol."},{"key":"10.1016\/j.tibs.2019.03.007_bb0310","doi-asserted-by":"crossref","first-page":"870","DOI":"10.1016\/j.ijbiomac.2018.05.229","article-title":"The N-acyltransferase Lnt: structure\u2013function insights from recent simultaneous studies","volume":"117","author":"Cheng","year":"2018","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.tibs.2019.03.007_bb0315","doi-asserted-by":"crossref","first-page":"28514","DOI":"10.1074\/jbc.M113.503284","article-title":"The mechanism of the amidases: mutating the glutamate adjacent to the catalytic triad inactivates the enzyme due to substrate mispositioning","volume":"288","author":"Weber","year":"2013","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tibs.2019.03.007_bb0320","doi-asserted-by":"crossref","first-page":"692","DOI":"10.1111\/mmi.12897","article-title":"Residues located on membrane-embedded flexible loops are essential for the second step of the apolipoprotein N-acyltransferase reaction","volume":"95","author":"Gelis-Jeanvoine","year":"2015","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.tibs.2019.03.007_bb0325","doi-asserted-by":"crossref","first-page":"27936","DOI":"10.1074\/jbc.M111.243519","article-title":"Kinetics and phospholipid specificity of apolipoprotein N-acyltransferase","volume":"286","author":"Hillmann","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tibs.2019.03.007_bb0330","doi-asserted-by":"crossref","first-page":"13372","DOI":"10.1074\/jbc.M611839200","article-title":"Amino acids at positions 3 and 4 determine the membrane specificity of Pseudomonas aeruginosa lipoproteins","volume":"282","author":"Narita","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tibs.2019.03.007_bb0335","doi-asserted-by":"crossref","first-page":"810","DOI":"10.1046\/j.1365-2958.1999.01647.x","article-title":"Testing the \u2018+2 rule\u2019 for lipoprotein sorting in the Escherichia coli cell envelope with a new genetic selection","volume":"34","author":"Anke","year":"1999","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.tibs.2019.03.007_bb0340","doi-asserted-by":"crossref","first-page":"1509","DOI":"10.1016\/j.bbamcr.2014.04.022","article-title":"Secretion of bacterial lipoproteins: through the cytoplasmic membrane, the periplasm and beyond","volume":"1843","author":"Zuckert","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.tibs.2019.03.007_bb0345","doi-asserted-by":"crossref","DOI":"10.1126\/science.aao6326","article-title":"Fatty acyl recognition and transfer by an integral membrane S-acyltransferase","volume":"359","author":"Rana","year":"2018","journal-title":"Science"},{"key":"10.1016\/j.tibs.2019.03.007_bb0350","doi-asserted-by":"crossref","first-page":"666","DOI":"10.1038\/nsmb.3436","article-title":"A two-helix motif positions the lysophosphatidic acid acyltransferase active site for catalysis within the membrane bilayer","volume":"24","author":"Robertson","year":"2017","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.tibs.2019.03.007_bb0355","doi-asserted-by":"crossref","first-page":"566","DOI":"10.1016\/j.tibs.2017.04.004","article-title":"Dynamic protein acylation: new substrates, mechanisms, and drug targets","volume":"42","author":"Lanyon-Hogg","year":"2017","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.tibs.2019.03.007_bb0360","doi-asserted-by":"crossref","first-page":"19598","DOI":"10.1074\/jbc.M701039200","article-title":"Structure of amidase from Pseudomonas aeruginosa showing a trapped acyl transfer reaction intermediate state","volume":"282","author":"Andrade","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tibs.2019.03.007_bb0365","doi-asserted-by":"crossref","first-page":"5250","DOI":"10.1021\/jm200217m","article-title":"Novel lipophilic acetohydroxamic acid derivatives based on conformationally constrained spiro carbocyclic 2,6-diketopiperazine scaffolds with potent trypanocidal activity","volume":"54","author":"Fytas","year":"2011","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.tibs.2019.03.007_bb0370","doi-asserted-by":"crossref","first-page":"408","DOI":"10.1111\/cbdd.13088","article-title":"Lipophilic conformationally constrained spiro carbocyclic 2,6-diketopiperazine-1-acetohydroxamic acid analogues as trypanocidal and leishmanicidal agents: an extended SAR study","volume":"91","author":"Zoidis","year":"2018","journal-title":"Chem. Biol. Drug Des."},{"key":"10.1016\/j.tibs.2019.03.007_bb0375","article-title":"The important role of halogen bond in substrate selectivity of enzymatic catalysis","volume":"6","author":"Jiang","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.tibs.2019.03.007_bb0380","doi-asserted-by":"crossref","first-page":"E1397","DOI":"10.3390\/molecules22091397","article-title":"Looking back, looking forward at halogen bonding in drug discovery","volume":"22","author":"Mendez","year":"2017","journal-title":"Molecules"},{"key":"10.1016\/j.tibs.2019.03.007_bb0385","doi-asserted-by":"crossref","first-page":"808","DOI":"10.1016\/j.bbapap.2008.11.005","article-title":"Outer membrane permeability and antibiotic resistance","volume":"1794","author":"Delcour","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.tibs.2019.03.007_bb0390","doi-asserted-by":"crossref","first-page":"261","DOI":"10.2147\/IDR.S144299","article-title":"Exploring bacterial outer membrane barrier to combat bad bugs","volume":"10","author":"Ghai","year":"2017","journal-title":"Infect. Drug Resist."},{"key":"10.1016\/j.tibs.2019.03.007_bb0395","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1016\/j.bmcl.2013.12.059","article-title":"New natural products as new leads for antibacterial drug discovery","volume":"24","author":"Brown","year":"2014","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.tibs.2019.03.007_bb0400","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1016\/j.tibs.2015.02.001","article-title":"Decoding and reprogramming complex polyketide assembly lines: prospects for synthetic biology","volume":"40","author":"Hertweck","year":"2015","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.tibs.2019.03.007_bb0405","doi-asserted-by":"crossref","first-page":"668","DOI":"10.1016\/j.tibs.2018.06.011","article-title":"How macrolide antibiotics work","volume":"43","author":"V\u00e1zquez-Laslop","year":"2018","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.tibs.2019.03.007_bb0410","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1016\/j.tibs.2017.06.007","article-title":"A bright future for serial femtosecond crystallography with XFELs","volume":"42","author":"Johansson","year":"2017","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.tibs.2019.03.007_bb0415","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/j.tibs.2014.10.005","article-title":"How cryo-EM is revolutionizing structural biology","volume":"40","author":"Bai","year":"2015","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.tibs.2019.03.007_bb0420","doi-asserted-by":"crossref","DOI":"10.1128\/mBio.01172-17","article-title":"Synergy between active efflux and outer membrane diffusion defines rules of antibiotic permeation into Gram-negative bacteria","volume":"8","author":"Krishnamoorthy","year":"2017","journal-title":"mBio"},{"key":"10.1016\/j.tibs.2019.03.007_bb0425","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1007084","article-title":"Synergy between conventional antibiotics and anti-biofilm peptides in a murine, sub-cutaneous abscess model caused by recalcitrant ESKAPE pathogens","volume":"14","author":"Pletzer","year":"2018","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.tibs.2019.03.007_bb0430","series-title":"Embracing the Future of Work to Unlock R&D Productivity \u2013 Measuring the Return from Pharmaceutical Innovation","author":"Deloitte Centre for Health Solutions","year":"2018"},{"key":"10.1016\/j.tibs.2019.03.007_bb0435","doi-asserted-by":"crossref","first-page":"960","DOI":"10.1002\/pro.5560040516","article-title":"Crystal structure of human pepsin and its complex with pepstatin","volume":"4","author":"Fujinaga","year":"1995","journal-title":"Protein Sci."},{"key":"10.1016\/j.tibs.2019.03.007_bb0440","doi-asserted-by":"crossref","first-page":"3755","DOI":"10.1093\/bioinformatics\/bty419","article-title":"NGL viewer: web-based molecular graphics for large complexes","volume":"34","author":"Rose","year":"2018","journal-title":"Bioinformatics"}],"container-title":["Trends in Biochemical Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0968000419300635?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0968000419300635?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,18]],"date-time":"2025-10-18T21:39:11Z","timestamp":1760823551000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0968000419300635"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,8]]},"references-count":88,"journal-issue":{"issue":"8","published-print":{"date-parts":[[2019,8]]}},"alternative-id":["S0968000419300635"],"URL":"https:\/\/doi.org\/10.1016\/j.tibs.2019.03.007","relation":{},"ISSN":["0968-0004"],"issn-type":[{"value":"0968-0004","type":"print"}],"subject":[],"published":{"date-parts":[[2019,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Targeting Lipoprotein Biogenesis: Considerations towards Antimicrobials","name":"articletitle","label":"Article Title"},{"value":"Trends in Biochemical Sciences","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.tibs.2019.03.007","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2019 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}