MmpL3 is the flippase for mycolic acids in mycobacteria

The Phyre2 web portal for protein modeling, prediction and analysis

Kelley, L. A., Mezulis, S., Yates, C. M., Wass, M. N., & Sternberg, M. J. E. (2015) · Nature Protocols · doi:10.1038/nprot.2015.053 · Cited by 9,652 · see citing works

THE ENVELOPE OF MYCOBACTERIA

Brennan, P. J., & Nikaido, H. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.000333 · Cited by 1,953 · see citing works

<i>inhA</i> , a Gene Encoding a Target for Isoniazid and Ethionamide in <i>Mycobacterium tuberculosis</i>

Banerjee, A., Dubnau, E., Quemard, A., Balasubramanian, V., Um, K. S., Wilson, T., Collins, D., de Lisle, G., & Jacobs, W. R. (1994) · Science · doi:10.1126/science.8284673 · Cited by 1,389 · see citing works

Rapid Cu-free click chemistry with readily synthesized biarylazacyclooctynones

Jewett, J. C., Sletten, E. M., & Bertozzi, C. R. (2010) · Journal of the American Chemical Society · doi:10.1021/ja100014q · Cited by 697 · see citing works

Pathway to Synthesis and Processing of Mycolic Acids in Mycobacterium tuberculosis

Takayama, K., Wang, C., & Besra, G. S. (2005) · Clinical Microbiology Reviews · doi:10.1128/cmr.18.1.81-101.2005 · Cited by 657 · see citing works

SQ109 Targets MmpL3, a Membrane Transporter of Trehalose Monomycolate Involved in Mycolic Acid Donation to the Cell Wall Core of Mycobacterium tuberculosis

Tahlan, K., Wilson, R., Kastrinsky, D. B., Arora, K., Nair, V., Fischer, E. R., Barnes, S. W., Walker, J. R., Alland, D., Barry, C. E., et al. (2012) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.05708-11 · Cited by 501 · see citing works

Inhibition of mycolic acid transport across the Mycobacterium tuberculosis plasma membrane

Grzegorzewicz, A. E., Pham, H., Gundi, V. A. K. B., Scherman, M. S., North, E. J., Hess, T., Jones, V., Gruppo, V., Born, S. E. M., Korduláková, J., et al. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.794 · Cited by 442 · see citing works

Contribution of theMycobacterium tuberculosisMmpL Protein Family to Virulence and Drug Resistance

Domenech, P., Reed, M. B., & Barry, C. E. (2005) · Infection and Immunity · doi:10.1128/iai.73.6.3492-3501.2005 · Cited by 362 · see citing works

Lipoprotein Sorting in Bacteria

Okuda, S., & Tokuda, H. (2010) · Annual Review of Microbiology · doi:10.1146/annurev-micro-090110-102859 · Cited by 327 · see citing works

Inactivation of the antigen 85C gene profoundly affects the mycolate content and alters the permeability of the <i>Mycobacterium tuberculosis</i> cell envelope

Jackson, M., Raynaud, C., Lanéelle, M., Guilhot, C., Laurent‐Winter, C., Ensergueix, D., Gicquel, B., & Daffé, M. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01310.x · Cited by 267 · see citing works

Mycobacterial outer membrane is a lipid bilayer and the inner membrane is unusually rich in diacyl phosphatidylinositol dimannosides

Bansal‐Mutalik, R., & Nikaido, H. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1403078111 · Cited by 254 · see citing works

Identification of Novel Inhibitors of M. tuberculosis Growth Using Whole Cell Based High-Throughput Screening

Stanley, S. A., Grant, S. S., Kawate, T., Iwase, N., Shimizu, M., Wivagg, C. N., Silvis, M. R., Kazyanskaya, E., Aquadro, J. A., Golas, A. J., et al. (2012) · ACS Chemical Biology · doi:10.1021/cb300151m · Cited by 252 · see citing works

MmpL8 is required for sulfolipid-1 biosynthesis and Mycobacterium tuberculosis virulence

Converse, S. E., Mougous, J. D., Leavell, M. D., Leary, J. A., Bertozzi, C. R., & Cox, J. S. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1030024100 · Cited by 250 · see citing works

MmpL3 Is the Cellular Target of the Antitubercular Pyrrole Derivative BM212

Rosa, V. L. L., Poce, G., Canseco, J. O., Buroni, S., Pasca, M. R., Biava, M., Raju, R. M., Porretta, G. C., Alfonso, S., Battilocchio, C., et al. (2011) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.05270-11 · Cited by 212 · see citing works

MmpL Genes Are Associated with Mycolic Acid Metabolism in Mycobacteria and Corynebacteria

Varela, C., Rittmann, D., Singh, A., Krumbach, K., Bhatt, K., Eggeling, L., Besra, G. S., & Bhatt, A. (2012) · Chemistry &amp; Biology · doi:10.1016/j.chembiol.2012.03.006 · Cited by 210 · see citing works

Novel Insights into the Mechanism of Inhibition of MmpL3, a Target of Multiple Pharmacophores in Mycobacterium tuberculosis

Li, W., Upadhyay, A., Fontes, F. L., North, E. J., Wang, Y., Crans, D. C., Grzegorzewicz, A. E., Jones, V., Franzblau, S. G., Lee, R. E., et al. (2014) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.03229-14 · Cited by 202 · see citing works

Probing the Mycobacterial Trehalome with Bioorthogonal Chemistry

Swarts, B. M., Holsclaw, C. M., Jewett, J. C., Alber, M., Fox, D. M., Siegrist, M. S., Leary, J. A., Kalscheuer, R., & Bertozzi, C. R. (2012) · Journal of the American Chemical Society · doi:10.1021/ja3062419 · Cited by 184 · see citing works

Indoleamides are active against drug-resistant Mycobacterium tuberculosis

Lun, S., Guo, H., Onajole, O. K., Pieroni, M., Gunosewoyo, H., Chen, G., Tipparaju, S. K., Ammerman, N. C., Kozikowski, A. P., & Bishai, W. R. (2013) · Nature Communications · doi:10.1038/ncomms3907 · Cited by 152 · see citing works

Indolcarboxamide Is a Preclinical Candidate for Treating Multidrug-Resistant Tuberculosis

Rao, S. P. S., Lakshminarayana, S. B., Kondreddi, R. R., Herve, M., Camacho, L. R., Bifani, P. J., Kalapala, S. K., Jiřiček, J., Ma, N. L., Tan, B. H., et al. (2013) · Science Translational Medicine · doi:10.1126/scitranslmed.3007355 · Cited by 148 · see citing works

Tetrahydropyrazolo[1,5-a]Pyrimidine-3-Carboxamide and N-Benzyl-6′,7′-Dihydrospiro[Piperidine-4,4′-Thieno[3,2-c]Pyran] Analogues with Bactericidal Efficacy against Mycobacterium tuberculosis Targeting MmpL3

Remuiñán, M. J., Pérez‐Herrán, E., Rullás, J., Alemparte, C., Martínez-Hoyos, M., Dow, D. J., Afari, J., Mehta, N., Esquivias, J., Jiménez, E., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060933 · Cited by 139 · see citing works

Mycobacteriophage Endolysins: Diverse and Modular Enzymes with Multiple Catalytic Activities

Payne, K. M., & Hatfull, G. F. (2012) · PLoS ONE · doi:10.1371/journal.pone.0034052 · Cited by 134 · see citing works

Interaction between Polyketide Synthase and Transporter Suggests Coupled Synthesis and Export of Virulence Lipid in M. tuberculosis

Jain, M., & Cox, J. S. (2005) · PLoS Pathogens · doi:10.1371/journal.ppat.0010002 · Cited by 125 · see citing works

MmpL11 Protein Transports Mycolic Acid-containing Lipids to the Mycobacterial Cell Wall and Contributes to Biofilm Formation in Mycobacterium smegmatis

Pacheco, S. A., Hsu, F., Powers, K. M., & Purdy, G. E. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.473371 · Cited by 124 · see citing works

A new piperidinol derivative targeting mycolic acid transport in Mycobacterium abscessus

Dupont, C., Viljoen, A. J., Dubar, F., Blaise, M., Bernut, A., Pawlik, A., Bouchier, C., Brosch, R., Guérardel, Y., Lelièvre, J., et al. (2016) · Molecular Microbiology · doi:10.1111/mmi.13406 · Cited by 119 · see citing works

Therapeutic Potential of the Mycobacterium tuberculosis Mycolic Acid Transporter, MmpL3

Li, W., Obregón‐Henao, A., Wallach, J. B., North, E. J., Lee, R. E., Jr., Juarrero, M. G., Schnappinger, D., & Jackson, M. (2016) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00826-16 · Cited by 118 · see citing works

Structure–Function Profile of MmpL3, the Essential Mycolic Acid Transporter from Mycobacterium tuberculosis

Belardinelli, J. M., Yazidi, A., Yang, L., Fabre, L., Li, W., Jacques, B., Angala, S. K., Rouiller, I., Zgurskaya, H. I., SYGUSCH, J., et al. (2016) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.6b00095 · Cited by 105 · see citing works

Improved BM212 MmpL3 Inhibitor Analogue Shows Efficacy in Acute Murine Model of Tuberculosis Infection

Poce, G., Bates, R. H., Alfonso, S., Cocozza, M., Porretta, G. C., Ballell, L., Rullás, J., Ortega, F., Logu, A. D., Agus, E., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056980 · Cited by 95 · see citing works

Biosynthesis and Translocation of Unsulfated Acyltrehaloses in Mycobacterium tuberculosis

Belardinelli, J. M., Larrouy-Maumus, G. J., Jones, V. M., de Carvalho, L. P. S., McNeil, M., & Jackson, M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.581199 · Cited by 77 · see citing works

Mycobacteriophage Ms6 LysB specifically targets the outer membrane of Mycobacterium smegmatis

Gil, F., Grzegorzewicz, A. E., Catalão, M. J., Vital, J. O., McNeil, M., & Pimentel, M. (2010) · Microbiology · doi:10.1099/mic.0.032821-0 · Cited by 69 · see citing works

THPP target assignment reveals EchA6 as an essential fatty acid shuttle in mycobacteria

Cox, J. A. G., Abrahams, K. A., Alemparte, C., Ghidelli, S., Rullás, J., Angulo‐Barturen, Í., Singh, A., Gurcha, S. S., Nataraj, V., Bethell, S., et al. (2016) · Nature Microbiology · doi:10.1038/nmicrobiol.2015.6 · Cited by 68 · see citing works

The Structure and Interactions of Periplasmic Domains of Crucial MmpL Membrane Proteins from Mycobacterium tuberculosis

Chim, N., Torres, R., Liu, Y., Capri, J., Batot, G., Whitelegge, J. P., & Goulding, C. W. (2015) · Chemistry & Biology · doi:10.1016/j.chembiol.2015.07.013 · Cited by 61 · see citing works

Lipoarabinomannan Localization and Abundance during Growth of Mycobacterium smegmatis

Dhiman, R. K., Dinadayala, P., Ryan, G. J., Lenaerts, A. J. M., Schenkel, A. R., & Crick, D. C. (2011) · Journal of Bacteriology · doi:10.1128/jb.05299-11 · Cited by 45 · see citing works

Spheroplast formation of Mycobacterium smegmatis and morphological aspects of their reversion to the bacillary form

Udou, T., Ogawa, M., & Mizuguchi, Y. (1982) · Journal of Bacteriology · doi:10.1128/jb.151.2.1035-1039.1982 · Cited by 35 · see citing works

An improved method for the preparation of mycobacterial spheroplasts and the mechanism involved in the reversion to bacillary form: electron microscopic and physiological study

Udou, T., Ogawa, M., & Mizuguchi, Y. (1983) · Canadian Journal of Microbiology · doi:10.1139/m83-010 · Cited by 19 · see citing works

The mycobacterial cell envelope — a moving target

Dulberger, C. L., Rubin, E. J., & Boutte, C. C. (2020) · Nature Reviews Microbiology · doi:10.1038/s41579-019-0273-7 · Cited by 365 · see citing works

Crystal Structures of Membrane Transporter MmpL3, an Anti-TB Drug Target

Zhang, B., Li, J., Yang, X., Wu, L., Zhang, J., Yang, Y., Zhao, Y., Zhang, L., Yang, X., Yang, X., et al. (2019) · Cell · doi:10.1016/j.cell.2019.01.003 · Cited by 263 · see citing works

MmpL3 is a lipid transporter that binds trehalose monomycolate and phosphatidylethanolamine

Su, C.-C., Klenotic, P. A., Bolla, J. R., Purdy, G. E., Robinson, C. V., & Yu, E. W. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1901346116 · Cited by 148 · see citing works

Mycobacterium smegmatis: The Vanguard of Mycobacterial Research

Sparks, I. L., Derbyshire, K. M., Jacobs, W. R., & Morita, Y. S. (2023) · Journal of Bacteriology · doi:10.1128/jb.00337-22 · Cited by 149 · see citing works

Direct Inhibition of MmpL3 by Novel Antitubercular Compounds

Li, W., Stevens, C. M., Pandya, A. N., Darzynkiewicz, Z., Bhattarai, P., Tong, W., Gonzalez-Juarrero, M., North, E. J., Zgurskaya, H. I., & Jackson, M. (2019) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.9b00048 · Cited by 97 · see citing works

Cell Walls and Membranes of Actinobacteria

Rahlwes, K. C., Sparks, I. L., & Morita, Y. S. (2019) · Subcellular Biochemistry · doi:10.1007/978-3-030-18768-2_13 · Cited by 65 · see citing works

Two Accessory Proteins Govern MmpL3 Mycolic Acid Transport in Mycobacteria

Fay, A., Czudnochowski, N., Rock, J. M., Johnson, J. R., Krogan, N. J., Rosenberg, O., & Glickman, M. S. (2019) · mBio · doi:10.1128/mbio.00850-19 · Cited by 65 · see citing works

DivIVA concentrates mycobacterial cell envelope assembly for initiation and stabilization of polar growth

Melzer, E. S., Sein, C. E., Chambers, J. J., & Siegrist, M. S. (2018) · Cytoskeleton · doi:10.1002/cm.21490 · Cited by 54 · see citing works

A new liquid chromatographic method for the identification of tuberculosis and other mycobacterium species

Schillack, V. R. (2007) · UpSpace Institutional Repository (University of Pretoria)

Mycolic acid patterns of some species of Mycobacterium

Minnikin, D. E., MINNIKIN, S. M., Parlett, J. H., et al. (1984) · Archives of Microbiology · doi:10.1007/bf00402005 · Cited by 166 · see citing works

Identification of mycobacteria by mycolic acid pattern.

Garza‐González, E., Guerrero‐Olazarán, M., Tijerina‐Menchaca, R., et al. (1998) · PubMed · Cited by 16 · see citing works

Distribution of a Novel Mycolic Acid in Species of the Genus Mycobacterium

Luquin, M., Lanéelle, M. A., Ausina, V., et al. (1991) · International Journal of Systematic Bacteriology · doi:10.1099/00207713-41-3-390 · Cited by 21 · see citing works

Utility of high-performance liquid chromatography analysis of mycolic acids and partial 16S rRNA gene sequencing for routine identification of Mycobacterium spp. in a national reference laboratory

Toney, N. C., Toney, S. R., & Butler, W. R. (2010) · Diagnostic Microbiology and Infectious Disease · doi:10.1016/j.diagmicrobio.2010.02.011 · Cited by 19 · see citing works