How sisters grow apart: mycobacterial growth and division

Bacterial Persistence as a Phenotypic Switch

Balaban, N. Q., Merrin, J., Chait, R., Kowalik, L., & Leibler, S. (2004) · Science · doi:10.1126/science.1099390 · Cited by 2,952

The spectrum of latent tuberculosis: rethinking the biology and intervention strategies

Barry, C. E., Boshoff, H. I., Dartois, V., Dick, T., Ehrt, S., Flynn, J., Schnappinger, D., Wilkinson, R. J., & Young, D. (2009) · Nature Reviews Microbiology · doi:10.1038/nrmicro2236 · Cited by 1,422

Genetic requirements for mycobacterial survival during infection

Sassetti, C. M., & Rubin, E. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2134250100 · Cited by 1,354

From the regulation of peptidoglycan synthesis to bacterial growth and morphology

Typas, A., Banzhaf, M., Gross, C. A., & Vollmer, W. (2012) · Nature Reviews Microbiology · doi:10.1038/nrmicro2677 · Cited by 1,273

Mycobacterial persistence requires the utilization of host cholesterol

Pandey, A. K., & Sassetti, C. M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711159105 · Cited by 1,064

High-Resolution Phenotypic Profiling Defines Genes Essential for Mycobacterial Growth and Cholesterol Catabolism

Griffin, J. E., Gawronski, J. D., DeJesus, M. A., Ioerger, T. R., Akerley, B. J., & Sassetti, C. M. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002251 · Cited by 1,048

The Role of the Granuloma in Expansion and Dissemination of Early Tuberculous Infection

Davis, J. M., & Ramakrishnan, L. (2009) · Cell · doi:10.1016/j.cell.2008.11.014 · Cited by 901

Advances in the development of new tuberculosis drugs and treatment regimens

Zumla, A., Nahid, P., & Cole, S. T. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4001 · Cited by 893

Bacterial cell division: assembly, maintenance and disassembly of the Z ring

Adams, D. W., & Errington, J. (2009) · Nature Reviews Microbiology · doi:10.1038/nrmicro2198 · Cited by 811

Correction: Corrigendum: Endogenous fructose production and metabolism in the liver contributes to the development of metabolic syndrome

Lanaspa, M. A., Ishimoto, T., Li, N., Cicerchi, C., Orlicky, D. J., Ruzycki, P., Rivard, C., Inaba, S., Roncal-Jimenez, C. A., Bales, E. S., et al. (2013) · Nature Communications · doi:10.1038/ncomms3929 · Cited by 796

Benzothiazinones Kill Mycobacterium tuberculosis by Blocking Arabinan Synthesis

Makarov, V., Manina, G., Mikusova, K., Möllmann, U., Ryabova, O., Saint-Joanis, B., Dhar, N., Pasca, M. R., Buroni, S., Lucarelli, A. P., et al. (2009) · Science · doi:10.1126/science.1171583 · Cited by 740

Peptidoglycan Molecular Requirements Allowing Detection by Nod1 and Nod2

Girardin, S. E., Travassos, L. H., Hervé, M., Blanot, D., Boneca, I. G., Philpott, D. J., Sansonetti, P. J., & Mengin-Lecreulx, D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307198200 · Cited by 686

Genome-wide requirements for Mycobacterium tuberculosis adaptation and survival in macrophages

Rengarajan, J., Bloom, B. R., & Rubin, E. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503272102 · Cited by 676

Tuberculous Granulomas Are Hypoxic in Guinea Pigs, Rabbits, and Nonhuman Primates

Via, L. E., Lin, P. L., Ray, S. M., Carrillo, J., Allen, S. S., Eum, S. Y., Taylor, K., Klein, E., Manjunatha, U., Gonzales, J., et al. (2008) · Infection and Immunity · doi:10.1128/iai.01515-07 · Cited by 664

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 660

Bacterial Cell Wall Synthesis: New Insights from Localization Studies

Scheffers, D.-J., & Pinho, M. G. (2005) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.69.4.585-607.2005 · Cited by 629

Cytokinesis in Bacteria

Errington, J., Daniel, R. A., & Scheffers, D.-J. (2003) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.67.1.52-65.2003 · Cited by 599

The immunological life cycle of tuberculosis

Ernst, J. D. (2012) · Nature Reviews Immunology · doi:10.1038/nri3259 · Cited by 577

Growth of Mycobacterium tuberculosis biofilms containing free mycolic acids and harbouring drug‐tolerant bacteria

Ojha, A. K., Baughn, A. D., Sambandan, D., Hsu, T., Trivelli, X., Guerardel, Y., Alahari, A., Kremer, L., Jacobs, W. R., & Hatfull, G. F. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06274.x · Cited by 545

Dynamic Persistence of Antibiotic-Stressed Mycobacteria

Wakamoto, Y., Dhar, N., Chait, R., Schneider, K., Signorino-Gelo, F., Leibler, S., & McKinney, J. D. (2013) · Science · doi:10.1126/science.1229858 · Cited by 542

Sterilization of granulomas is common in active and latent tuberculosis despite within-host variability in bacterial killing

Lin, P. L., Ford, C. B., Coleman, M. T., Myers, A. J., Gawande, R., Ioerger, T., Sacchettini, J., Fortune, S. M., & Flynn, J. L. (2014) · Nature Medicine · doi:10.1038/nm.3412 · Cited by 533

Coupled, Circumferential Motions of the Cell Wall Synthesis Machinery and MreB Filaments in B. subtilis

Garner, E. C., Bernard, R., Wang, W., Zhuang, X., Rudner, D. Z., & Mitchison, T. (2011) · Science · doi:10.1126/science.1203285 · Cited by 526

Microbial Cell Individuality and the Underlying Sources of Heterogeneity

Avery, S. V. (2006) · Nature Reviews Microbiology · doi:10.1038/nrmicro1460 · Cited by 521

Mycobacteria manipulate macrophage recruitment through coordinated use of membrane lipids

Cambier, C. J., Takaki, K. K., Larson, R. P., Hernandez, R. E., Tobin, D. M., Urdahl, K. B., Cosma, C. L., & Ramakrishnan, L. (2014) · Nature · doi:10.1038/nature12799 · Cited by 480

Asymmetry and Aging of Mycobacterial Cells Lead to Variable Growth and Antibiotic Susceptibility

Aldridge, B. B., Fernandez-Suarez, M., Heller, D., Ambravaneswaran, V., Irimia, D., Toner, M., & Fortune, S. M. (2012) · Science · doi:10.1126/science.1216166 · Cited by 454

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

Genomic analysis identifies targets of convergent positive selection in drug-resistant Mycobacterium tuberculosis

Farhat, M. R., Shapiro, B. J., Kieser, K. J., Sultana, R., Jacobson, K. R., Victor, T. C., Warren, R. M., Streicher, E. M., Calver, A., Sloutsky, A., et al. (2013) · Nature Genetics · doi:10.1038/ng.2747 · Cited by 440

Use of whole genome sequencing to estimate the mutation rate of Mycobacterium tuberculosis during latent infection

Ford, C. B., Lin, P. L., Chase, M. R., Shah, R. R., Iartchouk, O., Galagan, J., Mohaideen, N., Ioerger, T. R., Sacchettini, J. C., Lipsitch, M., et al. (2011) · Nature Genetics · doi:10.1038/ng.811 · Cited by 437

The Mycobacterium tuberculosis regulatory network and hypoxia

Galagan, J. E., Minch, K., Peterson, M., Lyubetskaya, A., Azizi, E., Sweet, L., Gomes, A., Rustad, T., Dolganov, G., Glotova, I., et al. (2013) · Nature · doi:10.1038/nature12337 · Cited by 431

Intracellular Mycobacterium tuberculosis Exploits Host-derived Fatty Acids to Limit Metabolic Stress

Lee, W., VanderVen, B. C., Fahey, R. J., & Russell, D. G. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.445056 · Cited by 424

Tuberculosis Pathogenesis and Immunity

Philips, J. A., & Ernst, J. D. (2012) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-011811-132458 · Cited by 416

Autolysins of Bacillus subtilis: multiple enzymes with multiple functions

Smith, T. J., Blackman, S. A., & Foster, S. J. (2000) · Microbiology · doi:10.1099/00221287-146-2-249 · Cited by 414

Bacterial Growth and Cell Division: a Mycobacterial Perspective

Hett, E. C., & Rubin, E. J. (2008) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00028-07 · Cited by 408

Mycobacterium tuberculosis Invasion of Macrophages: Linking Bacterial Gene Expression to Environmental Cues

Rohde, K. H., Abramovitch, R. B., & Russell, D. G. (2007) · Cell Host & Microbe · doi:10.1016/j.chom.2007.09.006 · Cited by 405

The Mycobacterium tuberculosis serine/threonine kinases PknA and PknB: substrate identification and regulation of cell shape

Kang, C.-M., Abbott, D. W., Park, S. T., Dascher, C. C., Cantley, L. C., & Husson, R. N. (2005) · Genes & Development · doi:10.1101/gad.1311105 · Cited by 388

Ubiquitin-Like Protein Involved in the Proteasome Pathway of Mycobacterium tuberculosis

Pearce, M. J., Mintseris, J., Ferreyra, J., Gygi, S. P., & Darwin, K. H. (2008) · Science · doi:10.1126/science.1163885 · Cited by 377

Mycobacterial Stationary Phase Induced by Low Oxygen Tension: Cell Wall Thickening and Localization of the 16-Kilodalton α-Crystallin Homolog

Cunningham, A. F., & Spreadbury, C. L. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.4.801-808.1998 · Cited by 361

Tryptophan Biosynthesis Protects Mycobacteria from CD4 T-Cell-Mediated Killing

Zhang, Y. J., Reddy, M. C., Ioerger, T. R., Rothchild, A. C., Dartois, V., Schuster, B. M., Trauner, A., Wallis, D., Galaviz, S., Huttenhower, C., et al. (2013) · Cell · doi:10.1016/j.cell.2013.10.045 · Cited by 351

The Peptidoglycan of Stationary-Phase Mycobacterium tuberculosis Predominantly Contains Cross-Links Generated by l,d -Transpeptidation

Lavollay, M., Arthur, M., Fourgeaud, M., Dubost, L., Marie, A., Veziris, N., Blanot, D., Gutmann, L., & Mainardi, J.-L. (2008) · Journal of Bacteriology · doi:10.1128/jb.00239-08 · Cited by 349

Microenvironments in Tuberculous Granulomas Are Delineated by Distinct Populations of Macrophage Subsets and Expression of Nitric Oxide Synthase and Arginase Isoforms

Mattila, J. T., Ojo, O. O., Kepka-Lenhart, D., Marino, S., Kim, J. H., Eum, S. Y., Via, L. E., Barry, C. E., Klein, E., Kirschner, D. E., et al. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1300113 · Cited by 347

A replication clock for Mycobacterium tuberculosis

Gill, W. P., Harik, N. S., Whiddon, M. R., Liao, R. P., Mittler, J. E., & Sherman, D. R. (2009) · Nature Medicine · doi:10.1038/nm.1915 · Cited by 341

Oxygenated mycolic acids are necessary for virulence of Mycobacterium tuberculosis in mice

Dubnau, E., Chan, J., Raynaud, C., Mohan, V. P., Lanéelle, M., Yu, K., Quémard, A., Smith, I., & Daffé, M. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.01882.x · Cited by 335

Metabolic Regulation of Mycobacterial Growth and Antibiotic Sensitivity

Baek, S.-H., Li, A. H., & Sassetti, C. M. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1001065 · Cited by 324

Direct Visualization by Cryo-EM of the Mycobacterial Capsular Layer: A Labile Structure Containing ESX-1-Secreted Proteins

Sani, M., Houben, E. N. G., Geurtsen, J., Pierson, J., de Punder, K., van Zon, M., Wever, B., Piersma, S. R., Jiménez, C. R., Daffé, M., et al. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1000794 · Cited by 311

Del-1, an Endogenous Leukocyte-Endothelial Adhesion Inhibitor, Limits Inflammatory Cell Recruitment

Choi, E. Y., Chavakis, E., Czabanka, M. A., Langer, H. F., Fraemohs, L., Economopoulou, M., Kundu, R. K., Orlandi, A., Zheng, Y. Y., Prieto, D. A., et al. (2008) · Science · doi:10.1126/science.1165218 · Cited by 309

Biosynthesis of the arabinogalactan-peptidoglycan complex of Mycobacterium tuberculosis

Crick, D. C., Mahapatra, S., & Brennan, P. J. (2001) · Glycobiology · doi:10.1093/glycob/11.9.107r · Cited by 293

Cholesterol Catabolism by Mycobacterium tuberculosis Requires Transcriptional and Metabolic Adaptations

Griffin, J. E., Pandey, A. K., Gilmore, S. A., Mizrahi, V., Mckinney, J. D., Bertozzi, C. R., & Sassetti, C. M. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.12.016 · Cited by 292

The Mycobacterium tuberculosis protein LdtMt2 is a nonclassical transpeptidase required for virulence and resistance to amoxicillin

Gupta, R., Lavollay, M., Mainardi, J.-L., Arthur, M., Bishai, W. R., & Lamichhane, G. (2010) · Nature Medicine · doi:10.1038/nm.2120 · Cited by 281

Multifunctional essentiality of succinate metabolism in adaptation to hypoxia in Mycobacterium tuberculosis

Eoh, H., & Rhee, K. Y. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1219375110 · Cited by 278

Extensive phosphorylation with overlapping specificity by Mycobacterium tuberculosis serine/threonine protein kinases

Prisic, S., Dankwa, S., Schwartz, D., Chou, M. F., Locasale, J. W., Kang, C.-M., Bemis, G., Church, G. M., Steen, H., & Husson, R. N. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913482107 · Cited by 268

Wag31, a homologue of the cell division protein DivIVA, regulates growth, morphology and polar cell wall synthesis in mycobacteria

Kang, C.-M., Nyayapathy, S., Lee, J.-Y., Suh, J.-W., & Husson, R. N. (2008) · Microbiology · doi:10.1099/mic.0.2007/014076-0 · Cited by 264

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 257

Location of Persisting Mycobacteria in a Guinea Pig Model of Tuberculosis Revealed by R207910

Lenaerts, A. J., Hoff, D., Aly, S., Ehlers, S., Andries, K., Cantarero, L., Orme, I. M., & Basaraba, R. J. (2007) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00276-07 · Cited by 257

Unique Transcriptome Signature of Mycobacterium tuberculosis in Pulmonary Tuberculosis

Rachman, H., Strong, M., Ulrichs, T., Grode, L., Schuchhardt, J., Mollenkopf, H., Kosmiadi, G. A., Eisenberg, D., & Kaufmann, S. H. E. (2006) · Infection and Immunity · doi:10.1128/iai.74.2.1233-1242.2006 · Cited by 243

Global Assessment of Genomic Regions Required for Growth in Mycobacterium tuberculosis

Zhang, Y. J., Ioerger, T. R., Huttenhower, C., Long, J. E., Sassetti, C. M., Sacchettini, J. C., & Rubin, E. J. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002946 · Cited by 242

Advances in understanding E. coli cell fission

de Boer, P. A. (2010) · Current Opinion in Microbiology · doi:10.1016/j.mib.2010.09.015 · Cited by 231

Increased NOD2-mediated recognition of N-glycolyl muramyl dipeptide

Coulombe, F., Divangahi, M., Veyrier, F., de Léséleuc, L., Gleason, J. L., Yang, Y., Kelliher, M. A., Pandey, A. K., Sassetti, C. M., Reed, M. B., et al. (2009) · Journal of Experimental Medicine · doi:10.1084/jem.20081779 · Cited by 231

Chapter 2 Biogenesis of the Cell Wall and Other Glycoconjugates of Mycobacterium tuberculosis

Kaur, D., Guerin, M. E., Škovierová, H., Brennan, P. J., & Jackson, M. (2009) · Advances in Applied Microbiology · doi:10.1016/s0065-2164(09)69002-x · Cited by 226

Three redundant murein endopeptidases catalyse an essential cleavage step in peptidoglycan synthesis of Escherichia coli K 12

Singh, S. K., SaiSree, L., Amrutha, R. N., & Reddy, M. (2012) · Molecular Microbiology · doi:10.1111/mmi.12058 · Cited by 214

Letting Sleeping dos Lie: Does Dormancy Play a Role in Tuberculosis?

Chao, M. C., & Rubin, E. J. (2010) · Annual Review of Microbiology · doi:10.1146/annurev.micro.112408.134043 · Cited by 214

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 & Biology · doi:10.1016/j.chembiol.2012.03.006 · Cited by 210

Lipidomics reveals control of Mycobacterium tuberculosis virulence lipids via metabolic coupling

Jain, M., Petzold, C. J., Schelle, M. W., Leavell, M. D., Mougous, J. D., Bertozzi, C. R., Leary, J. A., & Cox, J. S. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0610634104 · Cited by 209

A Comparative Lipidomics Platform for Chemotaxonomic Analysis of Mycobacterium tuberculosis

Layre, E., Sweet, L., Hong, S., Madigan, C. A., Desjardins, D., Young, D. C., Cheng, T.-Y., Annand, J. W., Kim, K., Shamputa, I. C., et al. (2011) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.10.013 · Cited by 205

Deletion of kasB in Mycobacterium tuberculosis causes loss of acid-fastness and subclinical latent tuberculosis in immunocompetent mice

Bhatt, A., Fujiwara, N., Bhatt, K., Gurcha, S. S., Kremer, L., Chen, B., Chan, J., Porcelli, S. A., Kobayashi, K., Besra, G. S., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608654104 · Cited by 202

Identification of the namH Gene, Encoding the Hydroxylase Responsible for the N-Glycolylation of the Mycobacterial Peptidoglycan

Raymond, J. B., Mahapatra, S., Crick, D. C., & Pavelka, M. S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m411006200 · Cited by 199

CD271 + Bone Marrow Mesenchymal Stem Cells May Provide a Niche for Dormant Mycobacterium tuberculosis

Das, B., Kashino, S. S., Pulu, I., Kalita, D., Swami, V., Yeger, H., Felsher, D. W., & Campos-Neto, A. (2013) · Science Translational Medicine · doi:10.1126/scitranslmed.3004912 · Cited by 188

Division and cell envelope regulation by Ser/Thr phosphorylation: Mycobacterium shows the way

Molle, V., & Kremer, L. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.07041.x · Cited by 185

FtsZ Protofilaments Use a Hinge-Opening Mechanism for Constrictive Force Generation

Li, Y., Hsin, J., Zhao, L., Cheng, Y., Shang, W., Huang, K. C., Wang, H.-W., & Ye, S. (2013) · Science · doi:10.1126/science.1239248 · Cited by 178

Subpolar addition of new cell wall is directed by DivIVA in mycobacteria

Meniche, X., Otten, R., Siegrist, M. S., Baer, C. E., Murphy, K. C., Bertozzi, C. R., & Sassetti, C. M. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1402158111 · Cited by 175

Single-cell dynamics of the chromosome replication and cell division cycles in mycobacteria

Santi, I., Dhar, N., Bousbaine, D., Wakamoto, Y., & McKinney, J. D. (2013) · Nature Communications · doi:10.1038/ncomms3470 · Cited by 170

A Phosphorylated Pseudokinase Complex Controls Cell Wall Synthesis in Mycobacteria

Gee, C. L., Papavinasasundaram, K. G., Blair, S. R., Baer, C. E., Falick, A. M., King, D. S., Griffin, J. E., Venghatakrishnan, H., Zukauskas, A., Wei, J.-R., et al. (2012) · Science Signaling · doi:10.1126/scisignal.2002525 · Cited by 169

A Mycobacterial Enzyme Essential for Cell Division Synergizes with Resuscitation-Promoting Factor

Hett, E. C., Chao, M. C., Deng, L. L., & Rubin, E. J. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.1000001 · Cited by 169

Genetic Requirements for the Survival of Tubercle Bacilli in Primates

Dutta, N. K., Mehra, S., Didier, P. J., Roy, C. J., Doyle, L. A., Alvarez, X., Ratterree, M., Be, N. A., Lamichhane, G., Jain, S. K., et al. (2010) · The Journal of Infectious Diseases · doi:10.1086/652497 · Cited by 165

Acid-Susceptible Mutants of Mycobacterium tuberculosis Share Hypersusceptibility to Cell Wall and Oxidative Stress and to the Host Environment

Vandal, O. H., Roberts, J. A., Odaira, T., Schnappinger, D., Nathan, C. F., & Ehrt, S. (2009) · Journal of Bacteriology · doi:10.1128/jb.00932-08 · Cited by 163

A partner for the resuscitation‐promoting factors of Mycobacterium tuberculosis

Hett, E. C., Chao, M. C., Steyn, A. J., Fortune, S. M., Deng, L. L., & Rubin, E. J. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.05945.x · Cited by 159

FtsEX is required for CwlO peptidoglycan hydrolase activity during cell wall elongation in Bacillus subtilis

Meisner, J., Montero Llopis, P., Sham, L., Garner, E., Bernhardt, T. G., & Rudner, D. Z. (2013) · Molecular Microbiology · doi:10.1111/mmi.12330 · Cited by 158

Cell‐Wall Alterations as an Attribute of Mycobacterium tuberculosis in Latent Infection

Seiler, P., Ulrichs, T., Bandermann, S., Pradl, L., Jörg, S., Krenn, V., Morawietz, L., Kaufmann, S. H. E., & Aichele, P. (2003) · The Journal of Infectious Diseases · doi:10.1086/378563 · Cited by 157

Meropenem inhibits D , D ‐carboxypeptidase activity in M ycobacterium tuberculosis

Kumar, P., Arora, K., Lloyd, J. R., Lee, I. Y., Nair, V., Fischer, E. R., Boshoff, H. I., & Barry, C. E. (2012) · Molecular Microbiology · doi:10.1111/j.1365-2958.2012.08199.x · Cited by 156

Direct interaction of FtsZ and MreB is required for septum synthesis and cell division in Escherichia coli

Fenton, A. K., & Gerdes, K. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.129 · Cited by 150

The missing piece of the type II fatty acid synthase system from Mycobacterium tuberculosis

Sacco, E., Covarrubias, A. S., O’Hare, H. M., Carroll, P., Eynard, N., Jones, T. A., Parish, T., Daffé, M., Bäckbro, K., & Quémard, A. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0704132104 · Cited by 149

Regulation of cell wall morphogenesis in Bacillus subtilis by recruitment of PBP1 to the MreB helix

Kawai, Y., Daniel, R. A., & Errington, J. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06601.x · Cited by 146

Prokayrotic Ubiquitin-Like Protein (Pup) Proteome of Mycobacterium tuberculosis

Festa, R. A., McAllister, F. E., Pearce, M. J., Mintseris, J., Burns, K. E., Gygi, S. P., & Darwin, K. H. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008589 · Cited by 143

The Genetic Requirements for Fast and Slow Growth in Mycobacteria

Beste, D. J. V., Espasa, M., Bonde, B. K., Kierzek, A. M., Stewart, G. R., & McFadden, J. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005349 · Cited by 142

Interaction and Modulation of Two Antagonistic Cell Wall Enzymes of Mycobacteria

Hett, E. C., Chao, M. C., & Rubin, E. J. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1001020 · Cited by 133

GTPase Activity of Mycobacterial FtsZ Is Impaired Due to Its Transphosphorylation by the Eukaryotic-type Ser/Thr Kinase, PknA

Thakur, M., & Chakraborti, P. K. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607216200 · Cited by 124

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

“Depupylation” of prokaryotic ubiquitin-like protein from mycobacterial proteasome substrates

Burns, K., Cerda-Maira, F. A., Wang, T., Li, H.-L., Bishai, W., & Darwin, K. (2010) · Molecules and Cells · doi:10.1016/j.molcel.2010.07.019 · Cited by 122

Regulation of Polar Peptidoglycan Biosynthesis by Wag31 Phosphorylation in Mycobacteria

Jani, C., Eoh, H., Lee, J. J., Hamasha, K., Sahana, M. B., Han, J., Nyayapathy, S., Lee, J.-Y., Suh, J., Lee, S. H., et al. (2010) · BMC Microbiology · doi:10.1186/1471-2180-10-327 · Cited by 119

Antigen 84, an Effector of Pleiomorphism inMycobacterium smegmatis

Nguyen, L., Scherr, N., Gatfield, J., Walburger, A., Pieters, J., & Thompson, C. J. (2007) · Journal of Bacteriology · doi:10.1128/jb.00726-07 · Cited by 117

Interference of Mycobacterium tuberculosis cell division by Rv2719c, a cell wall hydrolase

Chauhan, A., Lofton, H., Maloney, E., Moore, J., Fol, M., Madiraju, M. V. V. S., & Rajagopalan, M. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05333.x · Cited by 116

Transcriptional Control of the Mycobacterial embCAB Operon by PknH through a Regulatory Protein, EmbR, In Vivo

Sharma, K., Gupta, M., Pathak, M., Gupta, N., Koul, A., Sarangi, S., Baweja, R., & Singh, Y. (2006) · Journal of Bacteriology · doi:10.1128/jb.188.8.2936-2944.2006 · Cited by 113

Mycobacterial Lipid II Is Composed of a Complex Mixture of Modified Muramyl and Peptide Moieties Linked to Decaprenyl Phosphate

Mahapatra, S., Yagi, T., Belisle, J. T., Espinosa, B. J., Hill, P. J., McNeil, M., Brennan, P. J., & Crick, D. C. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.8.2747-2757.2005 · Cited by 108

Targeting the Formation of the Cell Wall Core of M. tuberculosis

Barry, C. E., Crick, D. C., & McNeil, M. (2007) · Infectious Disorders - Drug Targets · doi:10.2174/187152607781001808 · Cited by 107

Cell Division Site Placement and Asymmetric Growth in Mycobacteria

Joyce, G., Williams, K. J., Robb, M. L., Noens, E. E. E., Tizzano, B., Shahrezaei, V., & Robertson, B. D. (2012) · PLoS ONE · doi:10.1371/journal.pone.0044582 · Cited by 105

Colocalization and interaction between elongasome and divisome during a preparative cell division phase in E scherichia coli

van der Ploeg, R., Verheul, J., Vischer, N. O. E., Alexeeva, S., Hoogendoorn, E., Postma, M., Banzhaf, M., Vollmer, W., & den Blaauwen, T. (2013) · Molecular Microbiology · doi:10.1111/mmi.12150 · Cited by 104

Nonclassical Transpeptidases of Mycobacterium tuberculosis Alter Cell Size, Morphology, the Cytosolic Matrix, Protein Localization, Virulence, and Resistance to β-Lactams

Schoonmaker, M. K., Bishai, W. R., & Lamichhane, G. (2014) · Journal of Bacteriology · doi:10.1128/jb.01396-13 · Cited by 104

Interaction between FtsW and penicillin‐binding protein 3 (PBP3) directs PBP3 to mid‐cell, controls cell septation and mediates the formation of a trimeric complex involving FtsZ, FtsW and PBP3 in mycobacteria

Datta, P., Dasgupta, A., Singh, A. K., Mukherjee, P., Kundu, M., & Basu, J. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05491.x · Cited by 103

N Glycolylation of the Nucleotide Precursors of Peptidoglycan Biosynthesis of Mycobacterium spp. Is Altered by Drug Treatment

Mahapatra, S., Scherman, H., Brennan, P. J., & Crick, D. C. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.7.2341-2347.2005 · Cited by 103

The Reductase That Catalyzes Mycolic Motif Synthesis Is Required for Efficient Attachment of Mycolic Acids to Arabinogalactan

Lea‐Smith, D. J., Pyke, J. S., Tull, D., McConville, M. J., Coppel, R. L., & Crellin, P. K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608686200 · Cited by 100

The Dual Function of the Mycobacterium tuberculosis FadD32 Required for Mycolic Acid Biosynthesis

Léger, M., Gavalda, S., Guillet, V., van der Rest, B., Slama, N., Montrozier, H. L., Mourey, L., Quémard, A., Daffé, M., & Marrakchi, H. (2009) · Chemistry & Biology · doi:10.1016/j.chembiol.2009.03.012 · Cited by 97

Molecular structure of the Mycobacterium tuberculosis virulence factor, mycolic acid, determines the elicited inflammatory pattern

Beken, S. V., Dulayymi, J. R. A., Naessens, T., Koza, G., Maza-Iglesias, M., Rowles, R. R., Theunissen, C., Medts, J. D., Lanckacker, E. A., Baird, M. S., et al. (2010) · European Journal of Immunology · doi:10.1002/eji.201040719 · Cited by 95

Mycobacterium tuberculosis Proteins Involved in Mycolic Acid Synthesis and Transport Localize Dynamically to the Old Growing Pole and Septum

Carel, C., Nukdee, K., Cantaloube, S., Bonne, M., Diagne, C. T., Laval, F., Daffé, M., & Zerbib, D. (2014) · PLoS ONE · doi:10.1371/journal.pone.0097148 · Cited by 94

Novel role of Wag31 in protection of mycobacteria under oxidative stress

Mukherjee, P., Sureka, K., Datta, P., Hossain, T., Barik, S., Das, K. P., Kundu, M., & Basu, J. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06750.x · Cited by 90

Structure and Functional Regulation of RipA, a Mycobacterial Enzyme Essential for Daughter Cell Separation

Ruggiero, A., Marasco, D., Squeglia, F., Soldini, S., Pedone, E. M., Pedone, C., & Berisio, R. (2010) · Structure · doi:10.1016/j.str.2010.06.007 · Cited by 86

Mycobacterium tuberculosis Lacking All Mycolic Acid Cyclopropanation Is Viable but Highly Attenuated and Hyperinflammatory in Mice

Barkan, D., Hedhli, D., Yan, H.-G., Huygen, K., & Glickman, M. S. (2012) · Infection and Immunity · doi:10.1128/iai.00021-12 · Cited by 85

Mycobacterium tuberculosis FtsX extracellular domain activates the peptidoglycan hydrolase, RipC

Mavrici, D., Marakalala, M. J., Holton, J. M., Prigozhin, D. M., Gee, C. L., Zhang, Y. J., Rubin, E. J., & Alber, T. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321812111 · Cited by 81

Phosphorylation of the Mycobacterium tuberculosis β-Ketoacyl-Acyl Carrier Protein Reductase MabA Regulates Mycolic Acid Biosynthesis

Veyron-Churlet, R., Zanella-Cléon, I., Cohen-Gonsaud, M., Molle, V., & Kremer, L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.105189 · Cited by 80

Mycobacterium tuberculosis CwsA Interacts with CrgA and Wag31, and the CrgA-CwsA Complex Is Involved in Peptidoglycan Synthesis and Cell Shape Determination

Płociński, P., Arora, N., Sarva, K., Blaszczyk, E., Qin, H., Das, N., Płocińska, R., Ziolkiewicz, M., Dziadek, J., Kiran, M., et al. (2012) · Journal of Bacteriology · doi:10.1128/jb.01005-12 · Cited by 80

Biological Consequences and Advantages of Asymmetric Bacterial Growth

Kysela, D. T., Brown, P., Huang, K. C., & Brun, Y. V. (2013) · Annual Review of Microbiology · doi:10.1146/annurev-micro-092412-155622 · Cited by 79

Septal Localization of the Mycobacterium tuberculosis MtrB Sensor Kinase Promotes MtrA Regulon Expression

Płocińska, R., Gorla, P., Sarva, K., Vadrevu, I. S., Pandeeti, E. V. P., Arora, N., Płociński, P., Madiraju, M. V. V. S., & Rajagopalan, M. R. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.346544 · Cited by 78

Mycobacterium tuberculosis Origin of Replication and the Promoter for Immunodominant Secreted Antigen 85B Are the Targets of MtrA, the Essential Response Regulator

Rajagopalan, M. R., Dziedzic, R., Alzayer, M., Stankowska, D. L., Ouimet, M.-C., Bastedo, D. P., Marczynski, G. T., & Madiraju, M. V. V. S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.040097 · Cited by 76

Asymmetric growth and division in M ycobacterium spp.: compensatory mechanisms for non‐medial septa

Singh, B., Nitharwal, R. G., Ramesh, M., Pettersson, B. M. F., Kirsebom, L. A., & Dasgupta, S. (2013) · Molecular Microbiology · doi:10.1111/mmi.12169 · Cited by 73

Phosphorylation of InhA inhibits mycolic acid biosynthesis and growth of Mycobacterium tuberculosis

Molle, V., Gülten, G., Vilchèze, C., Veyron‐Churlet, R., Zanella‐Cléon, I., Sacchettini, J. C., Jacobs, W. R., & Kremer, L. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07446.x · Cited by 73

Cell polarity and the control of apical growth in Streptomyces

Flärdh, K. (2010) · Current Opinion in Microbiology · doi:10.1016/j.mib.2010.10.002 · Cited by 72

AftD, a novel essential arabinofuranosyltransferase from mycobacteria

Škovierová, H., Larrouy-Maumus, G. J., Zhang, J., Kaur, D., Barilone, N., Korduláková, J., Gilleron, M., Guadagnini, S., Beláňová, M., Prévost, M., et al. (2009) · Glycobiology · doi:10.1093/glycob/cwp116 · Cited by 72

Phosphorylation of Mycobacterial PcaA Inhibits Mycolic Acid Cyclopropanation

Corrales, R. M., Molle, V., Leiba, J., Mourey, L., de Chastellier, C., & Kremer, L. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.373209 · Cited by 70

Characterization of CrgA, a New Partner of the Mycobacterium tuberculosis Peptidoglycan Polymerization Complexes

Płociński, P., Ziolkiewicz, M., Kiran, M., Vadrevu, S., Nguyen, H. B., Hugonnet, J., Veckerlé, C., Arthur, M., Dziadek, J., Cross, T. A., et al. (2011) · Journal of Bacteriology · doi:10.1128/jb.00188-11 · Cited by 68

Mycobacterium tuberculosis ClpX Interacts with FtsZ and Interferes with FtsZ Assembly

Dziedzic, R., Kiran, M., Płociński, P., Ziolkiewicz, M., Brzostek, A. M., Moomey, M., Vadrevu, I. S., Dziadek, J., Madiraju, M. V. V. S., & Rajagopalan, M. R. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011058 · Cited by 67

Comparative genomics for mycobacterial peptidoglycan remodelling enzymes reveals extensive genetic multiplicity

Machowski, E. E., Senzani, S., Ealand, C. S., & Kana, B. D. (2014) · BMC Microbiology · doi:10.1186/1471-2180-14-75 · Cited by 65

Protein Complexes and Proteolytic Activation of the Cell Wall Hydrolase RipA Regulate Septal Resolution in Mycobacteria

Chao, M. C., Kieser, K. J., Minami, S., Mavrici, D., Aldridge, B. B., Fortune, S. M., Alber, T., & Rubin, E. J. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003197 · Cited by 61

Transcriptional regulation of lipid homeostasis in mycobacteria

Salzman, V., Mondino, S., Sala, C., Cole, S. T., Gago, G., & Gramajo, H. C. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07313.x · Cited by 58

N-Glycolylated Peptidoglycan Contributes to the Immunogenicity but Not Pathogenicity of Mycobacterium tuberculosis

Hansen, J. M., Surano, S., Veyrier, F. J., Domenech, P., Boneca, I. G., Azad, A. K., Rajaram, M. V. S., Schlesinger, L. S., Divangahi, M., Reed, M. B., et al. (2013) · The Journal of Infectious Diseases · doi:10.1093/infdis/jit622 · Cited by 58

A Role for the Class A Penicillin-Binding Protein PonA2 in the Survival ofMycobacterium smegmatisunder Conditions of Nonreplication

Patru, M.-M., & Pavelka, M. S. (2010) · Journal of Bacteriology · doi:10.1128/jb.00025-10 · Cited by 55

Transcriptional regulation of fatty acid biosynthesis in mycobacteria

Mondino, S., Gago, G., & Gramajo, H. C. (2013) · Molecular Microbiology · doi:10.1111/mmi.12282 · Cited by 49

Mutants of Mycobacterium smegmatis impaired in stationary-phase survival The GenBank accession numbers for the sequences determined in this work are: AJ277088 (mutant 272A), AJ277089 (mutant 272E), AJ27790 (mutant 317C), AJ277152 (mutant 492A) and AJ276883 (mutant 3910D).

Keer, J. T., Smeulders, M. J., Gray, K. M., & Williams, H. D. (2000) · Microbiology · doi:10.1099/00221287-146-9-2209 · Cited by 49

Biosynthetic Origin of the Galactosamine Substituent of Arabinogalactan in Mycobacterium tuberculosis

Škovierová, H., Larrouy-Maumus, G. J., Pham, H. T. T., Beláňová, M., Barilone, N., DasGupta, A., Mikušová, K., Gicquel, B., Gilleron, M., Brennan, P. J., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.188110 · Cited by 46

Mycobacterium tuberculosis septum site determining protein, Ssd encoded by rv3660c, promotes filamentation and elicits an alternative metabolic and dormancy stress response

England, K., Crew, R. M., & Slayden, R. A. (2011) · BMC Microbiology · doi:10.1186/1471-2180-11-79 · Cited by 45

Identification of a novel peptidoglycan hydrolase CwlM in Mycobacterium tuberculosis

Deng, L. L., Humphries, D. E., Arbeit, R. D., Carlton, L. E., Smole, S., & Carroll, J. D. (2004) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.09.021 · Cited by 40

Ligation of arabinogalactan to peptidoglycan in the cell wall of Mycobacterium smegmatis requires concomitant synthesis of the two wall polymers

Hancock, I. C., Carman, S., Besra, G. S., Brennan, P. J., & Waite, E. (2002) · Microbiology · doi:10.1099/00221287-148-10-3059 · Cited by 37

Morphological features and signature gene response elicited by inactivation of FtsI in Mycobacterium tuberculosis

Slayden, R. A., & Belisle, J. T. (2008) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkn507 · Cited by 34

Identification of genes of Mycobacterium tuberculosis upregulated during anaerobic persistence by fluorescence and kanamycin resistance selection

Saxena, A., Srivastava, V., Srivastava, R., & Srivastava, B. S. (2008) · Tuberculosis · doi:10.1016/j.tube.2008.01.003 · Cited by 27

Mycobacterium tuberculosis CwsA overproduction modulates cell division and cell wall synthesis

Płociński, P., Martinez, L. A., Sarva, K., Płocińska, R., Madiraju, M. V. V. S., & Rajagopalan, M. R. (2013) · Tuberculosis · doi:10.1016/s1472-9792(13)70006-4 · Cited by 21

Distinguishing between resistance, tolerance and persistence to antibiotic treatment

Brauner, A., Fridman, O., Gefen, O., & Balaban, N. Q. (2016) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2016.34 · Cited by 1,612

Anti-tuberculosis treatment strategies and drug development: challenges and priorities

Dartois, V. A., & Rubin, E. J. (2022) · Nature Reviews Microbiology · doi:10.1038/s41579-022-00731-y · Cited by 490

Heterogeneity in tuberculosis

Cadena, A. M., Fortune, S. M., & Flynn, J. L. (2017) · Nature Reviews Immunology · doi:10.1038/nri.2017.69 · Cited by 484

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

Staying in Shape: the Impact of Cell Shape on Bacterial Survival in Diverse Environments

Yang, D. C., Blair, K. M., & Salama, N. R. (2016) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00031-15 · Cited by 295