Massive gene decay in the leprosy bacillus.

Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence

Cole, S. T., Brosch, R., Parkhill, J., Garnier, T., Churcher, C., Harris, D., Gordon, S. V., Eiglmeier, K., Gas, S., Barry, C. E., et al. (1998) · Nature · doi:10.1038/31159 · Cited by 7,847

Artemis: sequence visualization and annotation

Rutherford, K. M., Parkhill, J., Crook, J., Horsnell, T., Rice, P., Rajandream, M., & Barrell, B. (2000) · Bioinform. · doi:10.1093/bioinformatics/16.10.944 · Cited by 3,295

The genome sequence of Rickettsia prowazekii and the origin of mitochondria

Andersson, S. G. E., Zomorodipour, A., Andersson, J. O., Sicheritz-Pontén, T., Alsmark, U. C. M., Podowski, R. M., Näslund, A. K., Eriksson, A.-S., Winkler, H. H., & Kurland, C. G. (1998) · Nature · doi:10.1038/24094 · Cited by 1,697

Persistence of Mycobacterium tuberculosis in macrophages and mice requires the glyoxylate shunt enzyme isocitrate lyase

McKinney, J. D., zu Bentrup, K. H., Muñoz‐Elías, E. J., Miczák, A., Chen, B., Chan, W.-T., Swenson, D. L., Sacchettini, J. C., Jacobs, W. R., & Russell, D. G. (2000) · Nature · doi:10.1038/35021074 · Cited by 1,361

A new DNA sequence assembly program

Bonfield, J., Smith, K. F., & Staden, R. (1995) · Nucleic Acids Research · doi:10.1093/nar/23.24.4992 · Cited by 978

Issues in searching molecular sequence databases

Altschul, S. F., Boguski, M. S., Gish, W. R., & Wootton, J. C. (1994) · Nature Genetics · doi:10.1038/ng0294-119 · Cited by 773

Complex lipid determines tissue-specific replication of Mycobacterium tuberculosis in mice

Cox, J. S., Chen, B., McNeil, M., & Jacobs, W. R. (1999) · Nature · doi:10.1038/47042 · Cited by 746

The Envelope Layers of Mycobacteria with Reference to their Pathogenicity

Daffé, M., & Draper, P. (1997) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/s0065-2911(08)60016-8 · Cited by 727

Complete DNA sequence of a serogroup A strain of Neisseria meningitidis Z2491

Parkhill, J., Achtman, M., James, K., Bentley, S. D., Churcher, C. M., Klee, S. R., Morelli, G., Basham, D., Brown, D., Chillingworth, T., et al. (2000) · Nature · doi:10.1038/35006655 · Cited by 699

A Novel Mycolic Acid Cyclopropane Synthetase Is Required for Cording, Persistence, and Virulence of Mycobacterium tuberculosis

Glickman, M. S., Cox, J. S., & Jacobs, W. R. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80250-6 · Cited by 656

Crystal structure of uncleaved L ‐aspartate‐α‐decarboxylase from Mycobacterium tuberculosis

Gopalan, G., Chopra, S., Ranganathan, A., & Swaminathan, K. (2006) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21126 · Cited by 36

Linkage disequilibrium pattern and age-at-diagnosis are critical for replicating genetic associations across ethnic groups in leprosy

Alter, A., Fava, V. M., Hương, N. T., Singh, M. M., Orlova, M., Thuc, N. V., Katoch, K., Thai, V. H., Ba, N. N., Abel, L., et al. (2012) · Human Genetics · doi:10.1007/s00439-012-1227-6 · Cited by 36

Systemic dissemination in tuberculosis and leprosy: do mycobacterial adhesins play a role?

Pessolani, M. C. V., Marques, M. A. M., Reddy, V. M., Locht, C., & Menozzi, F. D. (2003) · Microbes and Infection · doi:10.1016/s1286-4579(03)00098-4 · Cited by 36

Use of Short Tandem Repeat Sequences to Study Mycobacterium leprae in Leprosy Patients in Malawi and India

Young, S. K., Pönnighaus, J. M., Jain, S., Lucas, S. B., Suneetha, S. K., Lockwood, D. N. J., Young, D. B., & Fine, P. (2008) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0000214 · Cited by 36

EspL is essential for virulence and stabilizes EspE, EspF and EspH levels in Mycobacterium tuberculosis

Sala, C., Odermatt, N. T., Soler-Arnedo, P., Gülen, M. F., von Schultz, S., Benjak, A., & Cole, S. T. (2018) · PLOS Pathogens · doi:10.1371/journal.ppat.1007491 · Cited by 35

Direct and Inverted Repeats Elicit Genetic Instability by Both Exploiting and Eluding DNA Double-Strand Break Repair Systems in Mycobacteria

Wójcik, E. A., Brzostek, A. M., Bacolla, A., Mackiewicz, P., Vásquez, K. M., Korycka‐Machała, M., Jaworski, A., & Dziadek, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0051064 · Cited by 34

Trend of case detection and leprosy elimination in Brazil

Penna, M. P., & Penna, G. O. (2007) · Tropical Medicine & International Health · doi:10.1111/j.1365-3156.2007.01837.x · Cited by 35

Clofazimine Modulates the Expression of Lipid Metabolism Proteins in Mycobacterium leprae-Infected Macrophages

Degang, Y., Akama, T., Hara, T., Tanigawa, K., Ishido, Y., Gidoh, M., Makino, M., Ishii, N., & Suzuki, K. (2012) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0001936 · Cited by 35

Tuberculosis vaccine strain Mycobacterium bovis BCG Russia is a natural recA mutant

Keller, P. M., Böttger, E. C., & Sander, P. (2008) · BMC Microbiology · doi:10.1186/1471-2180-8-120 · Cited by 36

Mycobacterium Tuberculosis Evolutionary Pathogenesis and its Putative Impact on Drug Development

Chevalier, F. L., Cascioferro, A., Majlessi, L., Herrmann, J., & Brosch, R. (2014) · Future Microbiology · doi:10.2217/fmb.14.70 · Cited by 40

Mycobacterial DNA-binding protein 1 is critical for long term survival of Mycobacterium smegmatis and simultaneously coordinates cellular functions

Enany, S., Yoshida, Y., Tateishi, Y., Ozeki, Y., Nishiyama, A., Savitskaya, A. G., Yamaguchi, T., Ohara, Y., Yamamoto, T., Ato, M., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-06480-w · Cited by 37

The immunology of other mycobacteria: M. ulcerans, M. leprae

Röltgen, K., Pluschke, G., Spencer, J. S., Brennan, P. J., & Avanzi, C. (2020) · Seminars in Immunopathology · doi:10.1007/s00281-020-00790-4 · Cited by 35

Bacterial Pathogenomics

(2007) · ASM Press eBooks · doi:10.1128/9781555815530 · Cited by 35

Ongoing Genome Reduction inMycobacterium ulcerans

Rondini, S., Käser, M., Stinear, T. P., Tessier, M., Mangold, C., Dernick, G., Martin, N., Portaels, F., Certa, U., & Pluschke, G. (2007) · Emerging infectious diseases · doi:10.3201/eid1307.060205 · Cited by 35

Comparative study of overlapping genes in bacteria, with special reference to Rickettsia prowazekii and Rickettsia conorii

Sakharkar, K. R., Sakharkar, M. K., Verma, C. S., & Chow, V. T. K. (2005) · INTERNATIONAL JOURNAL OF SYSTEMATIC AND EVOLUTIONARY MICROBIOLOGY · doi:10.1099/ijs.0.63446-0 · Cited by 35

Biochemical Function of msl5 ( pks8 plus pks17 ) in Mycobacterium tuberculosis H37Rv: Biosynthesis of Monomethyl Branched Unsaturated Fatty Acids

Dubey, V. S., Sirakova, T. D., Cynamon, M. H., & Kolattukudy, P. E. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.15.4620-4625.2003 · Cited by 35

Structural and functional features of Rhodococcus ruber lipoarabinomannan

Gibson, K. J. C., Gilleron, M., Constant, P., Puzo, G., Nigou, J., & Besra, G. S. (2003) · Microbiology · doi:10.1099/mic.0.26161-0 · Cited by 35

Essentiality and functional analysis of type I and type III pantothenate kinases of Mycobacterium tuberculosis

Awasthy, D., Ambady, A., Bhat, J., Sheikh, G., Ravishankar, S., Subbulakshmi, V., Mukherjee, K., Sambandamurthy, V. K., & Sharma, U. K. (2010) · Microbiology · doi:10.1099/mic.0.040717-0 · Cited by 35

The Complete Genome Sequence of the Emerging Pathogen Mycobacterium haemophilum Explains Its Unique Culture Requirements

Tufariello, J. M., Kerantzas, C. A., Vilchèze, C., Calder, R. B., Nordberg, E. K., Fischer, J. A., Hartman, T. E., Yang, E. M., Driscoll, T., Cole, L. E., et al. (2015) · mBio · doi:10.1128/mbio.01313-15 · Cited by 35

(Actino)Bacterial “intelligence”: using comparative genomics to unravel the information processing capacities of microbes

Pinto, D., & Mascher, T. (2016) · Current Genetics · doi:10.1007/s00294-016-0569-3 · Cited by 35

Horizontal Gene Acquisitions, Mobile Element Proliferation, and Genome Decay in the Host-Restricted Plant PathogenErwinia Tracheiphila

Shapiro, L. R., Scully, E. D., Straub, T. J., Park, J., Stephenson, A. G., Beattie, G. A., Gleason, M. L., Kolter, R., Coelho, M., Moraes, C. Μ. D., et al. (2016) · Genome Biology and Evolution · doi:10.1093/gbe/evw016 · Cited by 37

Bayesian phylogenetic analysis reveals two-domain topology of S-adenosylhomocysteine hydrolase protein sequences

Stępkowski, T., Brzeziński, K., Legocki, A. B., Jaskólski, M., & Béna, G. (2004) · Molecular Phylogenetics and Evolution · doi:10.1016/j.ympev.2004.09.008 · Cited by 36

A systematic investigation identifies a significant number of probable pseudogenes in the Escherichia coli genome

Homma, K., Fukuchi, S., Kawabata, T., Ota, M., & Nishikawa, K. (2002) · Gene · doi:10.1016/s0378-1119(02)00794-1 · Cited by 35

Importance of the immune response to Mycobacterium leprae in the skin

Jin, S.-H., Ahn, K. J., & An, S. (2018) · Biomedical Dermatology · doi:10.1186/s41702-017-0012-5 · Cited by 34

Mammalian cell entry genes in Streptomyces may provide clues to the evolution of bacterial virulence

Clark, L. C., Seipke, R. F., Prieto, P., Willemse, J. J., van Wezel, G. P., Hutchings, M. I., & Hoskisson, P. A. (2013) · Scientific Reports · doi:10.1038/srep01109 · Cited by 34

Transcriptional analysis of ESAT-6 cluster 3 in Mycobacterium smegmatis

Maciag, A. E., Piazza, A., Riccardi, G., & Milano, A. (2009) · BMC Microbiology · doi:10.1186/1471-2180-9-48 · Cited by 34

Enhancing Sensitivity of Detection of Immune Responses toMycobacterium lepraePeptides in Whole-Blood Assays

Geluk, A., Schip, J. J. V. D. P.-V., van Meijgaarden, K. E., Commandeur, S., Drijfhout, J. W., Benckhuijsen, W. E., Franken, K. L. M. C., Naafs, B., & Ottenhoff, T. H. M. (2010) · Clinical and Vaccine Immunology · doi:10.1128/cvi.00046-10 · Cited by 34

The Dream of a Mycobacterium

Baranowski, C., Rego, E. H., & Rubin, E. J. (2019) · Microbiology Spectrum · doi:10.1128/microbiolspec.gpp3-0008-2018 · Cited by 36

Gene amelioration demonstrated: the journey of nascent genes in bacteria

Marri, P. R., & Golding, G. B. (2008) · Genome · doi:10.1139/g07-105 · Cited by 34

Slow-Onset Inhibition of 2-trans-Enoyl-ACP (CoA) Reductase from Mycobacterium tuberculosis by an Inorganic Complex

de Oliveira, J. S., Sousa, E. H. S., de Souza, O. N., Moreira, L., Santos, D. S., & Basso, L. A. (2006) · Current Pharmaceutical Design · doi:10.2174/138161206777698927 · Cited by 34

A Comprehensive Overview of Mycolic Acid Structure and Biosynthesis

Marrakchi, H., Bardou, F., Lanéelle, M., & Daffé, M. (2014) · ASM Press eBooks · doi:10.1128/9781555815783.ch4 · Cited by 34

Characterisation of methionine adenosyltransferase from Mycobacterium smegmatis and M. tuberculosis

Berger, B. J., & Knodel, M. H. (2003) · BMC Microbiology · doi:10.1186/1471-2180-3-12 · Cited by 34

Principles of microbial alchemy: insights from the Streptomyces coelicolor genome sequence.

Thompson, C. J., Fink, D., & Nguyen, L. (2002) · Genome biology · doi:10.1186/gb-2002-3-7-reviews1020 · Cited by 34

HemZ is essential for heme biosynthesis in Mycobacterium tuberculosis

Parish, T., Schaeffer, M., Roberts, G., & Duncan, K. (2005) · Tuberculosis · doi:10.1016/j.tube.2005.01.002 · Cited by 33

A historical overview of leprosy epidemiology and control activities in Amazonas, Brazil

Cunha, C., Pedrosa, V. L., Dias, L. C., Braga, A. B. C., Chrusciak‐Talhari, A., Santos, M., Penna, G. O., Talhari, S., & Talhari, C. C. (2015) · Revista da Sociedade Brasileira de Medicina Tropical · doi:10.1590/0037-8682-0103-2013 · Cited by 33

Mitochondrial DNA Copy Number, but Not Haplogroup, Confers a Genetic Susceptibility to Leprosy in Han Chinese from Southwest China

Wang, D., Su, L., Zhang, A., Li, Y., Li, X.-A., Chen, L., Long, H., & Yao, Y. (2012) · PLoS ONE · doi:10.1371/journal.pone.0038848 · Cited by 33

“Pseudo-pseudogenes” in bacterial genomes: Proteogenomics reveals a wide but low protein expression of pseudogenes in Salmonella enterica

Feng, Y., Wang, Z., Chien, K., Chen, H., Liang, Y., Hua, X., & Chiu, C. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac302 · Cited by 33

The Rhodococcal Cell Envelope: Composition, Organisation and Biosynthesis

Sutcliffe, I. C., Brown, A. K., & Dover, L. G. (2010) · Microbiology monographs · doi:10.1007/978-3-642-12937-7_2 · Cited by 33

Ecological perspectives on the sequenced genome collection

Martiny, J. B. H., & Field, D. (2005) · Ecology Letters · doi:10.1111/j.1461-0248.2005.00837.x · Cited by 33

Validating divergent ORF annotation of the Mycobacterium leprae genome through a full translation data set and peptide identification by tandem mass spectrometry

de Souza, G. A., Søfteland, T., Koehler, C. J., Thiede, B., & Wiker, H. G. (2009) · PROTEOMICS · doi:10.1002/pmic.200800955 · Cited by 33

Ancient-DNA reveals an Asian type of Mycobacterium leprae in medieval Scandinavia

Economou, C., Kjellström, A., Lidén, K., & Panagopoulos, I. (2012) · Journal of Archaeological Science · doi:10.1016/j.jas.2012.07.005 · Cited by 33

The Bacterial Chromosome

Saier, M. H. (2008) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230801921262 · Cited by 33

Microbial Cytochromes P450

McLean, K. J., Leys, D., & Munro, A. W. (2015) · Springer eBooks · doi:10.1007/978-3-319-12108-6_6 · Cited by 36

Genome interdependence in insect-bacterium symbioses.

Zientz, E., Silva, F. J., & Gross, R. (2001) · Genome biology · doi:10.1186/gb-2001-2-12-reviews1032 · Cited by 33

An improved strategy for selective and efficient enrichment of integral plasma membrane proteins of mycobacteria

Mattow, J., Siejak, F., Hagens, K., Schmidt, F., Koehler, C. J., Treumann, A., Schaible, U. E., & Kaufmann, S. H. E. (2007) · PROTEOMICS · doi:10.1002/pmic.200600928 · Cited by 33

Identification of TwoMycobacterium marinumLoci That Affect Interactions with Macrophages

El‐Etr, S. H., Subbian, S., Cirillo, S. L. G., & Cirillo, J. D. (2004) · Infection and Immunity · doi:10.1128/iai.72.12.6902-6913.2004 · Cited by 33

Nitric oxide scavenging by Mycobacterium leprae GlbO involves the formation of the ferric heme-bound peroxynitrite intermediate

Ascenzi, P., Bocedi, A., Bolognesi, M., Fabozzi, G., Milani, M., & Visca, P. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.11.031 · Cited by 33

Genomic features beyond Chlamydia trachomatis phenotypes: What do we think we know?

Nunes, A., Borrego, M. J., & Gomes, J. P. (2013) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2013.03.018 · Cited by 32

Tetrahydroisoquinolines affect the whole-cell phenotype of Mycobacterium tuberculosis by inhibiting the ATP-dependent MurE ligase

Guzman, J., Pesnot, T., Barrera, D. A., Davies, H., McMahon, E., Evangelopoulos, D., Mortazavi, P., Munshi, T., Maitra, A., Lamming, E., et al. (2015) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkv010 · Cited by 32

Mechanistic insight into mycobacterial MmpL protein function

Székely, R., & Cole, S. T. (2015) · Molecular Microbiology · doi:10.1111/mmi.13306 · Cited by 32

Shortening Buruli Ulcer Treatment with Combination Therapy Targeting the Respiratory Chain and Exploiting Mycobacterium ulcerans Gene Decay

Converse, P. J., Almeida, D. V., Tyagi, S. K., Xu, J., & Nuermberger, E. L. (2019) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00426-19 · Cited by 32

Palaeomicrobiology: Application of Ancient DNA Sequencing to Better Understand Bacterial Genome Evolution and Adaptation

Arriola, L. A., Cooper, A., & Weyrich, L. S. (2020) · Frontiers in Ecology and Evolution · doi:10.3389/fevo.2020.00040 · Cited by 35

Origin and fate of pseudogenes in Hemiascomycetes: a comparative analysis

Lafontaine, I., & Dujon, B. (2010) · BMC Genomics · doi:10.1186/1471-2164-11-260 · Cited by 32

Factors Behind Junk DNA in Bacteria

Gil, R., & Latorre, A. (2012) · Genes · doi:10.3390/genes3040634 · Cited by 32

Characterization of phylogenetically distant members of the adenylate cyclase family from mycobacteria: Rv1647 fromMycobacterium tuberculosisand its orthologue ML1399 fromM. leprae

Shenoy, A. R., SREENATH, N. P., Mahalingam, M., & Visweswariah, S. S. (2005) · Biochemical Journal · doi:10.1042/bj20041040 · Cited by 32

Advances in environmental genomics: towards an integrated view of micro-organisms and ecosystems

Bertin, P. N., Médigue, C., & Normand, P. (2008) · Microbiology · doi:10.1099/mic.0.2007/011791-0 · Cited by 32

Rv0216, a conserved hypothetical protein from Mycobacterium tuberculosis that is essential for bacterial survival during infection, has a double hotdog fold

Castell, A., Johansson, P., Unge, T., Jones, T. A., & Bäckbro, K. (2005) · Protein Science · doi:10.1110/ps.051442305 · Cited by 32

The Silencing of Pseudogenes

Mira, Á., & Pushker, R. (2005) · Molecular Biology and Evolution · doi:10.1093/molbev/msi209 · Cited by 32

Association ofActinobacillus pleuropneumoniaeCapsular Polysaccharide with Virulence in Pigs

Bandara, A. B. P. A., Lawrence, M. L., Veit, H. P., & Inzana, T. J. (2003) · Infection and Immunity · doi:10.1128/iai.71.6.3320-3328.2003 · Cited by 32

An acyl-CoA dehydrogenase is involved in the formation of the Δcis3 double bond in the acyl residue of the lipopeptide antibiotic friulimicin in Actinoplanes friuliensis

Heinzelmann, E., Berger, S., Müller, C., Härtner, T., Poralla, K., Wohlleben, W., & Schwartz, D. (2005) · Microbiology · doi:10.1099/mic.0.27844-0 · Cited by 32

An Evolutionary Analysis of Lateral Gene Transfer in Thymidylate Synthase Enzymes

Stern, A., Mayrose, I., Penn, O., Shaul, S., Gophna, U., & Pupko, T. (2010) · Systematic Biology · doi:10.1093/sysbio/syp104 · Cited by 31

Infection with Mycobacterium lepromatosis

Scollard, D. M. (2016) · American Journal of Tropical Medicine and Hygiene · doi:10.4269/ajtmh.16-0473 · Cited by 32

Leprosy Transmission in Amazonian Countries: Current Status and Future Trends

Schaub, R., Avanzi, C., Singh, P., Paniz‐Mondolfi, A., Cardona-Castro, N. M., Légua, P., Crespo, L., Sewpersad, K., Dávila-Rodríguez, J. J., Barreto, J. G., et al. (2020) · Current Tropical Medicine Reports · doi:10.1007/s40475-020-00206-1 · Cited by 31

Recent advances in the molecular biology ofLeifsonia xylisubsp.xyli, causal organism of ratoon stunting disease

Brumbley, S. M., Petrasovits, L. A., Hermann, S. R., Young, A., & Croft, B. J. (2006) · Australasian Plant Pathology · doi:10.1071/ap06074 · Cited by 31

Comparative Studies of the Cell Structures of Mycobacterium leprae and M. tuberculosis Using the Electron Microscopy Freeze‐Substitution Technique

Takade, A., Umeda, A., Matsuoka, M., Yoshida, S., Nakamura, M., & Amako, K. (2003) · Microbiology and Immunology · doi:10.1111/j.1348-0421.2003.tb03394.x · Cited by 31

Evolutionary Process of Amino Acid Biosynthesis in Corynebacterium at the Whole Genome Level

Nishio, Y., Nakamura, Y., Usuda, Y., Sugimoto, S., Matsui, K., Kawarabayasi, Y., Kikuchi, H., Gojobori, T., & Ikeo, K. (2004) · Molecular Biology and Evolution · doi:10.1093/molbev/msh175 · Cited by 31

Mycobacterial genomics

Gordon, S. V., Brosch, R., Eiglmeier, K., Garnier, T., Hewinson, R. G., & Cole, S. T. (2002) · Transactions of the Royal Society of Tropical Medicine and Hygiene · doi:10.1016/s0035-9203(02)90222-1 · Cited by 31

Protection against Mycobacterium leprae Infection by the ID83/GLA-SE and ID93/GLA-SE Vaccines Developed for Tuberculosis

Duthie, M. S., Coler, R. N., Laurance, J. D., Sampaio, L. H. F., Oliveira, R. M., Sousa, A. L. M., Stefani, M. M. A., Maeda, Y., Matsuoka, M., Makino, M., et al. (2014) · Infection and Immunity · doi:10.1128/iai.02145-14 · Cited by 30

Experimental Infection of Rhodnius prolixus (Hemiptera, Triatominae) with Mycobacterium leprae Indicates Potential for Leprosy Transmission

Neumann, A. D. S., Dias, F. D. A., Ferreira, J. D. S., Fontes, A. N. B., Rosa, P. S., Macedo, R. E., Oliveira, J. H. M., Teixeira, R. L. D. F., Pessolani, M. C. V., Moraes, M. O., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0156037 · Cited by 30

Evolution of Mycobacterium tuberculosis : New Insights into Pathogenicity and Drug Resistance

Boritsch, E. C., & Brosch, R. (2016) · Microbiology Spectrum · doi:10.1128/microbiolspec.tbtb2-0020-2016 · Cited by 37

Modulation of the Response to Mycobacterium leprae and Pathogenesis of Leprosy

Cabral, N., de Figueiredo, V., Gandini, M., Souza, C. F., Medeiros, R. C. A., Lery, L. M. S., Lara, F. A., de Macedo, C. S., Pessolani, M. C. V., & Pereira, G. M. B. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.918009 · Cited by 37

Using Mycobacterium marinum and its hosts to study tuberculosis

Ramakrishnan, L. (2004) · Cited by 30

Tuberculosis in the 21st century: an emerging pandemic?

Bjune, G. A. (2009) · Norsk Epidemiologi · doi:10.5324/nje.v15i2.211 · Cited by 30

Single Nucleotide Polymorphism Analysis of European Archaeological M. leprae DNA

Watson, C. L., & Lockwood, D. N. J. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007547 · Cited by 30

Insights from the molecular docking of withanolide derivatives to the target protein PknG from Mycobacterium tuberculosis

Santhi, N., & Aishwarya, S. (2011) · Bioinformation · doi:10.6026/97320630007001 · Cited by 30

A high-throughput screening platform for inhibitors of the riboflavin biosynthesis pathway

Kaiser, J., Illarionov, B. A., Rohdich, F., Eisenreich, W., Saller, S., den Brulle, J. V., Cushman, M., Bacher, A., & Fischer, M. J. (2007) · Analytical Biochemistry · doi:10.1016/j.ab.2007.02.033 · Cited by 30

Biomarkers for Leprosy: would you prefer T (cells)?

Geluk, A. (2013) · Leprosy Review · doi:10.47276/lr.84.1.3 · Cited by 30

Comparative Genomics in Prokaryotes

Gregory, T. R., & DeSalle, R. (2005) · Elsevier eBooks · doi:10.1016/b978-012301463-4/50012-7 · Cited by 30

Intracellular Mycobacterium leprae Utilizes Host Glucose as a Carbon Source in Schwann Cells

Borah, K., Girardi, K. D. C. D. V., Mendum, T. A., Lery, L. M. S., Beste, D. J. V., Lara, F. A., Pessolani, M. C. V., & McFadden, J. (2019) · mBio · doi:10.1128/mbio.02351-19 · Cited by 30

Application of the Genome Sequence to Address Concerns That Mycobacterium avium Subspecies Paratuberculosis Might Be a Foodborne Pathogen

Bannantine, J. P., Barletta, R. G., Reffett, J. K., Paustian, M. L., & Kapur, V. (2004) · Foodborne Pathogens and Disease · doi:10.1089/153531404772914419 · Cited by 30

Nitric Oxide and Mycobacterium leprae Pathogenicity

Visca, P., Fabozzi, G., Milani, M., Bolognesi, M., & Ascenzi, P. (2002) · IUBMB Life · doi:10.1080/15216540214542 · Cited by 31

Heparin-binding hemagglutinin (HBHA) ofMycobacterium lepraeis expressed during infection and enhances bacterial adherence to epithelial cells

de Lima, C. S., Marques, M. A. M., Debrie, A., Almeida, E., Silva, C. A. M., Brennan, P. J., Sarno, E. N., Menozzi, F. D., & Pessolani, M. C. V. (2009) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2009.01488.x · Cited by 30

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Genome Trees from Conservation Profiles

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Honey, I shrunk the genome

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