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not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R25\",\"id\":\"R25\",\"title\":\"Pneumococcal PcsB: muralytic activity, exact bond unresolved, 2014.\"}]"},{"id":"REF0026","ids":["R26"],"title":"A highly active and negatively charged Streptococcus pyogenes lysin with a rare D-alanyl-L-alanine endopeptidase activity protects mice against streptococcal bacteremia.","url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC4068442/","urls":["https://pmc.ncbi.nlm.nih.gov/articles/PMC4068442/"],"year":2014,"doi":"10.1128/aac.00115-14","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Lood R","Raz A","Molina H","Euler CW","Fischetti VA"],"journal":"Antimicrob Agents Chemother","searchText":"[{\"source\":\"data.references\",\"path\":\"data.json/references/R26\",\"id\":\"R26\",\"title\":\"A highly active and negatively charged Streptococcus pyogenes lysin with a rare D-alanyl-L-alanine endopeptidase activity protects mice against streptococcal bacteremia.\"}]"},{"id":"REF0027","ids":["R27","ENT-P08"],"title":"Role of the Group B antigen of Streptococcus agalactiae: a peptidoglycan-anchored polysaccharide involved in cell wall biogenesis.","url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC3375309/","urls":["https://pmc.ncbi.nlm.nih.gov/articles/PMC3375309/"],"year":2012,"doi":"10.1371/journal.ppat.1002756","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Caliot É","Dramsi S","Chapot-Chartier MP","Courtin P","Kulakauskas S","Péchoux C","Trieu-Cuot P","Mistou MY"],"journal":"PLoS Pathog","searchText":"[{\"source\":\"digest.records\",\"path\":\"digest-evidence.json/records/15\",\"title\":\"Role of the Group B Antigen of Streptococcus agalactiae: A Peptidoglycan-Anchored Polysaccharide Involved in Cell Wall Biogenesis (2012)\",\"id\":\"ENT-P08\",\"context\":\"Streptococcus agalactiae\",\"locator\":\"Figure 7C; Cell wall-anchored GBC is required for normal PG structure; Purification and structural analysis of PG; supporting Text S1/Table S3 referenced\",\"access\":\"partial\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R27\",\"id\":\"R27\",\"title\":\"Role of the Group B antigen of Streptococcus agalactiae: a peptidoglycan-anchored polysaccharide involved in cell wall biogenesis.\"}]"},{"id":"REF0028","ids":["R28"],"title":"Streptococcus pyogenes Ser/Thr kinase-regulated cell wall hydrolase is a cell division plane-recognizing and chain-forming virulence factor.","url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC2945579/","urls":["https://pmc.ncbi.nlm.nih.gov/articles/PMC2945579/"],"year":2010,"doi":"10.1074/jbc.m110.153825","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Pancholi V","Boël G","Jin H"],"journal":"J Biol Chem","searchText":"[{\"source\":\"data.references\",\"path\":\"data.json/references/R28\",\"id\":\"R28\",\"title\":\"Streptococcus pyogenes Ser/Thr kinase-regulated cell wall hydrolase is a cell division plane-recognizing and chain-forming virulence factor.\"}]"},{"id":"REF0029","ids":["R29"],"title":"Identification of the asparagine synthase responsible for D-Asp amidation in the Lactococcus lactis peptidoglycan interpeptide crossbridge.","url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC2681893/","urls":["https://pmc.ncbi.nlm.nih.gov/articles/PMC2681893/"],"year":2009,"doi":"10.1128/jb.00126-09","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Veiga P","Erkelenz M","Bernard E","Courtin P","Kulakauskas S","Chapot-Chartier MP"],"journal":"J Bacteriol","searchText":"[{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/32/sources/0\",\"title\":\"L. lactis AsnH and D-Asp bridge amidation, 2009.\",\"context\":\"Lactococcus lactis\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R29\",\"id\":\"R29\",\"title\":\"Identification of the asparagine synthase responsible for D-Asp amidation in the Lactococcus lactis peptidoglycan interpeptide crossbridge.\"}]"},{"id":"REF0030","ids":["R30"],"title":"AcmA of Lactococcus lactis is an N-acetylglucosaminidase with an optimal number of LysM domains for proper functioning.","url":"https://pubmed.ncbi.nlm.nih.gov/15943817/","urls":["https://pubmed.ncbi.nlm.nih.gov/15943817/"],"year":2005,"doi":"10.1111/j.1742-4658.2005.04706.x","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Steen A","Buist G","Horsburgh GJ","Venema G","Kuipers OP","Foster SJ","Kok J"],"journal":"FEBS J","searchText":"[{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/32/sources/1\",\"title\":\"L. lactis AcmA glucosaminidase, 2005.\",\"context\":\"Lactococcus lactis\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R30\",\"id\":\"R30\",\"title\":\"AcmA of Lactococcus lactis is an N-acetylglucosaminidase with an optimal number of LysM domains for proper functioning.\"}]"},{"id":"REF0031","ids":["R31"],"title":"Characterization of AcmB, an N-acetylglucosaminidase autolysin from Lactococcus lactis.","url":"https://pubmed.ncbi.nlm.nih.gov/12634338/","urls":["https://pubmed.ncbi.nlm.nih.gov/12634338/"],"year":2003,"doi":"10.1099/mic.0.25875-0","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Huard C","Miranda G","Wessner F","Bolotin A","Hansen J","Foster SJ","Chapot-Chartier MP"],"journal":"Microbiology (Reading)","searchText":"[{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/32/sources/2\",\"title\":\"L. lactis AcmB glucosaminidase, 2003.\",\"context\":\"Lactococcus lactis\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R31\",\"id\":\"R31\",\"title\":\"Characterization of AcmB, an N-acetylglucosaminidase autolysin from Lactococcus lactis.\"}]"},{"id":"REF0032","ids":["R32","OA001"],"title":"Identification of key peptidoglycan hydrolases for morphogenesis, autolysis, and peptidoglycan composition of Lactobacillus plantarum WCFS1.","url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC3533731/","urls":["https://pmc.ncbi.nlm.nih.gov/articles/PMC3533731/"],"year":2012,"doi":"10.1186/1475-2859-11-137","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Rolain T","Bernard E","Courtin P","Bron PA","Kleerebezem M","Chapot-Chartier MP","Hols P"],"journal":"Microb Cell Fact","searchText":"[{\"source\":\"digest.records\",\"path\":\"digest-evidence.json/records/17\",\"title\":\"Rolain et al. (2012). Identification of key peptidoglycan hydrolases for morphogenesis, autolysis, and peptidoglycan composition of Lactobacillus plantarum WCFS1.\",\"id\":\"OA001\",\"context\":\"Lactiplantibacillus plantarum (published as Lactobacillus plantarum)\",\"locator\":\"Purification and structural analysis of peptidoglycan section\",\"access\":\"partial\"},{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/30/sources/0\",\"title\":\"L. plantarum Acm2/LytA and PG composition, 2012.\",\"context\":\"Lactiplantibacillus plantarum\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R32\",\"id\":\"R32\",\"title\":\"Identification of key peptidoglycan hydrolases for morphogenesis, autolysis, and peptidoglycan composition of Lactobacillus plantarum WCFS1.\"}]"},{"id":"REF0033","ids":["R33"],"title":"Distinct and Specific Role of NlpC/P60 Endopeptidases LytA and LytB in Cell Elongation and Division of Lactobacillus plantarum.","url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC6473061/","urls":["https://pmc.ncbi.nlm.nih.gov/articles/PMC6473061/"],"year":2019,"doi":"10.3389/fmicb.2019.00713","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Duchêne MC","Rolain T","Knoops A","Courtin P","Chapot-Chartier MP","Dufrêne YF","Hallet BF","Hols P"],"journal":"Front Microbiol","searchText":"[{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/30/sources/1\",\"title\":\"L. plantarum LytA/LytB, 2019.\",\"context\":\"Lactiplantibacillus plantarum\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R33\",\"id\":\"R33\",\"title\":\"Distinct and Specific Role of NlpC/P60 Endopeptidases LytA and LytB in Cell Elongation and Division of Lactobacillus plantarum.\"}]"},{"id":"REF0034","ids":["R34"],"title":"Synthetic lethality of the lytE cwlO genotype in Bacillus subtilis is caused by lack of D,L-endopeptidase activity at the lateral cell wall.","url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC3272963/","urls":["https://pmc.ncbi.nlm.nih.gov/articles/PMC3272963/"],"year":2012,"doi":"10.1128/jb.05569-11","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Hashimoto M","Ooiwa S","Sekiguchi J"],"journal":"J Bacteriol","searchText":"[{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/3/sources/0\",\"title\":\"B. subtilis LytE/CwlO D,L-endopeptidase activities, 2012.\",\"context\":\"Bacillus subtilis\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R34\",\"id\":\"R34\",\"title\":\"Synthetic lethality of the lytE cwlO genotype in Bacillus subtilis is caused by lack of D,L-endopeptidase activity at the lateral cell wall.\"}]"},{"id":"REF0035","ids":["R35"],"title":"SecA2-dependent secretion of autolytic enzymes promotes Listeria monocytogenes pathogenesis.","url":"https://pubmed.ncbi.nlm.nih.gov/14527997/","urls":["https://pubmed.ncbi.nlm.nih.gov/14527997/"],"year":2003,"doi":"10.1073/pnas.2133653100","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Lenz LL","Mohammadi S","Geissler A","Portnoy DA"],"journal":"Proc Natl Acad Sci U S A","searchText":"[{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/35/sources/0\",\"title\":\"Listeria p60 and NamA, 2003.\",\"context\":\"Listeria monocytogenes\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R35\",\"id\":\"R35\",\"title\":\"SecA2-dependent secretion of autolytic enzymes promotes Listeria monocytogenes pathogenesis.\"}]"},{"id":"REF0036","ids":["R36"],"title":"Listeria cell-wall loss study and hydrolase classes, 2024.","url":"https://www.nature.com/articles/s41467-024-52633-7","urls":["https://www.nature.com/articles/s41467-024-52633-7"],"year":2024,"doi":null,"metadataVerified":false,"metadataVerificationStatus":"no_exact_identifier","searchText":"[{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/35/sources/1\",\"title\":\"Listeria cell-wall loss study and hydrolase classes, 2024.\",\"context\":\"Listeria monocytogenes\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R36\",\"id\":\"R36\",\"title\":\"Listeria cell-wall loss study and hydrolase classes, 2024.\"}]"},{"id":"REF0037","ids":["R37","OA004"],"title":"Clostridium difficile has an original peptidoglycan structure with a high level of N-acetylglucosamine deacetylation and mainly 3-3 cross-links.","url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC3190713/","urls":["https://pmc.ncbi.nlm.nih.gov/articles/PMC3190713/"],"year":2011,"doi":"10.1074/jbc.m111.259150","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Peltier J","Courtin P","El Meouche I","Lemée L","Chapot-Chartier MP","Pons JL"],"journal":"J Biol Chem","searchText":"[{\"source\":\"digest.records\",\"path\":\"digest-evidence.json/records/19\",\"title\":\"Peltier et al. (2011). Clostridium difficile Has an Original Peptidoglycan Structure with a High Level of N-Acetylglucosamine Deacetylation and Mainly 3-3 Cross-links.\",\"id\":\"OA004\",\"context\":\"Clostridioides difficile (published as Clostridium difficile)\",\"locator\":\"Figure 1; Tables 1 and 2; Figure 5; Results discussion of peaks X, Y and Z\",\"access\":\"indexed\"},{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/16/sources/0\",\"title\":\"C. difficile PG: extensive deacetylation and 3-3 crosslinks, 2011.\",\"context\":\"Clostridioides difficile\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R37\",\"id\":\"R37\",\"title\":\"Clostridium difficile has an original peptidoglycan structure with a high level of N-acetylglucosamine deacetylation and mainly 3-3 cross-links.\"}]"},{"id":"REF0038","ids":["R38"],"title":"Ser/Thr Kinase-Dependent Phosphorylation of the Peptidoglycan Hydrolase CwlA Controls Its Export and Modulates Cell Division in Clostridioides difficile.","url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC8262956/","urls":["https://pmc.ncbi.nlm.nih.gov/articles/PMC8262956/"],"year":2021,"doi":"10.1128/mbio.00519-21","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Garcia-Garcia T","Poncet S","Cuenot E","Douché T","Giai Gianetto Q","Peltier J","Courtin P","Chapot-Chartier MP","Matondo M","Dupuy B","Candela T","Martin-Verstraete I"],"journal":"mBio","searchText":"[{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/16/sources/1\",\"title\":\"C. difficile CwlA, 2021.\",\"context\":\"Clostridioides difficile\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R38\",\"id\":\"R38\",\"title\":\"Ser/Thr Kinase-Dependent Phosphorylation of the Peptidoglycan Hydrolase CwlA Controls Its Export and Modulates Cell Division in Clostridioides difficile.\"}]"},{"id":"REF0039","ids":["R39"],"title":"Cwp19 Is a Novel Lytic Transglycosylase Involved in Stationary-Phase Autolysis Resulting in Toxin Release in Clostridium difficile.","url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC6016235/","urls":["https://pmc.ncbi.nlm.nih.gov/articles/PMC6016235/"],"year":2018,"doi":"10.1128/mbio.00648-18","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Wydau-Dematteis S","El Meouche I","Courtin P","Hamiot A","Lai-Kuen R","Saubaméa B","Fenaille F","Butel MJ","Pons JL","Dupuy B","Chapot-Chartier MP","Peltier J"],"journal":"mBio","searchText":"[{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/16/sources/2\",\"title\":\"C. difficile Cwp19 LT specificity, 2018.\",\"context\":\"Clostridioides difficile\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R39\",\"id\":\"R39\",\"title\":\"Cwp19 Is a Novel Lytic Transglycosylase Involved in Stationary-Phase Autolysis Resulting in Toxin Release in Clostridium difficile.\"}]"},{"id":"REF0040","ids":["R40"],"title":"Clostridioides difficile canonical L,D-transpeptidases catalyze a novel type of peptidoglycan cross-links and are not required for beta-lactam resistance.","url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC10792238/","urls":["https://pmc.ncbi.nlm.nih.gov/articles/PMC10792238/"],"year":2024,"doi":"10.1016/j.jbc.2023.105529","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Galley NF","Greetham D","Alamán-Zárate MG","Williamson MP","Evans CA","Spittal WD","Buddle JE","Freeman J","Davis GL","Dickman MJ","Wilcox MH","Lovering AL","Fagan RP","Mesnage S"],"journal":"J Biol Chem","searchText":"[{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/16/sources/3\",\"title\":\"C. difficile noncanonical crosslinks: assignments require care, 2024.\",\"context\":\"Clostridioides difficile\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R40\",\"id\":\"R40\",\"title\":\"Clostridioides difficile canonical L,D-transpeptidases catalyze a novel type of peptidoglycan cross-links and are not required for beta-lactam resistance.\"}]"},{"id":"REF0041","ids":["R41"],"title":"C. perfringens / Streptomyces LL-DAP-Gly structure, 1970.","url":"https://orbi.uliege.be/handle/2268/85150","urls":["https://orbi.uliege.be/handle/2268/85150"],"year":1970,"doi":null,"metadataVerified":false,"metadataVerificationStatus":"no_exact_identifier","searchText":"[{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/17/sources/0\",\"title\":\"C. perfringens / Streptomyces LL-DAP-Gly structure, 1970.\",\"context\":\"Clostridium perfringens\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R41\",\"id\":\"R41\",\"title\":\"C. perfringens / Streptomyces LL-DAP-Gly structure, 1970.\"}]"},{"id":"REF0042","ids":["R42","OA017"],"title":"Diaminopimelic Acid Amidation in Corynebacteriales: NEW INSIGHTS INTO THE ROLE OF LtsA IN PEPTIDOGLYCAN MODIFICATION.","url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC4505564/","urls":["https://pmc.ncbi.nlm.nih.gov/articles/PMC4505564/"],"year":2015,"doi":"10.1074/jbc.m115.642843","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Levefaudes M","Patin D","de Sousa-d'Auria C","Chami M","Blanot D","Hervé M","Arthur M","Houssin C","Mengin-Lecreulx D"],"journal":"J Biol Chem","searchText":"[{\"source\":\"digest.records\",\"path\":\"digest-evidence.json/records/31\",\"title\":\"Levefaudes et al. (2015). Diaminopimelic Acid Amidation in Corynebacteriales: New Insights into the Role of LtsA in Peptidoglycan Modification.\",\"id\":\"OA017\",\"context\":\"Corynebacterium glutamicum\",\"locator\":\"Peptidoglycan Purification and Structure Analysis section; Table 1 and its footnote a\",\"access\":\"partial\"},{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/18/sources/0\",\"title\":\"C. glutamicum LtsA-dependent DAP amidation, 2015.\",\"context\":\"Corynebacterium glutamicum\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R42\",\"id\":\"R42\",\"title\":\"Diaminopimelic Acid Amidation in Corynebacteriales: NEW INSIGHTS INTO THE ROLE OF LtsA IN PEPTIDOGLYCAN MODIFICATION.\"}]"},{"id":"REF0043","ids":["R43"],"title":"The peptidoglycan of stationary-phase Mycobacterium tuberculosis predominantly contains cross-links generated by L,D-transpeptidation.","url":"https://pubmed.ncbi.nlm.nih.gov/18408028/","urls":["https://pubmed.ncbi.nlm.nih.gov/18408028/"],"year":2008,"doi":"10.1128/jb.00239-08","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Lavollay M","Arthur M","Fourgeaud M","Dubost L","Marie A","Veziris N","Blanot D","Gutmann L","Mainardi JL"],"journal":"J Bacteriol","searchText":"[{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/39/sources/0\",\"title\":\"M. tuberculosis 3-3 crosslinks, 2008.\",\"context\":\"Mycobacterium tuberculosis\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R43\",\"id\":\"R43\",\"title\":\"The peptidoglycan of stationary-phase Mycobacterium tuberculosis predominantly contains cross-links generated by L,D-transpeptidation.\"}]"},{"id":"REF0044","ids":["R44","OA016"],"title":"Meropenem inhibits D,D-carboxypeptidase activity in Mycobacterium tuberculosis.","url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC3468717/","urls":["https://pmc.ncbi.nlm.nih.gov/articles/PMC3468717/"],"year":2012,"doi":"10.1111/j.1365-2958.2012.08199.x","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Kumar P","Arora K","Lloyd JR","Lee IY","Nair V","Fischer E","Boshoff HI","Barry CE"],"journal":"Mol Microbiol","searchText":"[{\"source\":\"digest.records\",\"path\":\"digest-evidence.json/records/30\",\"title\":\"M. tuberculosis peptidoglycan reference (2012; full text not verified)\",\"id\":\"OA016\",\"context\":\"Mycobacterium tuberculosis\",\"locator\":\"Full-text verification pending\",\"access\":\"partial\"},{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/39/sources/1\",\"title\":\"M. tuberculosis mature PG and amidation, 2012.\",\"context\":\"Mycobacterium tuberculosis\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R44\",\"id\":\"R44\",\"title\":\"Meropenem inhibits D,D-carboxypeptidase activity in Mycobacterium tuberculosis.\"}]"},{"id":"REF0045","ids":["R45"],"title":"Peptidoglycan Hydrolases RipA and Ami1 Are Critical for Replication and Persistence of Mycobacterium tuberculosis in the Host.","url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC7064781/","urls":["https://pmc.ncbi.nlm.nih.gov/articles/PMC7064781/"],"year":2020,"doi":"10.1128/mbio.03315-19","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Healy C","Gouzy A","Ehrt S"],"journal":"mBio","searchText":"[{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/39/sources/2\",\"title\":\"M. tuberculosis RipA/RipB/Ami1; CwlM is a regulator, 2020.\",\"context\":\"Mycobacterium tuberculosis\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R45\",\"id\":\"R45\",\"title\":\"Peptidoglycan Hydrolases RipA and Ami1 Are Critical for Replication and Persistence of Mycobacterium tuberculosis in the Host.\"}]"},{"id":"REF0046","ids":["R46"],"title":"Three redundant murein endopeptidases catalyse an essential cleavage step in peptidoglycan synthesis of Escherichia coli K12.","url":"https://pubmed.ncbi.nlm.nih.gov/23062283/","urls":["https://pubmed.ncbi.nlm.nih.gov/23062283/"],"year":2012,"doi":"10.1111/mmi.12058","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Singh SK","SaiSree L","Amrutha RN","Reddy M"],"journal":"Mol Microbiol","searchText":"[{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/23/sources/0\",\"title\":\"E. coli MepS/MepM/MepH cleavage, 2012.\",\"context\":\"Escherichia coli\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R46\",\"id\":\"R46\",\"title\":\"Three redundant murein endopeptidases catalyse an essential cleavage step in peptidoglycan synthesis of Escherichia coli K12.\"}]"},{"id":"REF0047","ids":["R47"],"title":"Role of endopeptidases in peptidoglycan synthesis mediated by alternative cross-linking enzymes in Escherichia coli.","url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC8488565/","urls":["https://pmc.ncbi.nlm.nih.gov/articles/PMC8488565/"],"year":2021,"doi":"10.15252/embj.2021108126","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Voedts H","Dorchêne D","Lodge A","Vollmer W","Arthur M","Hugonnet JE"],"journal":"EMBO J","searchText":"[{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/23/sources/1\",\"title\":\"E. coli endopeptidases and alternative crosslinks, 2021.\",\"context\":\"Escherichia coli\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R47\",\"id\":\"R47\",\"title\":\"Role of endopeptidases in peptidoglycan synthesis mediated by alternative cross-linking enzymes in Escherichia coli.\"}]"},{"id":"REF0048","ids":["R48","OA006"],"title":"A Proteolytic Complex Targets Multiple Cell Wall Hydrolases in Pseudomonas aeruginosa.","url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC6050968/","urls":["https://pmc.ncbi.nlm.nih.gov/articles/PMC6050968/"],"year":2018,"doi":"10.1128/mbio.00972-18","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Srivastava D","Seo J","Rimal B","Kim SJ","Zhen S","Darwin AJ"],"journal":"mBio","searchText":"[{\"source\":\"digest.records\",\"path\":\"digest-evidence.json/records/20\",\"title\":\"A Proteolytic Complex Targets Multiple Cell Wall Hydrolases in Pseudomonas aeruginosa (2018).\",\"id\":\"OA006\",\"context\":\"Pseudomonas aeruginosa\",\"locator\":\"Figure 6 and supplementary Figure S1\",\"access\":\"indexed\"},{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/44/sources/0\",\"title\":\"P. aeruginosa MepM and other PG hydrolases, 2018.\",\"context\":\"Pseudomonas aeruginosa\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R48\",\"id\":\"R48\",\"title\":\"A Proteolytic Complex Targets Multiple Cell Wall Hydrolases in Pseudomonas aeruginosa.\"}]"},{"id":"REF0049","ids":["R49"],"title":"A New Class of Cell Wall-Recycling l,d-Carboxypeptidase Determines β-Lactam Susceptibility and Morphogenesis in Acinetobacter baumannii.","url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC8649774/","urls":["https://pmc.ncbi.nlm.nih.gov/articles/PMC8649774/"],"year":2021,"doi":"10.1128/mbio.02786-21","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Dai Y","Pinedo V","Tang AY","Cava F","Geisinger E"],"journal":"mBio","searchText":"[{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/0/sources/0\",\"title\":\"A. baumannii ElsL is an LD-carboxypeptidase, 2021.\",\"context\":\"Acinetobacter baumannii\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R49\",\"id\":\"R49\",\"title\":\"A New Class of Cell Wall-Recycling l,d-Carboxypeptidase Determines β-Lactam Susceptibility and Morphogenesis in Acinetobacter baumannii.\"}]"},{"id":"REF0050","ids":["R50"],"title":"Peptidoglycan Recycling Promotes Outer Membrane Integrity and Carbapenem Tolerance in Acinetobacter baumannii.","url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC9239154/","urls":["https://pmc.ncbi.nlm.nih.gov/articles/PMC9239154/"],"year":2022,"doi":"10.1128/mbio.01001-22","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Islam N","Kazi MI","Kang KN","Biboy J","Gray J","Ahmed F","Schargel RD","Boutte CC","Dörr T","Vollmer W","Boll JM"],"journal":"mBio","searchText":"[{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/0/sources/1\",\"title\":\"A. baumannii PBP7 and PG recycling, 2022.\",\"context\":\"Acinetobacter baumannii\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R50\",\"id\":\"R50\",\"title\":\"Peptidoglycan Recycling Promotes Outer Membrane Integrity and Carbapenem Tolerance in Acinetobacter baumannii.\"}]"},{"id":"REF0051","ids":["R51","OA010"],"title":"Substrate specificity of an elongation-specific peptidoglycan endopeptidase and its implications for cell wall architecture and growth of Vibrio cholerae.","url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC3769093/","urls":["https://pmc.ncbi.nlm.nih.gov/articles/PMC3769093/"],"year":2013,"doi":"10.1111/mmi.12323","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Dörr T","Cava F","Lam H","Davis BM","Waldor MK"],"journal":"Mol Microbiol","searchText":"[{\"source\":\"digest.records\",\"path\":\"digest-evidence.json/records/24\",\"title\":\"Substrate specificity of an elongation-specific peptidoglycan endopeptidase and its implications for cell wall architecture and growth of Vibrio cholerae (2013).\",\"id\":\"OA010\",\"context\":\"Vibrio cholerae\",\"locator\":\"HPLC analysis of PG and muropeptide identification section\",\"access\":\"indexed\"},{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/63/sources/0\",\"title\":\"V. cholerae ShyA cleavage, 2013.\",\"context\":\"Vibrio cholerae\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R51\",\"id\":\"R51\",\"title\":\"Substrate specificity of an elongation-specific peptidoglycan endopeptidase and its implications for cell wall architecture and growth of Vibrio cholerae.\"}]"},{"id":"REF0052","ids":["R52"],"title":"The AmiC/NlpD Pathway Dominates Peptidoglycan Breakdown in Neisseria meningitidis and Affects Cell Separation, NOD1 Agonist Production, and Infection.","url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC8929373/","urls":["https://pmc.ncbi.nlm.nih.gov/articles/PMC8929373/"],"year":2022,"doi":"10.1128/iai.00485-21","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Chan JM","Hackett KT","Woodhams KL","Schaub RE","Dillard JP"],"journal":"Infect Immun","searchText":"[{\"source\":\"data.references\",\"path\":\"data.json/references/R52\",\"id\":\"R52\",\"title\":\"The AmiC/NlpD Pathway Dominates Peptidoglycan Breakdown in Neisseria meningitidis and Affects Cell Separation, NOD1 Agonist Production, and Infection.\"}]"},{"id":"REF0053","ids":["R53"],"title":"Multiple peptidoglycan modification networks modulate Helicobacter pylori's cell shape, motility, and colonization potential.","url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC3310797/","urls":["https://pmc.ncbi.nlm.nih.gov/articles/PMC3310797/"],"year":2012,"doi":"10.1371/journal.ppat.1002603","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Sycuro LK","Wyckoff TJ","Biboy J","Born P","Pincus Z","Vollmer W","Salama NR"],"journal":"PLoS Pathog","searchText":"[{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/12/sources/0\",\"title\":\"H. pylori Csd enzymes and PG modification, 2012.\",\"context\":\"Campylobacter jejuni\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/27/sources/0\",\"title\":\"H. pylori Csd enzymes and PG modification, 2012.\",\"context\":\"Helicobacter pylori\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R53\",\"id\":\"R53\",\"title\":\"Multiple peptidoglycan modification networks modulate Helicobacter pylori's cell shape, motility, and colonization potential.\"}]"},{"id":"REF0054","ids":["R54"],"title":"Peptidoglycan LD-carboxypeptidase Pgp2 influences Campylobacter jejuni helical cell shape and pathogenic properties and provides the substrate for the DL-carboxypeptidase Pgp1.","url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC3961634/","urls":["https://pmc.ncbi.nlm.nih.gov/articles/PMC3961634/"],"year":2014,"doi":"10.1074/jbc.m113.491829","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Frirdich E","Vermeulen J","Biboy J","Soares F","Taveirne ME","Johnson JG","DiRita VJ","Girardin SE","Vollmer W","Gaynor EC"],"journal":"J Biol Chem","searchText":"[{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/12/sources/1\",\"title\":\"C. jejuni Pgp2/Pgp1 cleavage sequence, 2014.\",\"context\":\"Campylobacter jejuni\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/27/sources/1\",\"title\":\"C. jejuni Pgp2/Pgp1 cleavage sequence, 2014.\",\"context\":\"Helicobacter pylori\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R54\",\"id\":\"R54\",\"title\":\"Peptidoglycan LD-carboxypeptidase Pgp2 influences Campylobacter jejuni helical cell shape and pathogenic properties and provides the substrate for the DL-carboxypeptidase Pgp1.\"}]"},{"id":"REF0055","ids":["R55"],"title":"Multiple Campylobacter jejuni proteins affecting the peptidoglycan structure and the degree of helical cell curvature.","url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC10151779/","urls":["https://pmc.ncbi.nlm.nih.gov/articles/PMC10151779/"],"year":2023,"doi":"10.3389/fmicb.2023.1162806","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Frirdich E","Vermeulen J","Biboy J","Vollmer W","Gaynor EC"],"journal":"Front Microbiol","searchText":"[{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/12/sources/2\",\"title\":\"C. jejuni Pgp enzyme characterization, 2023.\",\"context\":\"Campylobacter jejuni\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/27/sources/2\",\"title\":\"C. jejuni Pgp enzyme characterization, 2023.\",\"context\":\"Helicobacter pylori\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R55\",\"id\":\"R55\",\"title\":\"Multiple Campylobacter jejuni proteins affecting the peptidoglycan structure and the degree of helical cell curvature.\"}]"},{"id":"REF0056","ids":["R56","OA019"],"title":"In silico MS/MS prediction for peptidoglycan profiling uncovers novel anti-inflammatory peptidoglycan fragments of the gut microbiota.","url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC10829024/","urls":["https://pmc.ncbi.nlm.nih.gov/articles/PMC10829024/"],"year":2024,"doi":"10.1039/d3sc05819k","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Kwan JMC","Liang Y","Ng EWL","Sviriaeva E","Li C","Zhao Y","Zhang XL","Liu XW","Wong SH","Qiao Y"],"journal":"Chem Sci","searchText":"[{\"source\":\"digest.records\",\"path\":\"digest-evidence.json/records/32\",\"title\":\"In silico MS/MS prediction for peptidoglycan profiling uncovers novel anti-inflammatory peptidoglycan fragments of the gut microbiota (2024). Chemical Science 15:1846-1859.\",\"id\":\"OA019\",\"context\":\"Bifidobacterium species and Fusobacterium nucleatum\",\"locator\":\"Figures 4 and 5; supplementary Figures S7 and S10\",\"access\":\"partial\"},{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/1/sources/1\",\"title\":\"In silico MS/MS prediction for peptidoglycan profiling uncovers novel anti-inflammatory peptidoglycan fragments of the gut microbiota\",\"context\":\"Akkermansia muciniphila\",\"locator\":\"Results: comprehensive PGN profiling in gut bacteria; Figures 4B and 5.\",\"access\":\"full_text\"},{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/6/sources/0\",\"title\":\"In silico MS/MS prediction for peptidoglycan profiling uncovers novel anti-inflammatory peptidoglycan fragments of the gut microbiota\",\"context\":\"Bifidobacterium adolescentis\",\"locator\":\"Figures 4B, 5 and S8B; Results: Lys/Orn heterogeneity and bridge composition.\",\"access\":\"full_text\"},{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/7/sources/1\",\"title\":\"In silico MS/MS prediction for peptidoglycan profiling uncovers novel anti-inflammatory peptidoglycan fragments of the gut microbiota\",\"context\":\"Bifidobacterium bifidum\",\"locator\":\"Figures 4B, 5 and S8B: species-specific PGN profiles.\",\"access\":\"full_text\"},{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/9/sources/0\",\"title\":\"In silico MS/MS prediction for peptidoglycan profiling uncovers novel anti-inflammatory peptidoglycan fragments of the gut microbiota\",\"context\":\"Bifidobacterium longum subsp. infantis\",\"locator\":\"Figures 4B, 5 and S8B: B. infantis specimen, distinct from B. adolescentis and B. bifidum.\",\"access\":\"full_text\"},{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/25/sources/0\",\"title\":\"Bifidobacterium, Akkermansia and Fusobacterium PG profiling, 2024.\",\"context\":\"Fusobacterium nucleatum\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/30/sources/2\",\"title\":\"Bifidobacterium, Akkermansia and Fusobacterium PG profiling, 2024.\",\"context\":\"Lactiplantibacillus plantarum\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R56\",\"id\":\"R56\",\"title\":\"In silico MS/MS prediction for peptidoglycan profiling uncovers novel anti-inflammatory peptidoglycan fragments of the gut microbiota.\"}]"},{"id":"REF0057","ids":["R57"],"title":"B. bifidum var. pennsylvanicus Orn/Ser/Asn structure, 1971.","url":"https://www.sciencedirect.com/science/article/pii/0003986171902001","urls":["https://www.sciencedirect.com/science/article/pii/0003986171902001"],"year":1971,"doi":null,"metadataVerified":false,"metadataVerificationStatus":"no_exact_identifier","searchText":"[{\"source\":\"data.references\",\"path\":\"data.json/references/R57\",\"id\":\"R57\",\"title\":\"B. bifidum var. pennsylvanicus Orn/Ser/Asn structure, 1971.\"}]"},{"id":"REF0058","ids":["R58"],"title":"Peptidoglycan precursor from Fusobacterium nucleatum contains lanthionine.","url":"https://pubmed.ncbi.nlm.nih.gov/1987169/","urls":["https://pubmed.ncbi.nlm.nih.gov/1987169/"],"year":1991,"doi":"10.1128/jb.173.2.900-902.1991","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Fredriksen A","Vasstrand EN","Jensen HB"],"journal":"J Bacteriol","searchText":"[{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/25/sources/1\",\"title\":\"F. nucleatum lanthionine PG precursor, 1991.\",\"context\":\"Fusobacterium nucleatum\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R58\",\"id\":\"R58\",\"title\":\"Peptidoglycan precursor from Fusobacterium nucleatum contains lanthionine.\"}]"},{"id":"REF0059","ids":["R59"],"title":"Peptidoglycan composition of gramnegative obligately anaerobic rods.","url":"https://www.jstage.jst.go.jp/article/jgam1955/27/3/27_3_199/_article/-char/en","urls":["https://www.jstage.jst.go.jp/article/jgam1955/27/3/27_3_199/_article/-char/en"],"year":1981,"doi":"10.2323/jgam.27.199","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["EIICHI MIYAGAWA","RYOZO AZUMA","TSUNEJI SUTO"],"journal":"The Journal of General and Applied Microbiology","searchText":"[{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/4/sources/1\",\"title\":\"Peptidoglycan composition of gram-negative obligately anaerobic rods\",\"context\":\"Bacteroides fragilis\",\"locator\":\"Abstract: B. fragilis NCTC 9343 composition; composition evidence only.\",\"access\":\"abstract\"},{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/5/sources/1\",\"title\":\"Peptidoglycan composition of gram-negative obligately anaerobic rods\",\"context\":\"Bacteroides thetaiotaomicron\",\"locator\":\"Abstract: mDAP detected in B. thetaiotaomicron; composition evidence only.\",\"access\":\"abstract\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R59\",\"id\":\"R59\",\"title\":\"Peptidoglycan composition of gramnegative obligately anaerobic rods.\"}]"},{"id":"REF0060","ids":["R60","OA020","REF0060","JUTRAS2019"],"title":"Borrelia burgdorferi peptidoglycan is a persistent antigen in patients with Lyme arthritis.","url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC6613144/","urls":["https://pmc.ncbi.nlm.nih.gov/articles/PMC6613144/"],"year":2019,"doi":"10.1073/pnas.1904170116","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Jutras BL","Lochhead RB","Kloos ZA","Biboy J","Strle K","Booth CJ","Govers SK","Gray J","Schumann P","Vollmer W","Bockenstedt LK","Steere AC","Jacobs-Wagner C","Jacobs-Wagner C"],"journal":"Proc Natl Acad Sci U S A","searchText":"[{\"source\":\"digest.records\",\"path\":\"digest-evidence.json/records/33\",\"title\":\"Jutras et al. (2019). Borrelia burgdorferi peptidoglycan is a persistent antigen in patients with Lyme arthritis.\",\"id\":\"OA020\",\"context\":\"Borrelia burgdorferi\",\"locator\":\"Figure 1A; SI Appendix Table S1; PG Structural and Chemical Analysis section; Figure 4B\",\"access\":\"indexed\"},{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/10/sources/0\",\"title\":\"B. burgdorferi Orn/Gly PG structure, 2019.\",\"context\":\"Borrelia burgdorferi\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"chemotype.nomenclature\",\"context\":\"borrelia\",\"title\":\"Borrelia burgdorferi peptidoglycan is a persistent antigen in patients with Lyme arthritis\",\"locator\":\"Figure 1A and associated structural description; SI Appendix Table S1\",\"access\":\"indexed_excerpt\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R60\",\"id\":\"R60\",\"title\":\"Borrelia burgdorferi peptidoglycan is a persistent antigen in patients with Lyme arthritis.\"},{\"source\":\"data.references\",\"path\":\"data.json/references/REF0060\",\"id\":\"REF0060\",\"title\":\"Borrelia burgdorferi peptidoglycan is a persistent antigen in patients with Lyme arthritis.\"}]"},{"id":"REF0061","ids":["R61"],"title":"Bacterial and host enzymes modulate the inflammatory response produced by the peptidoglycan of the Lyme disease agent.","url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC11741416/","urls":["https://pmc.ncbi.nlm.nih.gov/articles/PMC11741416/"],"year":2025,"doi":"10.1101/2025.01.08.631998","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["McCausland JW","Kloos ZA","Irnov I","Sonnert ND","Zhou J","Putnick R","Mueller EA","Steere AC","Palm NW","Grimes CL","Jacobs-Wagner C"],"journal":"bioRxiv","publicationStatus":"preprint","searchText":"[{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/10/sources/1\",\"title\":\"B. burgdorferi PG cleavage enzymes, 2025.\",\"context\":\"Borrelia burgdorferi\",\"locator\":\"Retained model reference; not newly reviewed for this species\",\"access\":\"legacy\"},{\"source\":\"data.references\",\"path\":\"data.json/references/R61\",\"id\":\"R61\",\"title\":\"Bacterial and host enzymes modulate the inflammatory response produced by the peptidoglycan of the Lyme disease agent.\"}]"},{"id":"REF0062","ids":["R62"],"title":"Pathogenic Chlamydia Lack a Classical Sacculus but Synthesize a Narrow, Mid-cell Peptidoglycan Ring, Regulated by MreB, for Cell Division.","url":"https://pubmed.ncbi.nlm.nih.gov/27144308/","urls":["https://pubmed.ncbi.nlm.nih.gov/27144308/"],"year":2016,"doi":"10.1371/journal.ppat.1005590","metadataVerified":true,"metadataVerificationStatus":"verified","authors":["Liechti G","Kuru E","Packiam M","Hsu YP","Tekkam S","Hall E","Rittichier JT","VanNieuwenhze M","Brun YV","Maurelli AT"],"journal":"PLoS Pathog","searchText":"[{\"source\":\"atlas.species.sources\",\"path\":\"atlas-updates.json/species/14/sources/0\",\"title\":\"Chlamydial division-associated PG ring, 2016.\",\"context\":\"Chlamydia trachomatis\",\"locator\":\"Retained model reference; 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