3.4.21.92 Anemia, Hypochromic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=15549267&form=6&db=m Chlorosis during nitrogen starvation is altered by carbon dioxide and temperature status and is mediated by the ClpP1 protease in Synechococcus elongatus. unassigned - 3.4.21.92 Anemia, Hypochromic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=15563614&form=6&db=m Inactivation of the clpC1 gene encoding a chloroplast Hsp100 molecular chaperone causes growth retardation, leaf chlorosis, lower photosynthetic activity, and a specific reduction in photosystem content. causal interaction,therapeutic application,unassigned 1,1,0 3.4.21.92 Anemia, Hypochromic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=20382967&form=6&db=m ClpC1, an ATP-dependent Clp protease in plastids, is involved in iron homeostasis in Arabidopsis leaves. unassigned - 3.4.21.92 Blindness http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=32873765&form=6&db=m The ClpX and ClpP2 Orthologs of Chlamydia trachomatis Perform Discrete and Essential Functions in Organism Growth and Development. unassigned - 3.4.21.92 Dehydration http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=9375397&form=6&db=m A nuclear gene, erd1, encoding a chloroplast-targeted Clp protease regulatory subunit homolog is not only induced by water stress but also developmentally up-regulated during senescence in Arabidopsis thaliana. therapeutic application,unassigned 1,0 3.4.21.92 Hypersensitivity http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=9299335&form=6&db=m Communication of ClpXP protease hypersensitivity to bacteriophage Mu repressor isoforms. causal interaction,unassigned 1,0 3.4.21.92 Infections http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=9570408&form=6&db=m The ClpC ATPase of Listeria monocytogenes is a general stress protein required for virulence and promoting early bacterial escape from the phagosome of macrophages. ongoing research,unassigned 4,0 3.4.21.92 Infections http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=17185548&form=6&db=m Proteomic comparison of Mycobacterium avium subspecies paratuberculosis grown in vitro and isolated from clinical cases of ovine paratuberculosis. unassigned - 3.4.21.92 Infections http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=18992803&form=6&db=m Helicobacter pylori mutants defective in the clpP ATP-dependant protease and the chaperone clpA display reduced macrophage and murine survival. ongoing research,therapeutic application,unassigned 3,1,0 3.4.21.92 Infections http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=19220325&form=6&db=m Caseinolytic protease: a protein vaccine which could elicit serotype-independent protection against invasive pneumococcal infection. causal interaction,diagnostic usage,ongoing research,therapeutic application 2,1,4,2 3.4.21.92 Infections http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=22359499&form=6&db=m Mycobacterium tuberculosis ClpP1 and ClpP2 Function Together in Protein Degradation and Are Required for Viability in vitro and During Infection. ongoing research,therapeutic application,unassigned 4,1,0 3.4.21.92 Infections http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=23584755&form=6&db=m The ClpP peptidase of Wolbachia endobacteria is a novel target for drug development against filarial infections. causal interaction,therapeutic application,unassigned 3,4,0 3.4.21.92 Infections http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=23995637&form=6&db=m Regulation of host hemoglobin binding by the Staphylococcus aureus Clp proteolytic system. causal interaction,ongoing research,unassigned 1,3,0 3.4.21.92 Infections http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=27831584&form=6&db=m The development of small-molecule modulators for ClpP protease activity. causal interaction,unassigned 4,0 3.4.21.92 Infections http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=27849175&form=6&db=m Two isoforms of Clp peptidase in Pseudomonas aeruginosa control distinct aspects of cellular physiology. causal interaction,unassigned 1,0 3.4.21.92 Infections http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28271875&form=6&db=m In Vivo-Selected Pyrazinoic Acid-Resistant Mycobacterium tuberculosis Strains Harbor Missense Mutations in the Aspartate Decarboxylase PanD and the Unfoldase ClpC1. diagnostic usage,ongoing research,therapeutic application,unassigned 1,1,1,0 3.4.21.92 Infections http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=30543804&form=6&db=m Development of high throughput screening methods for inhibitors of ClpC1P1P2 from Mycobacteria tuberculosis. causal interaction,unassigned 3,0 3.4.21.92 Infections http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=30602512&form=6&db=m Rufomycin Targets ClpC1 Proteolysis in Mycobacterium tuberculosis and M. abscessus. therapeutic application,unassigned 3,0 3.4.21.92 Infections http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=31409659&form=6&db=m Dual RNA-seq in Streptococcus pneumoniae Infection Reveals Compartmentalized Neutrophil Responses in Lung and Pleural Space. unassigned - 3.4.21.92 Infections http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=32031798&form=6&db=m Discovery of Novel Peptidomimetic Boronate ClpP Inhibitors with Noncanonical Enzyme Mechanism as Potent Virulence Blockers in Vitro and in Vivo. causal interaction,therapeutic application,unassigned 3,4,0 3.4.21.92 Infections http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=32323346&form=6&db=m Alteration of protein homeostasis mediates the interaction of Pseudomonas aeruginosa with Staphylococcus aureus. ongoing research,therapeutic application,unassigned 1,2,0 3.4.21.92 Infections http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=32753509&form=6&db=m The Stringent Stress Response Controls Proteases and Global Regulators under Optimal Growth Conditions in Pseudomonas aeruginosa. causal interaction,ongoing research,therapeutic application,unassigned 1,2,1,0 3.4.21.92 Infections http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=32873765&form=6&db=m The ClpX and ClpP2 Orthologs of Chlamydia trachomatis Perform Discrete and Essential Functions in Organism Growth and Development. unassigned - 3.4.21.92 Infections http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=33237740&form=6&db=m Development of Antibiotics That Dysregulate the Neisserial ClpP Protease. unassigned - 3.4.21.92 Infections http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=34048895&form=6&db=m Recent advances in Clp protease modulation to address virulence, resistance and persistence of MRSA infection. causal interaction,ongoing research,therapeutic application,unassigned 4,3,1,0 3.4.21.92 Infections http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=34497598&form=6&db=m Loss of the ClpXP Protease Leads to Decreased Resistance to Cell-Envelope Targeting Antimicrobials in Bacillus anthracis Sterne. unassigned - 3.4.21.92 Infertility http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=20643392&form=6&db=m Association of tubal factor infertility with elevated antibodies to Chlamydia trachomatis caseinolytic protease P. causal interaction,diagnostic usage,unassigned 3,2,0 3.4.21.92 Leprosy http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=29666623&form=6&db=m Autoimmunity to Tropomyosin-Specific Peptides Induced by Mycobacterium leprae in Leprosy Patients: Identification of Mimicking Proteins. causal interaction,ongoing research,unassigned 3,4,0 3.4.21.92 Leukemia, Myeloid, Acute http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=32761807&form=6&db=m The role of mitochondrial proteases in leukemic cells and leukemic stem cells. causal interaction,diagnostic usage,therapeutic application,unassigned 4,1,3,0 3.4.21.92 Liver Cirrhosis, Biliary http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=11059856&form=6&db=m Antibodies against the COOH-terminal region of E. coli ClpP protease in patients with primary biliary cirrhosis. diagnostic usage,ongoing research,therapeutic application,unassigned 3,2,2,0 3.4.21.92 Liver Cirrhosis, Biliary http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=11434633&form=6&db=m Antibodies to Clp protease in primary biliary cirrhosis: possible role of a mimicking T-cell epitope. diagnostic usage,ongoing research,therapeutic application,unassigned 2,1,1,0 3.4.21.92 Liver Cirrhosis, Biliary http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=11804659&form=6&db=m Antibodies against homologous microbial caseinolytic proteases P characterise primary biliary cirrhosis. therapeutic application,unassigned 2,0 3.4.21.92 Liver Diseases http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=11059856&form=6&db=m Antibodies against the COOH-terminal region of E. coli ClpP protease in patients with primary biliary cirrhosis. diagnostic usage,ongoing research,therapeutic application,unassigned 3,2,2,0 3.4.21.92 Malaria http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=15812672&form=6&db=m Plasmodium (Haemamoeba) cathemerium gene sequences for phylogenetic analysis of malaria parasites. diagnostic usage,ongoing research,therapeutic application,unassigned 3,2,1,0 3.4.21.92 Malaria http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=17393186&form=6&db=m Bayesian analysis of new and old malaria parasite DNA sequence data demonstrates the need for more phylogenetic signal to clarify the descent of Plasmodium falciparum. unassigned - 3.4.21.92 Malaria http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=20541613&form=6&db=m Malaria parasite sequences from chimpanzee support the co-speciation hypothesis for the origin of virulent human malaria (Plasmodium falciparum). unassigned - 3.4.21.92 Malaria http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=20545854&form=6&db=m A cyanobacterial serine protease of Plasmodium falciparum is targeted to the apicoplast and plays an important role in its growth and development. causal interaction,therapeutic application,unassigned 3,4,0 3.4.21.92 Malaria http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28917450&form=6&db=m A novel class of Plasmodial ClpP protease inhibitors as potential antimalarial agents. causal interaction,therapeutic application,unassigned 2,3,0 3.4.21.92 Malaria, Avian http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=15812672&form=6&db=m Plasmodium (Haemamoeba) cathemerium gene sequences for phylogenetic analysis of malaria parasites. diagnostic usage,ongoing research,therapeutic application,unassigned 3,2,1,0 3.4.21.92 Neoplasms http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=11292737&form=6&db=m Disruption of the genes for ClpXP protease in Salmonella enterica serovar Typhimurium results in persistent infection in mice, and development of persistence requires endogenous gamma interferon and tumor necrosis factor alpha. causal interaction,therapeutic application,unassigned 4,1,0 3.4.21.92 Neoplasms http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=16317774&form=6&db=m The up-regulation of proteasome subunits and lysosomal proteases in hepatocellular carcinomas of the HBx gene knockin transgenic mice. causal interaction,diagnostic usage,ongoing research,unassigned 4,1,2,0 3.4.21.92 Neoplasms http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=33336683&form=6&db=m Mechanisms of imipridones in targeting mitochondrial metabolism in cancer cells. causal interaction,unassigned 2,0 3.4.21.92 Neoplasms http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=34045646&form=6&db=m Small molecule inhibitors of the mitochondrial ClpXP protease possess cytostatic potential and re-sensitize chemo-resistant cancers. therapeutic application,unassigned 3,0 3.4.21.92 Neoplasms http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=34207660&form=6&db=m Mitochondrial Caseinolytic Protease P: A Possible Novel Prognostic Marker and Therapeutic Target in Cancer. causal interaction,diagnostic usage,ongoing research,therapeutic application 1,4,3,4 3.4.21.92 Neoplasms http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=34438398&form=6&db=m Contribution of the Clp Protease to Bacterial Survival and Mitochondrial Homoeostasis. ongoing research,unassigned 3,0 3.4.21.92 Neuroblastoma http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=23643883&form=6&db=m Streptococcus pneumoniae ClpP protease induces apoptosis via caspase-independent pathway in human neuroblastoma cells: cytoplasmic relocalization of p53. ongoing research,therapeutic application,unassigned 3,1,0 3.4.21.92 Parasitic Diseases http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=32471865&form=6&db=m A chemical inhibitor of heat shock protein 78 (HSP78) from Leishmania donovani represents a potential antileishmanial drug candidate. ongoing research,therapeutic application,unassigned 1,3,0 3.4.21.92 Persistent Infection http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=11292737&form=6&db=m Disruption of the genes for ClpXP protease in Salmonella enterica serovar Typhimurium results in persistent infection in mice, and development of persistence requires endogenous gamma interferon and tumor necrosis factor alpha. causal interaction,therapeutic application,unassigned 4,1,0 3.4.21.92 Plant Diseases http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=33326777&form=6&db=m Antagonistic Regulation by CPN60A and CLPC1 of TRXL1 that Regulates MDH Activity Leading to Plant Disease Resistance and Thermotolerance. ongoing research,therapeutic application,unassigned 1,1,0 3.4.21.92 Pneumococcal Infections http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=17524530&form=6&db=m Enhanced protection against pneumococcal infection elicited by immunization with the combination of PspA, PspC, and ClpP. ongoing research,therapeutic application,unassigned 3,1,0 3.4.21.92 Pneumococcal Infections http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=18930162&form=6&db=m Mucosal immunization with purified ClpP could elicit protective efficacy against pneumococcal pneumonia and sepsis in mice. causal interaction,therapeutic application,unassigned 2,3,0 3.4.21.92 Pneumococcal Infections http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=19220325&form=6&db=m Caseinolytic protease: a protein vaccine which could elicit serotype-independent protection against invasive pneumococcal infection. causal interaction,diagnostic usage,ongoing research,therapeutic application 2,1,4,2 3.4.21.92 Pneumococcal Infections http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=20038538&form=6&db=m Immunization with a combination of three pneumococcal proteins confers additive and broad protection against Streptococcus pneumoniae Infections in Mice. ongoing research,therapeutic application,unassigned 4,1,0 3.4.21.92 Pneumococcal Infections http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=22728705&form=6&db=m Mucosal immunization with caseinolytic protease X elicited cross-protective immunity against pneumococcal infection in mice. therapeutic application,unassigned 1,0 3.4.21.92 Pneumonia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=32386322&form=6&db=m The ClpXP Protease Contributes to Staphylococcus aureus Pneumonia. causal interaction,diagnostic usage,ongoing research,therapeutic application 3,3,1,1 3.4.21.92 Pneumonia, Staphylococcal http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=32386322&form=6&db=m The ClpXP Protease Contributes to Staphylococcus aureus Pneumonia. causal interaction,diagnostic usage,ongoing research,therapeutic application 3,3,1,1 3.4.21.92 Sepsis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=18034862&form=6&db=m Streptococcus pneumoniae: proteomics of surface proteins for vaccine development. therapeutic application,unassigned 2,0 3.4.21.92 Sexually Transmitted Diseases http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=31575885&form=6&db=m The functional ClpXP protease of Chlamydia trachomatis requires distinct clpP genes from separate genetic loci. ongoing research,therapeutic application,unassigned 1,1,0 3.4.21.92 Sexually Transmitted Diseases http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=32873765&form=6&db=m The ClpX and ClpP2 Orthologs of Chlamydia trachomatis Perform Discrete and Essential Functions in Organism Growth and Development. unassigned - 3.4.21.92 Staphylococcal Infections http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=32031798&form=6&db=m Discovery of Novel Peptidomimetic Boronate ClpP Inhibitors with Noncanonical Enzyme Mechanism as Potent Virulence Blockers in Vitro and in Vivo. causal interaction,therapeutic application,unassigned 3,4,0 3.4.21.92 Starvation http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=8416909&form=6&db=m Role of Clp protease subunits in degradation of carbon starvation proteins in Escherichia coli. causal interaction,therapeutic application,unassigned 1,2,0 3.4.21.92 Starvation http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=8550468&form=6&db=m Regulation of Escherichia coli starvation sigma factor (sigma s) by ClpXP protease. therapeutic application,unassigned 1,0 3.4.21.92 Starvation http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=11442836&form=6&db=m Role of the response regulator RssB in sigma recognition and initiation of sigma proteolysis in Escherichia coli. therapeutic application,unassigned 1,0 3.4.21.92 Starvation http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=12486047&form=6&db=m Global role for ClpP-containing proteases in stationary-phase adaptation of Escherichia coli. ongoing research,unassigned 1,0 3.4.21.92 Starvation http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=15549267&form=6&db=m Chlorosis during nitrogen starvation is altered by carbon dioxide and temperature status and is mediated by the ClpP1 protease in Synechococcus elongatus. unassigned - 3.4.21.92 Starvation http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=22123255&form=6&db=m Validation of the essential ClpP protease in Mycobacterium tuberculosis as a novel drug target. causal interaction,ongoing research,therapeutic application,unassigned 2,3,3,0 3.4.21.92 Starvation http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=32037686&form=6&db=m Inter- and intramolecular regulation of protein depupylation in Mycobacterium smegmatis. causal interaction,diagnostic usage,unassigned 1,1,0 3.4.21.92 Starvation http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=32389745&form=6&db=m Mycobacterium smegmatis MSMEG_0129 is a nutrition-associated regulator that interacts with CarD and ClpP2. causal interaction,unassigned 3,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=10231573&form=6&db=m Species variation in ATP-dependent protein degradation: protease profiles differ between mycobacteria and protease functions differ between Mycobacterium smegmatis and Escherichia coli. therapeutic application,unassigned 1,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=17242518&form=6&db=m Insights into the inter-ring plasticity of caseinolytic proteases from the X-ray structure of Mycobacterium tuberculosis ClpP1. unassigned - 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=19016865&form=6&db=m Mycobacterium tuberculosis ClpC1: characterization and role of the N-terminal domain in its function. ongoing research,therapeutic application,unassigned 4,1,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=20625433&form=6&db=m Mycobacterium tuberculosis ClpX interacts with FtsZ and interferes with FtsZ assembly. ongoing research,unassigned 1,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=20661284&form=6&db=m Characterization of a Clp protease gene regulator and the reaeration response in Mycobacterium tuberculosis. ongoing research,therapeutic application,unassigned 4,1,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=20887733&form=6&db=m The Clp Chaperones and Proteases of the Human Malaria Parasite Plasmodium falciparum. therapeutic application,unassigned 1,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=20975890&form=6&db=m A ClpP protein model as tuberculosis target for screening marine compounds. unassigned - 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=21563281&form=6&db=m The natural product cyclomarin kills Mycobacterium tuberculosis by targeting the ClpC1 subunit of the caseinolytic protease. unassigned - 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=22123255&form=6&db=m Validation of the essential ClpP protease in Mycobacterium tuberculosis as a novel drug target. causal interaction,ongoing research,therapeutic application,unassigned 2,3,3,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=22132756&form=6&db=m Assembly and proteolytic processing of mycobacterial ClpP1 and ClpP2. unassigned - 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=22286948&form=6&db=m The active ClpP protease from M. tuberculosis is a complex composed of a heptameric ClpP1 and a ClpP2 ring. ongoing research,therapeutic application,unassigned 1,2,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=22359499&form=6&db=m Mycobacterium tuberculosis ClpP1 and ClpP2 Function Together in Protein Degradation and Are Required for Viability in vitro and During Infection. ongoing research,therapeutic application,unassigned 4,1,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=23284674&form=6&db=m The C-terminus of ClpC1 of Mycobacterium tuberculosis is crucial for its oligomerization and function. causal interaction,ongoing research,therapeutic application,unassigned 4,4,1,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=24047344&form=6&db=m Antibacterial Activity of and Resistance to Small Molecule Inhibitors of the ClpP Peptidase. diagnostic usage,unassigned 3,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=24603869&form=6&db=m Post-Translational Regulation via Clp Protease Is Critical for Survival of Mycobacterium tuberculosis. ongoing research,unassigned 2,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=24976069&form=6&db=m Substrate delivery by the AAA+ ClpX and ClpC1 unfoldases activates the mycobacterial ClpP1P2 peptidase. therapeutic application,unassigned 4,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=25267638&form=6&db=m Crystal structure of Mycobacterium tuberculosis ClpP1P2 suggests a model for peptidase activation by AAA+ partner binding and substrate delivery. ongoing research,unassigned 2,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=25337208&form=6&db=m Cloning and characterization of Clp protease proteolytic subunit 2 and its implication in clinical diagnosis of tuberculosis. diagnostic usage,ongoing research,therapeutic application,unassigned 4,2,1,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=25421483&form=6&db=m The Cyclic Peptide Ecumicin Targeting ClpC1 Is Active against Mycobacterium tuberculosis In Vivo. causal interaction,diagnostic usage,therapeutic application,unassigned 3,3,4,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=25759383&form=6&db=m Cleavage specificity of Mycobacterium tuberculosis ClpP1P2 protease and identification of novel peptide substrates and boronate inhibitors with anti-bacterial activity. therapeutic application,unassigned 3,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=25933022&form=6&db=m The Mycobacterium tuberculosis ClpP1P2 Protease Interacts Asymmetrically with Its ATPase Partners ClpX and ClpC1. ongoing research,therapeutic application,unassigned 1,2,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=25944857&form=6&db=m Target mechanism-based whole-cell screening identifies bortezomib as an inhibitor of caseinolytic protease in mycobacteria. causal interaction,therapeutic application,unassigned 2,4,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26091017&form=6&db=m Correction: The Mycobacterium tuberculosis ClpP1P2 Protease Interacts Asymmetrically with Its ATPase Partners ClpX and ClpC1. unassigned - 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26472355&form=6&db=m Gift from Nature: Cyclomarin?A Kills Mycobacteria and Malaria Parasites by Distinct Modes of Action. ongoing research,unassigned 2,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26586403&form=6&db=m Anti-tuberculosis lead molecules from natural products targeting Mycobacterium tuberculosis ClpC1. unassigned - 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26858247&form=6&db=m Structure and Functional Properties of the Active Form of the Proteolytic Complex, ClpP1P2, from Mycobacterium tuberculosis. ongoing research,therapeutic application,unassigned 4,1,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26919556&form=6&db=m Acyldepsipeptide antibiotics kill mycobacteria by preventing the physiological functions of the ClpP1P2 protease. ongoing research,unassigned 1,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=27241518&form=6&db=m Total synthesis of cyclomarins A, C and D, marine cyclic peptides with interesting anti-tuberculosis and anti-malaria activities. diagnostic usage,therapeutic application,unassigned 1,1,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=27872068&form=6&db=m Missense Mutations in the Unfoldase ClpC1 of the Caseinolytic Protease Complex Are Associated with Pyrazinamide Resistance in Mycobacterium tuberculosis. causal interaction,unassigned 2,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28196969&form=6&db=m Mutation in clpC1 encoding an ATP-dependent ATPase involved in protein degradation is associated with pyrazinamide resistance in Mycobacterium tuberculosis. causal interaction,unassigned 2,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28271875&form=6&db=m In Vivo-Selected Pyrazinoic Acid-Resistant Mycobacterium tuberculosis Strains Harbor Missense Mutations in the Aspartate Decarboxylase PanD and the Unfoldase ClpC1. diagnostic usage,ongoing research,therapeutic application,unassigned 1,1,1,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28317028&form=6&db=m Mycobacterial Caseinolytic Protease Gene Regulator ClgR Is a Substrate of Caseinolytic Protease. causal interaction,therapeutic application,unassigned 2,4,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28342755&form=6&db=m Mutation analysis of the interactions between Mycobacterium tuberculosis caseinolytic protease C1 (ClpC1) and ecumicin. diagnostic usage,unassigned 1,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28496439&form=6&db=m Bortezomib Warhead-Switch Confers Dual Activity against Mycobacterial Caseinolytic Protease and Proteasome and Selectivity against Human Proteasome. ongoing research,therapeutic application,unassigned 3,4,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28612535&form=6&db=m [Prediction and Analysis of Epitopes in clpP2 of Mycobacterium tuberculosis]. ongoing research,therapeutic application,unassigned 1,2,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=29632076&form=6&db=m The antibiotic cyclomarin blocks arginine-phosphate-induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis. unassigned - 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=30005200&form=6&db=m Design, synthesis and biological evaluation of novel pyrrole derivatives as potential ClpP1P2 inhibitor against Mycobacterium tuberculosis. therapeutic application,unassigned 4,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=30463272&form=6&db=m Mycobacterium tuberculosis ClpC1 N-Terminal Domain Is Dispensable for Adaptor Protein-Dependent Allosteric Regulation. therapeutic application,unassigned 1,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=30602512&form=6&db=m Rufomycin Targets ClpC1 Proteolysis in Mycobacterium tuberculosis and M. abscessus. therapeutic application,unassigned 3,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=30990022&form=6&db=m High-Resolution Structure of ClpC1-Rufomycin and Ligand Binding Studies Provide a Framework to Design and Optimize Anti-Tuberculosis Leads. therapeutic application,unassigned 3,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=32123115&form=6&db=m An allosteric switch regulates Mycobacterium tuberculosis ClpP1P2 protease function as established by cryo-EM and methyl-TROSY NMR. therapeutic application,unassigned 1,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=32158237&form=6&db=m Detection of Novel Gene Mutations Associated with Pyrazinamide Resistance in Multidrug-Resistant Mycobacterium tuberculosis Clinical Isolates in Southern China. diagnostic usage,therapeutic application,unassigned 4,1,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=32409584&form=6&db=m The unfoldase ClpC1 of Mycobacterium tuberculosis regulates the expression of a distinct subset of proteins having intrinsically disordered termini. ongoing research,unassigned 1,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=32782432&form=6&db=m Delving Into the Functional Meaning of Phenotypic Variation in Mycobacterial Persistence: Who Benefits the Most From Programmed Death of Individual Cells? causal interaction,unassigned 1,0 3.4.21.92 Tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=33229461&form=6&db=m ClpX Is Essential and Activated by Single-Strand DNA Binding Protein in Mycobacteria. unassigned -