Property | Value | Creator | Evidence | PMID | Comment |
Citation | ClgR regulation of chaperone and protease systems is essential for Mycobacterium tuberculosis parasitism of the macrophage. authors,M. Estorninho,H. Smith,J. Thole,J. Harders-Westerveen,A. Kierzek,RE. Butler,O. Neyrolles,GR. Stewart Microbiology (Reading, Engl.) 2010 | akankshajain.21 | IEP | 20688819 | Co-expression (Functional linkage) |
Interaction | Regulatory Rv2475c | akankshajain.21 | IEP | | Co-expression (Functional linkage) authors,M. Estorninho,H. Smith,J. Thole,J. Harders-Westerveen,A. Kierzek,RE. Butler,O. Neyrolles,GR. Stewart ClgR regulation of chaperone and protease systems is essential for Mycobacterium tuberculosis parasitism of the macrophage. Microbiology (Reading, Engl.) 2010 |
Interaction | PhysicalInteraction Rv2457c | akankshajain.21 | IDA | | Structural analysis AK. Gupta, VM. Katoch et al. Microarray analysis of efflux pump genes in multidrug-resistant Mycobacterium tuberculosis during stress induced by common anti-tuberculous drugs. Microb. Drug Resist. 2010 |
Citation | Insights into the inter-ring plasticity of caseinolytic proteases from the X-ray structure of Mycobacterium tuberculosis ClpP1. H. Ingvarsson, MJ. Mat et al. Acta Crystallogr. D Biol. Crystallogr. 2007 | akankshajain.21 | IDA | 17242518 | Structural analysis |
Interaction | PhysicalInteraction Rv2460c | akankshajain.21 | IDA | | Structural analysis H. Ingvarsson, MJ. Mat et al. Insights into the inter-ring plasticity of caseinolytic proteases from the X-ray structure of Mycobacterium tuberculosis ClpP1. Acta Crystallogr. D Biol. Crystallogr. 2007 |
Interaction | PhysicalInteraction Rv2457c | akankshajain.21 | IDA | | Structural analysis H. Ingvarsson, MJ. Mat et al. Insights into the inter-ring plasticity of caseinolytic proteases from the X-ray structure of Mycobacterium tuberculosis ClpP1. Acta Crystallogr. D Biol. Crystallogr. 2007 |
Citation | The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation. authors,A. Gribun,MS. Kimber,R. Ching,R. Sprangers,KM. Fiebig,WA. Houry J. Biol. Chem. 2005 | akankshajain.21 | IDA | 15701650 | Structural analysis |
Interaction | PhysicalInteraction Rv2460c | akankshajain.21 | IDA | | Structural analysis authors,A. Gribun,MS. Kimber,R. Ching,R. Sprangers,KM. Fiebig,WA. Houry The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation. J. Biol. Chem. 2005 |
Interaction | PhysicalInteraction Rv2457c | akankshajain.21 | IDA | | Structural analysis authors,A. Gribun,MS. Kimber,R. Ching,R. Sprangers,KM. Fiebig,WA. Houry The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation. J. Biol. Chem. 2005 |
Citation | ClpP: a distinctive family of cylindrical energy-dependent serine proteases. authors,AY. Yu,WA. Houry FEBS Lett. 2007 | richasinha4u | IDA | 17499722 | Spectrophotometric Analysis |
Interaction | Regulatory Rv2457c | richasinha4u | IDA | | Spectrophotometric Analysis authors,AY. Yu,WA. Houry ClpP: a distinctive family of cylindrical energy-dependent serine proteases. FEBS Lett. 2007 |
Citation | Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli. authors,MR. Maurizi,WP. Clark,Y. Katayama,S. Rudikoff,J. Pumphrey,B. Bowers,S. Gottesman J. Biol. Chem. 1990 | richasinha4u | IDA | 2197275 | Structural Analysis |
Interaction | Regulatory Rv2457c | richasinha4u | IDA | | Structural Analysis authors,MR. Maurizi,WP. Clark,Y. Katayama,S. Rudikoff,J. Pumphrey,B. Bowers,S. Gottesman Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli. J. Biol. Chem. 1990 |
Citation | The ATP-dependent Clp protease of Escherichia coli. Sequence of clpA and identification of a Clp-specific substrate. authors,S. Gottesman,WP. Clark,MR. Maurizi J. Biol. Chem. 1990 | richasinha4u | IDA | 2186030 | Structural Analysis |
Interaction | Regulatory Rv2457c | richasinha4u | IDA | | Structural Analysis authors,S. Gottesman,WP. Clark,MR. Maurizi The ATP-dependent Clp protease of Escherichia coli. Sequence of clpA and identification of a Clp-specific substrate. J. Biol. Chem. 1990 |
Citation | ClpP: a distinctive family of cylindrical energy-dependent serine proteases. authors,AY. Yu,WA. Houry FEBS Lett. 2007 | richasinha4u | IDA | 17499722 | Structural Analysis |
Interaction | Regulatory Rv2457c | richasinha4u | IDA | | Structural Analysis authors,AY. Yu,WA. Houry ClpP: a distinctive family of cylindrical energy-dependent serine proteases. FEBS Lett. 2007 |
Citation | Microarray analysis of efflux pump genes in multidrug-resistant Mycobacterium tuberculosis during stress induced by common anti-tuberculous drugs. AK. Gupta, VM. Katoch et al. Microb. Drug Resist. 2010 | akankshajain.21 | IDA | 20001742 | Structural analysis |
Interaction | PhysicalInteraction Rv2460c | akankshajain.21 | IDA | | Structural analysis AK. Gupta, VM. Katoch et al. Microarray analysis of efflux pump genes in multidrug-resistant Mycobacterium tuberculosis during stress induced by common anti-tuberculous drugs. Microb. Drug Resist. 2010 |
Interaction | PhysicalInteraction Rv2460c | akankshajain.21 | IDA | | Structural analysis authors,A. Gribun,MS. Kimber,R. Ching,R. Sprangers,KM. Fiebig,WA. Houry The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation. J. Biol. Chem. 2005 |
Citation | Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli. authors,MR. Maurizi,WP. Clark,Y. Katayama,S. Rudikoff,J. Pumphrey,B. Bowers,S. Gottesman J. Biol. Chem. 1990 | richasinha4u | IDA | 2197275 | Spectrophotometric Analysis |
Interaction | Regulatory Rv2457c | richasinha4u | IDA | | Spectrophotometric Analysis authors,MR. Maurizi,WP. Clark,Y. Katayama,S. Rudikoff,J. Pumphrey,B. Bowers,S. Gottesman Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli. J. Biol. Chem. 1990 |
Citation | The ATP-dependent Clp protease of Escherichia coli. Sequence of clpA and identification of a Clp-specific substrate. authors,S. Gottesman,WP. Clark,MR. Maurizi J. Biol. Chem. 1990 | richasinha4u | IDA | 2186030 | Spectrophotometric Analysis |
Interaction | Regulatory Rv2457c | richasinha4u | IDA | | Spectrophotometric Analysis authors,S. Gottesman,WP. Clark,MR. Maurizi The ATP-dependent Clp protease of Escherichia coli. Sequence of clpA and identification of a Clp-specific substrate. J. Biol. Chem. 1990 |
Interaction | PhysicalInteraction Rv2457c | richasinha4u | IDA | | Structural Analysis authors,B. Banecki,A. Wawrzynow,J. Puzewicz,C. Georgopoulos,M. Zylicz Structure-function analysis of the zinc-binding region of the Clpx molecular chaperone. J. Biol. Chem. 2001 |
Interaction | PhysicalInteraction Rv2457c | richasinha4u | IDA | | Structural Analysis authors,LW. Donaldson,U. Wojtyra,WA. Houry Solution structure of the dimeric zinc binding domain of the chaperone ClpX. J. Biol. Chem. 2003 |
Interaction | PhysicalInteraction Rv2457c | richasinha4u | IDA | | Structural Analysis authors,AY. Yu,WA. Houry ClpP: a distinctive family of cylindrical energy-dependent serine proteases. FEBS Lett. 2007 |
Interaction | PhysicalInteraction Rv2460c | akankshajain.21 | IDA | | Structural analysis AK. Gupta, VM. Katoch et al. Microarray analysis of efflux pump genes in multidrug-resistant Mycobacterium tuberculosis during stress induced by common anti-tuberculous drugs. Microb. Drug Resist. 2010 |
Interaction | PhysicalInteraction Rv2457c | vmevada102 | ISO | | Structural analysis authors,A. Gribun,MS. Kimber,R. Ching,R. Sprangers,KM. Fiebig,WA. Houry The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation. J. Biol. Chem. 2005 |
Interaction | PhysicalInteraction Rv2457c | richasinha4u | IDA | | Spectrophotometric Analysis authors,B. Banecki,A. Wawrzynow,J. Puzewicz,C. Georgopoulos,M. Zylicz Structure-function analysis of the zinc-binding region of the Clpx molecular chaperone. J. Biol. Chem. 2001 |
Interaction | PhysicalInteraction Rv2457c | richasinha4u | IDA | | Spectrophotometric Analysis authors,LW. Donaldson,U. Wojtyra,WA. Houry Solution structure of the dimeric zinc binding domain of the chaperone ClpX. J. Biol. Chem. 2003 |
Interaction | PhysicalInteraction Rv2457c | richasinha4u | IDA | | Spectrophotometric Analysis authors,AY. Yu,WA. Houry ClpP: a distinctive family of cylindrical energy-dependent serine proteases. FEBS Lett. 2007 |
Interaction | PhysicalInteraction Rv2457c | vmevada102 | ISO | | Structural analysis AK. Gupta, VM. Katoch et al. Microarray analysis of efflux pump genes in multidrug-resistant Mycobacterium tuberculosis during stress induced by common anti-tuberculous drugs. Microb. Drug Resist. 2010 |