Manuscript Number : IJSRST184937

In-silico Homology Modeling of MMP25 involved in Asthma

Authors(2) :-Yogesh N. Joshi, Shruti G. Gajul

Asthma is a chronic long term inflammatory disease of the airways of lungs in which the airways narrow, swell and produce extra mucus. This leads to a limitation of the flow of air to and from the lungs, causing shortness of breathing. According to the latest WHO estimates released in December 2016, there were 3,97,000 deaths in 2015 and about 334 million patients are suffering from asthma across the world. It is caused by a combination of genetic and environment factors. Exposure to second hand smoke, exhaust fumes or other types of allergens is the major risk factors for developing asthma. Subsequent work suggest that the MMP25 protein plays a crucial role for causing airway remodeling in asthma disease by cleaving fibronectin, a extracellular component secreted by fibroblast which maintains the form, solidity and integrity of the lungs. In the present study, we used different In-Silico tools and techniques which includes retrieval of MMP25 protein sequence from UniProt KB database and the sequence analysis was performed by using Protparam tool which concluded that the protein was unstable and basic in nature. The secondary structure was predicted by using GOR tool which indicated that the percentage of coils was higher than the percentage of alpha helix and extended strand. Then the 3D structure of MMP25 was predicted by using SWISS MODEL server and the model was validated by using PROCHECK analysis tool. After validation of the model, the validation score was 89.40% indicating that the model was of good quality and the predicted 3D structure was deposited in protein model database (PMDB). Further study on MMP25 protein can be carried out in molecular docking and in structure based drug designing (SBDD) to inhibit airway remodeling in asthma.

Authors and Affiliations

Yogesh N. Joshi
Department of PG Studies and Research in Bioinformatics, Walchand Centre for Biotechnology, Walchand College of Arts & Science, Solapur, Maharashtra, India
Shruti G. Gajul
Department of PG Studies and Research in Bioinformatics, Walchand Centre for Biotechnology, Walchand College of Arts & Science, Solapur, Maharashtra, India

In-Silico, Asthma, MMP25, UniProtKB, Homology Modeling

  1. "Asthma Fact sheet ?307". WHO. November 2013.
  2. NHLBI Guideline 2007, pp. 11-12.
  3. Murray, John F. (2010). "Ch. 38 Asthma". In Mason, Robert J.; Murray, John F.; Broaddus, V. Courtney; Nadel, Jay A.; Martin, Thomas R.; King. Jr., Talmadge E.; Schraufnagel, Dean E. Murray and Nadel’s textbook of respiratory medicine (5th ed.). Elsevier.ISBN 1-4160-4710-7.
  4. Rosner, Fred (2002). "The Life of Moses Maimonides, a Prominent Medieval Physician" (pdf).Einstein Quart J BiolMed. 19 (3): 125-128.
  5. Martinez F. D. (2007). "Genes, environments, development and asthma: a reappraisal". European Respiratory Journal. 29 (1):179-84. doi:10.1183/09031936.00087906.PMID 17197483.
  6. Tan, DJ; Walters, EH; Perret, JL; Lodge, CJ; Lowe, AJ; Matheson, MC; Dharmage, SC (February 2015). "Age-of-asthma onset as a determinant of different asthma phenotypes in adults: a systematic review and meta-analysis of 23. doi:10.1586/17476348.2015.1000311. PMID 25584929.
  7. Elward, Graham Douglas, Kurtis S. (2010). Asthma. London: Manson Pub. pp. 27–29. ISBN 978-1-84076-513-7.
  8. British Guideline 2009, p.4
  9. Available from:-(http://www.aafa.org/page/asthma-diagnosis.aspx).
  10. The Global Asthma Report 2014. Auckland, New Zealand: Global Asthma Network, 2014. Available from: (http://www.globalasthmareport.org/resources/Global_Asthma_Report_2014.pdf).
  11. Agarwal R, Denning DW, Chakrabarti A. Estimation of the burden of chronic and allergic pulmonary aspergillosis in India. (PLOS One) 2014; 9: e114745.
  12. Murthy KJR, Sastry JG. Economic burden of asthma. In: Burden of disease in India. Background papers. Available from: http://www.who.int/macronedth/action/NCMH_Burden of disease_%2829 Sep%202005%29.pdf.
  13. GBD 2015 Mortality and Causes of Death, Collaborators. (8 October 2016). "Global, regional, and national life expectancy, all-cause mortality, and cause-specific mortality for 249 causes of death, 1980–2015: a systematic analysis for the Global Burden of Disease Study 2015". Lancet. 388 (10053): 1459–1544. doi:10.1016/S0140-6736(16)31012-1. PMC 5388903?Freely accessible.PMID 27733281.
  14. Verma RP, Hansch C (March 2007). "Matrix metalloproteinases (MMPs): chemical-biological functions and (Q)SARs" (PDF). Bioorg. Med. Chem. 15 (6): 2223–68. doi:10.1016/j.bmc.2007.01.011. PMID 17275314.
  15. "Collagenolytic activity in amphibian tissues: a tissue culture assay". Proceedings of the National Academy of Sciences. 48 (6): 1014–22. June 1962. doi:10.1073/pnas.48.6.1014. PMC 220898?Freely accessible.PMID 13902219.
  16. II M., YAMAMOTO H., ADACHI Y., MARUYAMA Y., SHINOMURA Y., Role of MMP-7 (matrilysin) in human cancer invasion, apoptosis, growth, and angiogenesis, ExpBiol Med (Maywood), 2006,231(1):20-27.
  17. BRUMMER O., BOHMER G., HOLLWITZ B., FLEMMING P., PETRY K.U., KUHNLE H., MMP-1 and MMP-2 in the cervix uteri in different steps of malignant transformation- an immunohistochemical study, gynecoloncol, 2002, 84(2):222-227.
  18. CURRY T.E.JR., OSTEEN K.G., The matrix metalloproteinase system: changes, regulation, and impact throughout the ovarian and uterine reproductive cycle, Endocr Rev, 2003, 24(4):428-465.
  19. FOLGUERAS A.R., PENDAS A.M., SANCHEZ L.M.,LOPEZ-OTIN C., Matrix metalloproteinases in cancer: from new functions to improved inhibition strategies, Int J DevBiol, 2004, 48(5-6):411-424.
  20. Gross J, Lapiere C (1962). "COLLAGENOLYTIC ACTIVITY IN AMPHIBIAN TISSUES: A TISSUE CULTURE ASSAY". ProcNatlAcadSci USA. 48 (6): 1014–22. doi:10.1073/pnas.48.6.1014. PMC 220898?Freely accessible.PMID 13902219.
  21. VISSE R., NAGASE H., Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function and biochemistry, Circ Res, 2003, 92(8):827-839.
  22. MARCHENKO G. N., MARCHENKO N. D., STRONGIN A. Y., The structure and regulation of the human and mouse matrix metalloproteinase-21 gene and protein, Biochem J, 2003, 372(Pt 2):503-515.
  23. Pei D (Feb 2000). "Leukolysin/MMP25/MT6-MMP: a novel matrix metalloproteinase specifically expressed in the leukocyte lineage". Cell Res. 9 (4): 291–303. doi:10.1038/sj.cr.7290028. PMID 10628838.
  24. Velasco G, Cal S, Merlos-Suarez A, Ferrando AA, Alvarez S, Nakano A, Arribas J, Lopez-Otin C (Mar 2000). "Human MT6-matrix metalloproteinase: identification, progelatinaseA activation, and expression in brain tumors". Cancer Res. 60 (4): 877–82. PMID 10706098.
  25. "Entrez Gene: MMP25 matrix metallopeptidase 25".
  26. KOJIMA S., ITOH Y., MATSUMOTO S., MASUHO Y.,SEIKI M., Membrane-type 6 matrix metalloproteinase (MT6-MMP, MMP-25) is the secongglycosyl-phosphatidyl inositol (GPI)-anchored MMP,FEBS Lett, 2000,480(2–3):142–146.
  27. PEI D., Leukolysin/MMP25/MT6–MMP: a novel matrix metalloproteinase specifically expressed in the leukocyte lineage, Cell Res, 1999, 9(4):291-303.
  28. Available from: http://www.jacionline.org/article/S0091-6749(05)03316-6/fulltext.
  29. Magrane M. And the UniProt consortium.UniProt Knowledgebase: a hub of integrated protein data Database, 2011, bar009.
  30. Gasteiger E, Hooglan C, Gattiker A, Duvaud S, Wilkins MR, Appel RD et al. The Proteomics Protocols Handbook, Human Press, 2005, 571-607.
  31. 31Garnier J, Gibrat J-F. Robson B. GOR secondary structure prediction method version Methods in Enzymology K. F. Doolittle Ed 1996;266:540-553
  32. 32Arnold K, Bordoli L, Kopp J, Schwede T. The SWISSMODEL Workspace: A web-based environment for protein structure homology modelling. Bioinformatics 2006; 22:195-201
  33. Laskowski RA, MacArthur MW, Moss DS, Thornton JM. PROCHECK - a program to check the stereochemical quality of protein structures. J App. Cryst. 1993; 26:283-291

Publication Details

Published in : Volume 4 | Issue 9 | July-August 2018
Date of Publication : 2018-07-30
License:  This work is licensed under a Creative Commons Attribution 4.0 International License.
Page(s) : 202-208
Manuscript Number : IJSRST184937
Publisher : Technoscience Academy

Print ISSN : 2395-6011, Online ISSN : 2395-602X

Cite This Article :

Yogesh N. Joshi, Shruti G. Gajul, " In-silico Homology Modeling of MMP25 involved in Asthma", International Journal of Scientific Research in Science and Technology(IJSRST), Print ISSN : 2395-6011, Online ISSN : 2395-602X, Volume 4, Issue 9, pp.202-208, July-August-2018.
Journal URL : https://ijsrst.com/IJSRST184937
Citation Detection and Elimination     |      | |
  • NHLBI Guideline 2007, pp. 11-12.
  • Murray, John F. (2010). "Ch. 38 Asthma". In Mason, Robert J.; Murray, John F.; Broaddus, V. Courtney; Nadel, Jay A.; Martin, Thomas R.; King. Jr., Talmadge E.; Schraufnagel, Dean E. Murray and Nadel’s textbook of respiratory medicine (5th ed.). Elsevier.ISBN 1-4160-4710-7.
  • Rosner, Fred (2002). "The Life of Moses Maimonides, a Prominent Medieval Physician" (pdf).Einstein Quart J BiolMed. 19 (3): 125-128.
  • Martinez F. D. (2007). "Genes, environments, development and asthma: a reappraisal". European Respiratory Journal. 29 (1):179-84. doi:10.1183/09031936.00087906.PMID 17197483.
  • Tan, DJ; Walters, EH; Perret, JL; Lodge, CJ; Lowe, AJ; Matheson, MC; Dharmage, SC (February 2015). "Age-of-asthma onset as a determinant of different asthma phenotypes in adults: a systematic review and meta-analysis of 23. doi:10.1586/17476348.2015.1000311. PMID 25584929.
  • Elward, Graham Douglas, Kurtis S. (2010). Asthma. London: Manson Pub. pp. 27–29. ISBN 978-1-84076-513-7.
  • British Guideline 2009, p.4
  • Available from:-(http://www.aafa.org/page/asthma-diagnosis.aspx).
  • The Global Asthma Report 2014. Auckland, New Zealand: Global Asthma Network, 2014. Available from: (http://www.globalasthmareport.org/resources/Global_Asthma_Report_2014.pdf).
  • Agarwal R, Denning DW, Chakrabarti A. Estimation of the burden of chronic and allergic pulmonary aspergillosis in India. (PLOS One) 2014; 9: e114745.
  • Murthy KJR, Sastry JG. Economic burden of asthma. In: Burden of disease in India. Background papers. Available from: http://www.who.int/macronedth/action/NCMH_Burden of disease_%2829 Sep%202005%29.pdf.
  • GBD 2015 Mortality and Causes of Death, Collaborators. (8 October 2016). "Global, regional, and national life expectancy, all-cause mortality, and cause-specific mortality for 249 causes of death, 1980–2015: a systematic analysis for the Global Burden of Disease Study 2015". Lancet. 388 (10053): 1459–1544. doi:10.1016/S0140-6736(16)31012-1. PMC 5388903?Freely accessible.PMID 27733281.
  • Verma RP, Hansch C (March 2007). "Matrix metalloproteinases (MMPs): chemical-biological functions and (Q)SARs" (PDF). Bioorg. Med. Chem. 15 (6): 2223–68. doi:10.1016/j.bmc.2007.01.011. PMID 17275314.
  • "Collagenolytic activity in amphibian tissues: a tissue culture assay". Proceedings of the National Academy of Sciences. 48 (6): 1014–22. June 1962. doi:10.1073/pnas.48.6.1014. PMC 220898?Freely accessible.PMID 13902219.
  • II M., YAMAMOTO H., ADACHI Y., MARUYAMA Y., SHINOMURA Y., Role of MMP-7 (matrilysin) in human cancer invasion, apoptosis, growth, and angiogenesis, ExpBiol Med (Maywood), 2006,231(1):20-27.
  • BRUMMER O., BOHMER G., HOLLWITZ B., FLEMMING P., PETRY K.U., KUHNLE H., MMP-1 and MMP-2 in the cervix uteri in different steps of malignant transformation- an immunohistochemical study, gynecoloncol, 2002, 84(2):222-227.
  • CURRY T.E.JR., OSTEEN K.G., The matrix metalloproteinase system: changes, regulation, and impact throughout the ovarian and uterine reproductive cycle, Endocr Rev, 2003, 24(4):428-465.
  • FOLGUERAS A.R., PENDAS A.M., SANCHEZ L.M.,LOPEZ-OTIN C., Matrix metalloproteinases in cancer: from new functions to improved inhibition strategies, Int J DevBiol, 2004, 48(5-6):411-424.
  • Gross J, Lapiere C (1962). "COLLAGENOLYTIC ACTIVITY IN AMPHIBIAN TISSUES: A TISSUE CULTURE ASSAY". ProcNatlAcadSci USA. 48 (6): 1014–22. doi:10.1073/pnas.48.6.1014. PMC 220898?Freely accessible.PMID 13902219.
  • VISSE R., NAGASE H., Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function and biochemistry, Circ Res, 2003, 92(8):827-839.
  • MARCHENKO G. N., MARCHENKO N. D., STRONGIN A. Y., The structure and regulation of the human and mouse matrix metalloproteinase-21 gene and protein, Biochem J, 2003, 372(Pt 2):503-515.
  • Pei D (Feb 2000). "Leukolysin/MMP25/MT6-MMP: a novel matrix metalloproteinase specifically expressed in the leukocyte lineage". Cell Res. 9 (4): 291–303. doi:10.1038/sj.cr.7290028. PMID 10628838.
  • Velasco G, Cal S, Merlos-Suarez A, Ferrando AA, Alvarez S, Nakano A, Arribas J, Lopez-Otin C (Mar 2000). "Human MT6-matrix metalloproteinase: identification, progelatinaseA activation, and expression in brain tumors". Cancer Res. 60 (4): 877–82. PMID 10706098.
  • "Entrez Gene: MMP25 matrix metallopeptidase 25".
  • KOJIMA S., ITOH Y., MATSUMOTO S., MASUHO Y.,SEIKI M., Membrane-type 6 matrix metalloproteinase (MT6-MMP, MMP-25) is the secongglycosyl-phosphatidyl inositol (GPI)-anchored MMP,FEBS Lett, 2000,480(2–3):142–146.
  • PEI D., Leukolysin/MMP25/MT6–MMP: a novel matrix metalloproteinase specifically expressed in the leukocyte lineage, Cell Res, 1999, 9(4):291-303.
  • Available from: http://www.jacionline.org/article/S0091-6749(05)03316-6/fulltext.
  • Magrane M. And the UniProt consortium.UniProt Knowledgebase: a hub of integrated protein data Database, 2011, bar009.
  • Gasteiger E, Hooglan C, Gattiker A, Duvaud S, Wilkins MR, Appel RD et al. The Proteomics Protocols Handbook, Human Press, 2005, 571-607.
  • 31Garnier J, Gibrat J-F. Robson B. GOR secondary structure prediction method version Methods in Enzymology K. F. Doolittle Ed 1996;266:540-553
  • 32Arnold K, Bordoli L, Kopp J, Schwede T. The SWISSMODEL Workspace: A web-based environment for protein structure homology modelling. Bioinformatics 2006; 22:195-201
  • Laskowski RA, MacArthur MW, Moss DS, Thornton JM. PROCHECK - a program to check the stereochemical quality of protein structures. J App. Cryst. 1993; 26:283-291
    • " target="_blank"> BibTeX     |
  • NHLBI Guideline 2007, pp. 11-12.
  • Murray, John F. (2010). "Ch. 38 Asthma". In Mason, Robert J.; Murray, John F.; Broaddus, V. Courtney; Nadel, Jay A.; Martin, Thomas R.; King. Jr., Talmadge E.; Schraufnagel, Dean E. Murray and Nadel’s textbook of respiratory medicine (5th ed.). Elsevier.ISBN 1-4160-4710-7.
  • Rosner, Fred (2002). "The Life of Moses Maimonides, a Prominent Medieval Physician" (pdf).Einstein Quart J BiolMed. 19 (3): 125-128.
  • Martinez F. D. (2007). "Genes, environments, development and asthma: a reappraisal". European Respiratory Journal. 29 (1):179-84. doi:10.1183/09031936.00087906.PMID 17197483.
  • Tan, DJ; Walters, EH; Perret, JL; Lodge, CJ; Lowe, AJ; Matheson, MC; Dharmage, SC (February 2015). "Age-of-asthma onset as a determinant of different asthma phenotypes in adults: a systematic review and meta-analysis of 23. doi:10.1586/17476348.2015.1000311. PMID 25584929.
  • Elward, Graham Douglas, Kurtis S. (2010). Asthma. London: Manson Pub. pp. 27–29. ISBN 978-1-84076-513-7.
  • British Guideline 2009, p.4
  • Available from:-(http://www.aafa.org/page/asthma-diagnosis.aspx).
  • The Global Asthma Report 2014. Auckland, New Zealand: Global Asthma Network, 2014. Available from: (http://www.globalasthmareport.org/resources/Global_Asthma_Report_2014.pdf).
  • Agarwal R, Denning DW, Chakrabarti A. Estimation of the burden of chronic and allergic pulmonary aspergillosis in India. (PLOS One) 2014; 9: e114745.
  • Murthy KJR, Sastry JG. Economic burden of asthma. In: Burden of disease in India. Background papers. Available from: http://www.who.int/macronedth/action/NCMH_Burden of disease_%2829 Sep%202005%29.pdf.
  • GBD 2015 Mortality and Causes of Death, Collaborators. (8 October 2016). "Global, regional, and national life expectancy, all-cause mortality, and cause-specific mortality for 249 causes of death, 1980–2015: a systematic analysis for the Global Burden of Disease Study 2015". Lancet. 388 (10053): 1459–1544. doi:10.1016/S0140-6736(16)31012-1. PMC 5388903?Freely accessible.PMID 27733281.
  • Verma RP, Hansch C (March 2007). "Matrix metalloproteinases (MMPs): chemical-biological functions and (Q)SARs" (PDF). Bioorg. Med. Chem. 15 (6): 2223–68. doi:10.1016/j.bmc.2007.01.011. PMID 17275314.
  • "Collagenolytic activity in amphibian tissues: a tissue culture assay". Proceedings of the National Academy of Sciences. 48 (6): 1014–22. June 1962. doi:10.1073/pnas.48.6.1014. PMC 220898?Freely accessible.PMID 13902219.
  • II M., YAMAMOTO H., ADACHI Y., MARUYAMA Y., SHINOMURA Y., Role of MMP-7 (matrilysin) in human cancer invasion, apoptosis, growth, and angiogenesis, ExpBiol Med (Maywood), 2006,231(1):20-27.
  • BRUMMER O., BOHMER G., HOLLWITZ B., FLEMMING P., PETRY K.U., KUHNLE H., MMP-1 and MMP-2 in the cervix uteri in different steps of malignant transformation- an immunohistochemical study, gynecoloncol, 2002, 84(2):222-227.
  • CURRY T.E.JR., OSTEEN K.G., The matrix metalloproteinase system: changes, regulation, and impact throughout the ovarian and uterine reproductive cycle, Endocr Rev, 2003, 24(4):428-465.
  • FOLGUERAS A.R., PENDAS A.M., SANCHEZ L.M.,LOPEZ-OTIN C., Matrix metalloproteinases in cancer: from new functions to improved inhibition strategies, Int J DevBiol, 2004, 48(5-6):411-424.
  • Gross J, Lapiere C (1962). "COLLAGENOLYTIC ACTIVITY IN AMPHIBIAN TISSUES: A TISSUE CULTURE ASSAY". ProcNatlAcadSci USA. 48 (6): 1014–22. doi:10.1073/pnas.48.6.1014. PMC 220898?Freely accessible.PMID 13902219.
  • VISSE R., NAGASE H., Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function and biochemistry, Circ Res, 2003, 92(8):827-839.
  • MARCHENKO G. N., MARCHENKO N. D., STRONGIN A. Y., The structure and regulation of the human and mouse matrix metalloproteinase-21 gene and protein, Biochem J, 2003, 372(Pt 2):503-515.
  • Pei D (Feb 2000). "Leukolysin/MMP25/MT6-MMP: a novel matrix metalloproteinase specifically expressed in the leukocyte lineage". Cell Res. 9 (4): 291–303. doi:10.1038/sj.cr.7290028. PMID 10628838.
  • Velasco G, Cal S, Merlos-Suarez A, Ferrando AA, Alvarez S, Nakano A, Arribas J, Lopez-Otin C (Mar 2000). "Human MT6-matrix metalloproteinase: identification, progelatinaseA activation, and expression in brain tumors". Cancer Res. 60 (4): 877–82. PMID 10706098.
  • "Entrez Gene: MMP25 matrix metallopeptidase 25".
  • KOJIMA S., ITOH Y., MATSUMOTO S., MASUHO Y.,SEIKI M., Membrane-type 6 matrix metalloproteinase (MT6-MMP, MMP-25) is the secongglycosyl-phosphatidyl inositol (GPI)-anchored MMP,FEBS Lett, 2000,480(2–3):142–146.
  • PEI D., Leukolysin/MMP25/MT6–MMP: a novel matrix metalloproteinase specifically expressed in the leukocyte lineage, Cell Res, 1999, 9(4):291-303.
  • Available from: http://www.jacionline.org/article/S0091-6749(05)03316-6/fulltext.
  • Magrane M. And the UniProt consortium.UniProt Knowledgebase: a hub of integrated protein data Database, 2011, bar009.
  • Gasteiger E, Hooglan C, Gattiker A, Duvaud S, Wilkins MR, Appel RD et al. The Proteomics Protocols Handbook, Human Press, 2005, 571-607.
  • 31Garnier J, Gibrat J-F. Robson B. GOR secondary structure prediction method version Methods in Enzymology K. F. Doolittle Ed 1996;266:540-553
  • 32Arnold K, Bordoli L, Kopp J, Schwede T. The SWISSMODEL Workspace: A web-based environment for protein structure homology modelling. Bioinformatics 2006; 22:195-201
  • Laskowski RA, MacArthur MW, Moss DS, Thornton JM. PROCHECK - a program to check the stereochemical quality of protein structures. J App. Cryst. 1993; 26:283-291
    • " target="_blank">RIS     |
  • NHLBI Guideline 2007, pp. 11-12.
  • Murray, John F. (2010). "Ch. 38 Asthma". In Mason, Robert J.; Murray, John F.; Broaddus, V. Courtney; Nadel, Jay A.; Martin, Thomas R.; King. Jr., Talmadge E.; Schraufnagel, Dean E. Murray and Nadel’s textbook of respiratory medicine (5th ed.). Elsevier.ISBN 1-4160-4710-7.
  • Rosner, Fred (2002). "The Life of Moses Maimonides, a Prominent Medieval Physician" (pdf).Einstein Quart J BiolMed. 19 (3): 125-128.
  • Martinez F. D. (2007). "Genes, environments, development and asthma: a reappraisal". European Respiratory Journal. 29 (1):179-84. doi:10.1183/09031936.00087906.PMID 17197483.
  • Tan, DJ; Walters, EH; Perret, JL; Lodge, CJ; Lowe, AJ; Matheson, MC; Dharmage, SC (February 2015). "Age-of-asthma onset as a determinant of different asthma phenotypes in adults: a systematic review and meta-analysis of 23. doi:10.1586/17476348.2015.1000311. PMID 25584929.
  • Elward, Graham Douglas, Kurtis S. (2010). Asthma. London: Manson Pub. pp. 27–29. ISBN 978-1-84076-513-7.
  • British Guideline 2009, p.4
  • Available from:-(http://www.aafa.org/page/asthma-diagnosis.aspx).
  • The Global Asthma Report 2014. Auckland, New Zealand: Global Asthma Network, 2014. Available from: (http://www.globalasthmareport.org/resources/Global_Asthma_Report_2014.pdf).
  • Agarwal R, Denning DW, Chakrabarti A. Estimation of the burden of chronic and allergic pulmonary aspergillosis in India. (PLOS One) 2014; 9: e114745.
  • Murthy KJR, Sastry JG. Economic burden of asthma. In: Burden of disease in India. Background papers. Available from: http://www.who.int/macronedth/action/NCMH_Burden of disease_%2829 Sep%202005%29.pdf.
  • GBD 2015 Mortality and Causes of Death, Collaborators. (8 October 2016). "Global, regional, and national life expectancy, all-cause mortality, and cause-specific mortality for 249 causes of death, 1980–2015: a systematic analysis for the Global Burden of Disease Study 2015". Lancet. 388 (10053): 1459–1544. doi:10.1016/S0140-6736(16)31012-1. PMC 5388903?Freely accessible.PMID 27733281.
  • Verma RP, Hansch C (March 2007). "Matrix metalloproteinases (MMPs): chemical-biological functions and (Q)SARs" (PDF). Bioorg. Med. Chem. 15 (6): 2223–68. doi:10.1016/j.bmc.2007.01.011. PMID 17275314.
  • "Collagenolytic activity in amphibian tissues: a tissue culture assay". Proceedings of the National Academy of Sciences. 48 (6): 1014–22. June 1962. doi:10.1073/pnas.48.6.1014. PMC 220898?Freely accessible.PMID 13902219.
  • II M., YAMAMOTO H., ADACHI Y., MARUYAMA Y., SHINOMURA Y., Role of MMP-7 (matrilysin) in human cancer invasion, apoptosis, growth, and angiogenesis, ExpBiol Med (Maywood), 2006,231(1):20-27.
  • BRUMMER O., BOHMER G., HOLLWITZ B., FLEMMING P., PETRY K.U., KUHNLE H., MMP-1 and MMP-2 in the cervix uteri in different steps of malignant transformation- an immunohistochemical study, gynecoloncol, 2002, 84(2):222-227.
  • CURRY T.E.JR., OSTEEN K.G., The matrix metalloproteinase system: changes, regulation, and impact throughout the ovarian and uterine reproductive cycle, Endocr Rev, 2003, 24(4):428-465.
  • FOLGUERAS A.R., PENDAS A.M., SANCHEZ L.M.,LOPEZ-OTIN C., Matrix metalloproteinases in cancer: from new functions to improved inhibition strategies, Int J DevBiol, 2004, 48(5-6):411-424.
  • Gross J, Lapiere C (1962). "COLLAGENOLYTIC ACTIVITY IN AMPHIBIAN TISSUES: A TISSUE CULTURE ASSAY". ProcNatlAcadSci USA. 48 (6): 1014–22. doi:10.1073/pnas.48.6.1014. PMC 220898?Freely accessible.PMID 13902219.
  • VISSE R., NAGASE H., Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function and biochemistry, Circ Res, 2003, 92(8):827-839.
  • MARCHENKO G. N., MARCHENKO N. D., STRONGIN A. Y., The structure and regulation of the human and mouse matrix metalloproteinase-21 gene and protein, Biochem J, 2003, 372(Pt 2):503-515.
  • Pei D (Feb 2000). "Leukolysin/MMP25/MT6-MMP: a novel matrix metalloproteinase specifically expressed in the leukocyte lineage". Cell Res. 9 (4): 291–303. doi:10.1038/sj.cr.7290028. PMID 10628838.
  • Velasco G, Cal S, Merlos-Suarez A, Ferrando AA, Alvarez S, Nakano A, Arribas J, Lopez-Otin C (Mar 2000). "Human MT6-matrix metalloproteinase: identification, progelatinaseA activation, and expression in brain tumors". Cancer Res. 60 (4): 877–82. PMID 10706098.
  • "Entrez Gene: MMP25 matrix metallopeptidase 25".
  • KOJIMA S., ITOH Y., MATSUMOTO S., MASUHO Y.,SEIKI M., Membrane-type 6 matrix metalloproteinase (MT6-MMP, MMP-25) is the secongglycosyl-phosphatidyl inositol (GPI)-anchored MMP,FEBS Lett, 2000,480(2–3):142–146.
  • PEI D., Leukolysin/MMP25/MT6–MMP: a novel matrix metalloproteinase specifically expressed in the leukocyte lineage, Cell Res, 1999, 9(4):291-303.
  • Available from: http://www.jacionline.org/article/S0091-6749(05)03316-6/fulltext.
  • Magrane M. And the UniProt consortium.UniProt Knowledgebase: a hub of integrated protein data Database, 2011, bar009.
  • Gasteiger E, Hooglan C, Gattiker A, Duvaud S, Wilkins MR, Appel RD et al. The Proteomics Protocols Handbook, Human Press, 2005, 571-607.
  • 31Garnier J, Gibrat J-F. Robson B. GOR secondary structure prediction method version Methods in Enzymology K. F. Doolittle Ed 1996;266:540-553
  • 32Arnold K, Bordoli L, Kopp J, Schwede T. The SWISSMODEL Workspace: A web-based environment for protein structure homology modelling. Bioinformatics 2006; 22:195-201
  • Laskowski RA, MacArthur MW, Moss DS, Thornton JM. PROCHECK - a program to check the stereochemical quality of protein structures. J App. Cryst. 1993; 26:283-291
    • " target="_blank">CSV

    Article Preview