The DOI matches its Crossref record; 275 of the 275 references it cites were found in a registry or an index.
Matrix Metalloproteinases in Lung: Multiple, Multifarious, and Multifaceted
Open accessAbstract
The matrix metalloproteinases (MMPs), a family of 25 secreted and cell surface-bound neutral proteinases, process a large array of extracellular and cell surface proteins under normal and pathological conditions. MMPs play critical roles in lung organogenesis, but their expression, for the most part, is downregulated after generation of the alveoli. Our knowledge about the resurgence of the MMPs that occurs in most inflammatory diseases of the lung is rapidly expanding. Although not all members of the MMP family are found within the lung tissue, many are upregulated during the acute and chronic phases of these diseases. Furthermore, potential MMP targets in the lung include all structural proteins in the extracellular matrix (ECM), cell adhesion molecules, growth factors, cytokines, and chemokines. However, what is less known is the role of MMP proteolysis in modulating the function of these substrates in vivo. Because of their multiplicity and substantial substrate overlap, MMPs are thought to have redundant functions. However, as we explore in this review, such redundancy most likely evolved as a necessary compensatory mechanism given the critical regulatory importance of MMPs. While inhibition of MMPs has been proposed as a therapeutic option in a variety of inflammatory lung conditions, a complete understanding of the biology of these complex enzymes is needed before we can reasonably consider them as therapeutic targets.
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1 retracted
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Self-citationOxidants, oxidative stress and the biology of ageing
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New functions for the matrix metalloproteinases in cancer progression
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Self-citationHow Matrix Metalloproteinases Regulate Cell Behavior
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Self-citationChronic Obstructive Pulmonary Disease
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A matrix metalloproteinase expressed on the surface of invasive tumour cells
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Cited by
The Roles of Matrix Metalloproteinases and Their Inhibitors in Human Diseases
Cabral-Pacheco, G. A., Garza-Veloz, I., Castruita-De la Rosa, C., Ramirez-Acuña, J. M., Perez-Romero, B. A., Guerrero-Rodriguez, J. F., Martinez-Avila, N., & Martinez-Fierro, M. L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249739 · Cited by 1,820
Preparing for the First Breath: Genetic and Cellular Mechanisms in Lung Development
Morrisey, E. E., & Hogan, B. L. M. (2010) · Developmental Cell · doi:10.1016/j.devcel.2009.12.010 · Cited by 964
The role of TIMPs in regulation of extracellular matrix proteolysis
Arpino, V., Brock, M., & Gill, S. E. (2015) · Matrix Biology · doi:10.1016/j.matbio.2015.03.005 · Cited by 734
Matrix Metalloproteinases as Therapeutic Targets for Idiopathic Pulmonary Fibrosis
Craig, V. J., Zhang, L., Hagood, J. S., & Owen, C. A. (2015) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2015-0020tr · Cited by 507
Tuberculous Granuloma Induction via Interaction of a Bacterial Secreted Protein with Host Epithelium
Volkman, H. E., Pozos, T. C., Zheng, J., Davis, J. M., Rawls, J. F., & Ramakrishnan, L. (2010) · Science · doi:10.1126/science.1179663 · Cited by 448
Metadata
- Authors
- Greenlee, K. J., Werb, Z., & Kheradmand, F.
- Venue
- Physiological Reviews
- Publisher
- American Physiological Society
- Published
- 2007-01
- Volume
- 87
- Issue
- 1
- Pages
- 69-98
- ISSN
- 0031-9333 (ISSN-L)
- 1522-1210
- OpenAlex
- W2162313829
- Cited by
- 474
- References
- 275
- FWCI
- 1.59
- Type
- journal article
- Language
- en
- Open access
- green
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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