The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family.

Van Wart, H E; Birkedal-Hansen, H

doi:10.1073/pnas.87.14.5578

Cited by 1,475Protease and Inhibitor MechanismsBlood Coagulation and Thrombosis MechanismsPeptidase Inhibition and Analysis

The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family.

Open access

Van Wart, H E, Birkedal-Hansen, H·1990·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.87.14.5578PMC PMC54368

Open this paper in CoChat — free account

Abstract

The general applicability of the "cysteine-switch" activation mechanism to the members of the matrix metalloproteinase (MMP) gene family is examined here. All currently known members of the MMP gene family share the characteristic that they are synthesized in a latent, inactive, form. Recent evidence suggests that this latency in human fibroblast collagenase (HFC) is the result of formation of an intramolecular complex between the single cysteine residue in its propeptide domain and the essential zinc atom in the catalytic domain, a complex that blocks the active site. Latent HFC can be activated by multiple means, all of which effect the dissociation of the cysteine residue from the complex. This is referred to as the "cysteine-switch" mechanism of activation. The propeptide domain that contains the critical cysteine residue and the catalytic domain that contains the zinc-binding site are the only two domains common to all of the MMPs. The amino acid sequences surrounding both the critical cysteine residue and a region of the protein chains containing two of the putative histidine zinc-binding ligands are highly conserved in all of the MMPs. A survey of the literature shows that many of the individual MMPs can be activated by the multiple means observed for latent HFC. These observations support the view that the cysteine-switch mechanism is applicable to all members of this gene family. This mechanism is unprecedented in enzymology as far as we know and offers the opportunity for multiple modes of physiological activation of these important enzymes. Since conditions in different cells and tissues may match those necessary to effect one of these activation modes for a given MMP, this may offer metabolic flexibility in the control of MMP activation.

Integrity signals

Registry

Crossref · 10.1073/pnas.87.14.5578

Cites

51 of 51 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

The ADAM and ADAMTS families of metalloproteases are encoded by over 40 human genes, mediate cell-cell and cell-matrix interactions, and are involved in a range of human diseases.
“The ADAM (A Disintegrin And Metalloprotease) and ADAMTS families of metalloproteases are encoded by over 40 human genes, mediate cell-cell and cell-matrix interactions (20, 21) and are involved in a range of human diseases, including cancer metastasis, inflammatory disorders, neurological diseases and asthma (21, 22).”
From Accurate prediction of protein structures and interactions using a 3-track network (2021) · cites this paper as [21]

Electrochemical Photolysis of Water at a Semiconductor Electrode
FUJISHIMA, A., & HONDA, K. (1972) · Nature · doi:10.1038/238037a0 · Cited by 34,169 · see citing works
SV40-transformed Human Lung Fibroblasts Secrete a 92-kDa Type IV Collagenase Which Is Identical to That Secreted by Normal Human Macrophages
Wilhelm, S. M., Collier, I. E., Marmer, B. L., Eisen, A. Z., Grant, G. A., & Goldberg, G. I. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)71480-4 · Cited by 1,109 · see citing works
H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen.
Collier, I. E., Wilhelm, S. M., Eisen, A. Z., Marmer, B. L., Grant, G. A., Seltzer, J. L., Kronberger, A., He, C. S., Bauer, E. A., & Goldberg, G. I. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68680-6 · Cited by 1,044 · see citing works
Multiple modes of activation of latent human fibroblast collagenase: evidence for the role of a Cys73 active-site zinc complex in latency and a "cysteine switch" mechanism for activation.
Springman, E. B., Angleton, E. L., Birkedal‐Hansen, H., & Wart, H. E. V. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.1.364 · Cited by 713 · see citing works
Self-citation
Endogenous Activation of Latent Collagenase by Rheumatoid Synovial Cells
Werb, Z., Mainardi, C. L., Vater, C. A., & Harris, E. D. (1977) · New England Journal of Medicine · doi:10.1056/nejm197705052961801 · Cited by 685 · see citing works
Human fibroblast collagenase. Complete primary structure and homology to an oncogene transformation-induced rat protein.
Goldberg, G. I., Wilhelm, S. M., Kronberger, A., Bauer, E. A., Grant, G. A., & Eisen, A. Z. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84605-7 · Cited by 632 · see citing works
Oxidative Autoactivation of Latent Collagenase by Human Neutrophils
Weiss, S. J., Peppin, G. J., Ortiz, X., Ragsdale, C. G., & Test, S. T. (1985) · Science · doi:10.1126/science.2982211 · Cited by 472 · see citing works
A unique signature identifies a family of zinc‐dependent metallopeptidases
Jongeneel, C. V., Bouvier, J., & Bairoch, A. (1989) · FEBS Letters · doi:10.1016/0014-5793(89)80471-5 · Cited by 462 · see citing works
Comparison of human stromelysin and collagenase by cloning and sequence analysis
Whitham, S. E., Murphy, G., Angel, P. E., Rahmsdorf, H. J., Smith, B. J., Lyons, A., Harris, T. J. R., Reynolds, J. J., Herrlich, P. A., & Docherty, A. (1986) · Biochemical Journal · doi:10.1042/bj2400913 · Cited by 436 · see citing works
Active-site zinc ligands and activated H2O of zinc enzymes.
Vallée, B. L., & Auld, D. S. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.1.220 · Cited by 434 · see citing works
The collagenase gene family in humans consists of at least four members
Müller, D., Quantin, B., Gesnel, M.-C., Millon, R., Abecassis, J., & Breathnach, R. (1988) · Biochemical Journal · doi:10.1042/bj2530187 · Cited by 365 · see citing works
The Activation of Human Type IV Collagenase Proenzyme
Stetler‐Stevenson, W. G., Krutzsch, H. C., Wacher, M. P., Margulies, I., & Liotta, L. A. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94193-1 · Cited by 335 · see citing works
Epidermal growth factor and oncogenes induce transcription of the same cellular mRNA in rat fibroblasts.
Matrisian, L. M., Glaichenhaus, N., Gesnel, M.-C., & Breathnach, R. (1985) · The EMBO Journal · doi:10.1002/j.1460-2075.1985.tb03799.x · Cited by 333 · see citing works
Human skin fibroblast stromelysin: structure, glycosylation, substrate specificity, and differential expression in normal and tumorigenic cells.
Wilhelm, S. M., Collier, I. E., Kronberger, A., Eisen, A. Z., Marmer, B. L., Grant, G. A., Bauer, E. A., & Goldberg, G. I. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.19.6725 · Cited by 321 · see citing works
Molecular structure of an aspartic proteinase zymogen, porcine pepsinogen, at 1.8 Å resolution
James, M. N. G., & Sielecki, A. R. (1986) · Nature · doi:10.1038/319033a0 · Cited by 299 · see citing works
Genes for alkaline protease and neutral protease from Bacillus amyloliquefaciens contain a large open reading frame between the regions coding for signal sequence and mature protein
Vasantha, N., Thompson, L. D., Rhodes, C. S., Banner, C., Nagle, J. W., & Filpula, D. R. (1984) · Journal of Bacteriology · doi:10.1128/jb.159.3.811-819.1984 · Cited by 275 · see citing works
Activation of the endogenous metalloproteinase, gelatinase, by triggered human neutrophils.
Peppin, G. J., & Weiss, S. J. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.12.4322 · Cited by 258 · see citing works
Collagenase production by human skin fibroblasts
Bauer, E. A., Stricklin, G. P., Jeffrey, J. J., & Eisen, A. Z. (1975) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(75)90243-0 · Cited by 254 · see citing works
Molecular characterization and nucleotide sequence of the Pseudomonas aeruginosa elastase structural gene
Bever, R., & Iglewski, B. H. (1988) · Journal of Bacteriology · doi:10.1128/jb.170.9.4309-4314.1988 · Cited by 232 · see citing works
Evidence that latent collagenases are enzyme-inhibitor complexes
Sellers, A., Cartwright, E., Murphy, G., & Reynolds, J. J. (1977) · Biochemical Journal · doi:10.1042/bj1630303 · Cited by 221 · see citing works
Pump-1 cDNA codes for a protein with characteristics similar to those of classical collagenase family members
Quantin, B., Murphy, G., & Breathnach, R. (1989) · Biochemistry · doi:10.1021/bi00439a004 · Cited by 210 · see citing works
Human skin fibroblast procollagenase: mechanisms of activation by organomercurials and trypsin
Stricklin, G. P., Jeffrey, J. J., Roswit, W. T., & Eisen, A. Z. (1983) · Biochemistry · doi:10.1021/bi00270a009 · Cited by 200 · see citing works
Detergent-activation of latent collagenase and resolution of its component molecules
Birkedal‐Hansen, H., & TAYLOR, R. E. (1982) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(82)80120-4 · Cited by 197 · see citing works
Self-citation
Cloning and sequencing ofSerratiaprotease gene
Nakahama, K., Yoshimura, K., Marumoto, R., Kikuchi, M., Lee, I. S., Hase, T., & Matsubara, H. (1986) · Nucleic Acids Research · doi:10.1093/nar/14.14.5843 · Cited by 189 · see citing works
Zymogens of Proteolytic Enzymes
Kassell, B., & Kay, J. (1973) · Science · doi:10.1126/science.180.4090.1022 · Cited by 172 · see citing works
Structure-function relationships in the collagenase family member transin.
Sánchez‐López, R., Nicholson, R. C., Gesnel, M.-C., Matrisian, L. M., & Breathnach, R. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37870-0 · Cited by 169 · see citing works
The activation of human skin fibroblast procollagenase. Sequence identification of the major conversion products.
Grant, G. A., Eisen, A. Z., Marmer, B. L., Roswit, W. T., & Goldberg, G. I. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45657-8 · Cited by 169 · see citing works
The latent collagenase and gelatinase of human polymorphonuclear neutrophil leucocytes
Murphy, G., Bretz, U., Baggiolini, M., & Reynolds, J. J. (1980) · Biochemical Journal · doi:10.1042/bj1920517 · Cited by 165 · see citing works
[8] Catabolism and turnover of collagens: Collagenases
Birkedal‐Hansen, H. (1987) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(87)44177-3 · Cited by 157 · see citing works
Self-citation
Nucleotide sequence and promoter region for the neutral protease gene from Bacillus stearothermophilus
Takagi, M., Imanaka, T., & Aiba, S. (1985) · Journal of Bacteriology · doi:10.1128/jb.163.3.824-831.1985 · Cited by 137 · see citing works
Sequences coding for part of oncogene-induced transin are highly conserved in a related rat gene
Breathnach, R., Matrisian, L. M., Gesnel, M.-C., Staub, A., & Leroy, P. (1987) · Nucleic Acids Research · doi:10.1093/nar/15.3.1139 · Cited by 128 · see citing works
MECHANISMS OF ZYMOGEN ACTIVATION
Stroud, R. M., Kossiakoff, A. A., & Chambers, J. L. (1977) · Annual Review of Biophysics and Bioengineering · doi:10.1146/annurev.bb.06.060177.001141 · Cited by 117 · see citing works
A gene for rabbit synovial cell collagenase: member of a family of metalloproteinases that degrades the connective tissue matrix
Fini, M. E., Plucinska, I. M., Mayer, A. S., Gross, R., & Brinckerhoff, C. (1987) · Biochemistry · doi:10.1021/bi00393a032 · Cited by 112 · see citing works
Characterization and activation of procollagenase from human polymorphonuclear leucocytes
Knäuper, V., KRÄMER, S., Reinke, H., & TSCHECHE, H. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb15489.x · Cited by 100 · see citing works
Monoclonal antibodies to human fibroblast procollagenase. Inhibition of enzymatic activity, affinity purification of the enzyme, and evidence for clustering of epitopes in the amino-terminal end of the activated enzyme
BIRKEDAL‐HANSEN, B., Moore, W. G. I., TAYLOR, R. E., Bhown, A. S., & Birkedal‐Hansen, H. (1988) · Biochemistry · doi:10.1021/bi00418a016 · Cited by 91 · see citing works
Self-citation
Role of granulocyte collagenase in collagen degradation.
Gs, L., Daniels, J. R., Lian, J. B., & Burleigh, M. C. (1972) · PubMed Central · Cited by 87 · see citing works
Latent and Active Human Polymorphonuclear Leukocyte Collagenases
MACARTNEY, H. W., & Tschesche, H. (1983) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1983.tb07118.x · Cited by 87 · see citing works
Cloning of a complementary dna for rabbit proactivator. a metalloproteinase that activates synovial cell collagenase, shares homology with stromelysin and transin, and is coordinately regulated with collagenase
Fini, M. E., Karmilowicz, M. J., Ruby, P. L., Beeman, A. M., Borges, K. A., & Brinckerhoff, C. (1987) · Arthritis & Rheumatism · doi:10.1002/art.1780301108 · Cited by 84 · see citing works
Short and long spacer sequences and other structural features of zinc binding sites in zinc enzymes
Vallée, B. L., & Auld, D. S. (1989) · FEBS Letters · doi:10.1016/0014-5793(89)81805-8 · Cited by 78 · see citing works
Procarboxypeptidase A and carboxypeptidase A of the spiny Pacific dogfish (Squalus acanthias)
Neurath, H., & Lacko, A. G. (1970) · Biochemistry · doi:10.1021/bi00826a010 · Cited by 68 · see citing works
Latent collagenase from human polymorphonuclear leucocytes and activation to collagenase by removal of an inhibitor
MACARTNEY, H. W., & Tschesche, H. (1980) · FEBS Letters · doi:10.1016/0014-5793(80)80282-1 · Cited by 66 · see citing works
A New Principle of Regulation of Enzymic Activity
Tschesche, H., & MACARTNEY, H. W. (1981) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1981.tb05687.x · Cited by 65 · see citing works
The Primary Structure ofBacillus cereusNeutral Proteinase and Comparison with Thermolysin andBacillus subtilisNeutral Proteinase
Sidler, W., Niederer, E., Suter, F., & Zuber, H. (1986) · Biological Chemistry Hoppe-Seyler · doi:10.1515/bchm3.1986.367.2.643 · Cited by 61 · see citing works
Human fibroblast collagenase contains an amino acid sequence homologous to the zinc-binding site of Serratia protease.
McKerrow, J. H. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45517-2 · Cited by 59 · see citing works
Nucleotide sequence of the pepN gene encoding aminopeptidase N of Escherichia coli
Foglino, M., Gharbi, S., & Lazdunski, A. M. (1986) · Gene · doi:10.1016/0378-1119(86)90366-5 · Cited by 56 · see citing works
Purification of a Gelatin-Degrading Type IV Collagenase Secreted by ras Oncogene-Transformed Fibroblasts
Spinucci, C., Zucker, S., Wieman, J. M., Lysik, R. M., Imhof, B., Ramamurthy, N., Liotta, L. A., & Nagase, H. (1988) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/80.17.1416 · Cited by 37 · see citing works
Synovial Collagenase and Joint Diseases: The Significancy of Latent Collagenase with Special Reference to Rheumatoid Arthritis
Shigeto, A. B. E., Shinmei, M., & Nagai, Y. (1973) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a130154 · Cited by 36 · see citing works
The stoichiometric activation of human skin fibroblast pro-collagenase by factors present in human skin and rat uterus
Tyree, B., Seltzer, J. L., Halme, J. K., Jeffrey, J. J., & Eisen, A. Z. (1981) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(81)90530-0 · Cited by 29 · see citing works
Evidence of homologous relationship between thermolysin and neutral protease A of Bacillus subtilis.
Levy, P. L., Pangburn, M. K., Burstein, Y., Ericsson, L. H., Neurath, H., & Walsh, K. A. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.11.4341 · Cited by 27 · see citing works
Gold sodium thiomalate activates latent human leukocyte collagenase
Lindy, S., Sorsa, T. A., Suomalainen, K., & Turto, H. (1986) · FEBS Letters · doi:10.1016/0014-5793(86)81523-x · Cited by 20 · see citing works
Activation of human leucocyte procollagenase by rheumatoid synovial tissue culture medium.
Wize, J., Abgarowicz, T., Wojtecka-Lukasik, E., Ksiȩżny, S., & Dancewicz, A. M. (1975) · Annals of the Rheumatic Diseases · doi:10.1136/ard.34.6.520 · Cited by 12 · see citing works

Flagged first, then by citations

Sorted by citations

Accurate prediction of protein structures and interactions using a 3-track network
Baek, M., DiMaio, F., Anishchenko, I., Dauparas, J., Ovchinnikov, S., Lee, G. R., Wang, J., Cong, Q., Kinch, L. N., Schaeffer, R. D., et al. (2021) · doi:10.1101/2021.06.14.448402 · Cited by 5,542 · see citing works
Matrix Metalloproteinases and Tissue Inhibitors of Metalloproteinases: Structure, Function, and Biochemistry
Visse, R., & Nagase, H. (2003) · Circulation Research · doi:10.1161/01.res.0000070112.80711.3d · Cited by 4,575 · see citing works
How Matrix Metalloproteinases Regulate Cell Behavior
Sternlicht, M. D., & Werb, Z. (2001) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.17.1.463 · Cited by 3,959 · see citing works
Matrix Metalloproteinases
Nagase, H., & Woessner, J. F. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.31.21491 · Cited by 3,905 · see citing works
Matrix Metalloproteinases: A Review
Birkedal‐Hansen, H., Moore, W. G. I., Bodden, M., Windsor, L. J., BIRKEDAL‐HANSEN, B., DeCarlo, A. A., & Engler, J. A. (1993) · Critical Reviews in Oral Biology & Medicine · doi:10.1177/10454411930040020401 · Cited by 2,957 · see citing works
Self-citation
Cancer metastasis and angiogenesis: An imbalance of positive and negative regulation
Liotta, L. A., Steeg, P. S., & Stetler‐Stevenson, W. G. (1991) · Cell · doi:10.1016/0092-8674(91)90642-c · Cited by 2,701 · see citing works
Role of Oxidative Modifications in Atherosclerosis
Stocker, R., & Keaney, J. F. (2004) · Physiological Reviews · doi:10.1152/physrev.00047.2003 · Cited by 2,611 · see citing works
A matrix metalloproteinase expressed on the surface of invasive tumour cells
Sato, H., Takino, T., Okada, Y., Cao, J. P., Shinagawa, A., Yamamoto, E., & Seiki, M. (1994) · Nature · doi:10.1038/370061a0 · Cited by 2,534 · see citing works
Matrix metalloproteinases as modulators of inflammation and innate immunity
Parks, W. C., Wilson, C. L., & López-Boado, Y. S. (2004) · Nature Reviews Immunology · doi:10.1038/nri1418 · Cited by 1,929 · see citing works
Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-α
Moss, M. L., Jin, S.-L. C., Milla, M. E., Burkhart, W., Carter, H. L., Chen, W., Clay, W. C., Didsbury, J. R., Hassler, D. F., Hoffman, C. R., et al. (1997) · Nature · doi:10.1038/385733a0 · Cited by 1,611 · see citing works
Mechanism Of Cell Surface Activation Of 72-kDa Type IV Collagenase
Strongin, A. Y., Collier, I. E., Bannikov, G. A., Marmer, B. L., Grant, G. A., & Goldberg, G. I. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.10.5331 · Cited by 1,589 · see citing works
Function and Mechanism of Zinc Metalloenzymes
McCall, K. A., Huang, C.-C., & Fierke, C. A. (2000) · Journal of Nutrition · doi:10.1093/jn/130.5.1437s · Cited by 1,144 · see citing works
Reactive oxygen species produced by macrophage-derived foam cells regulate the activity of vascular matrix metalloproteinases in vitro. Implications for atherosclerotic plaque stability.
Rajagopalan, S., Meng, X. P., Ramasamy, S., Harrison, D. G., & Galis, Z. S. (1996) · Journal of Clinical Investigation · doi:10.1172/jci119076 · Cited by 1,137 · see citing works
A novel metalloproteinase gene specifically expressed in stromal cells of breast carcinomas
Basset, P., Bellocq, J., Wolf, C., Stoll, I., Hutin, P., Limacher, J. M., Podhajcer, O. L., Chenard, M., Rio, M., & Chambon, P. (1990) · Nature · doi:10.1038/348699a0 · Cited by 1,125 · see citing works
Regulation of matrix metalloproteinases: An overview
Chakraborti, S., Mandal, M., Das, S. K., Mandal, A., & Chakraborti, T. (2003) · Molecular and Cellular Biochemistry · doi:10.1023/a:1026028303196 · Cited by 1,123 · see citing works
Myocardial Matrix Remodeling and the Matrix Metalloproteinases: Influence on Cardiac Form and Function
Spinale, F. G. (2007) · Physiological Reviews · doi:10.1152/physrev.00012.2007 · Cited by 1,109 · see citing works
Matrix metalloproteinases: a tail of a frog that became a prince
Brinckerhoff, C., & Matrisian, L. M. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm763 · Cited by 1,098 · see citing works
A Novel Proteolytic Cleavage Involved in Notch Signaling
Brou, C., Logeat, F., Gupta-Rossi, N., Chable-Bessia, C., Bail, O. L., Doedens, J. R., Cumano, A., Roux, P., Black, R. A., & Israël, A. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80417-7 · Cited by 1,089 · see citing works
Proteolytic remodeling of extracellular matrix
Birkedal‐Hansen, H. (1995) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(95)80116-2 · Cited by 1,063 · see citing works
Self-citation
The ADAMs family of metalloproteases: multidomain proteins with multiple functionsPreprint
Seals, D. F., & Courtneidge, S. A. (2003) · Genes & Development · doi:10.1101/gad.1039703 · Cited by 1,058 · see citing works
Metalloproteinases and Wound Healing
Caley, M. P., Martins, V., & O’Toole, E. A. (2015) · Advances in Wound Care · doi:10.1089/wound.2014.0581 · Cited by 1,003 · see citing works
Hemilability of Hybrid Ligands and the Coordination Chemistry of Oxazoline-Based Systems
Braunstein, P., & Naud, F. (2001) · Angewandte Chemie International Edition · doi:10.1002/1521-3773(20010216)40:4 · Cited by 951 · see citing works
S-nitrosylation of matrix metalloproteinases: signaling pathway to neuronal cell death
Gu, Z., Kaul, M., Yan, B., Kridel, S. J., Cui, J., Strongin, A., Smith, J. W., Liddington, R. C., & Lipton, S. A. (2002) · Science · doi:10.1126/science.1073634 · Cited by 950 · see citing works
Matrix metalloproteinases in neuroinflammation
Rosenberg, G. A. (2002) · Glia · doi:10.1002/glia.10108 · Cited by 868 · see citing works
Structure of von Willebrand Factor-cleaving Protease (ADAMTS13), a Metalloprotease Involved in Thrombotic Thrombocytopenic Purpura
Zheng, X. L., Chung, D. W., Τakayama, T. K., Majerus, E. M., Sadler, J. E., & Fujikawa, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100515200 · Cited by 839 · see citing works
Physiology and pathophysiology of matrix metalloproteases
Klein, T., & Bischoff, R. (2010) · Amino Acids · doi:10.1007/s00726-010-0689-x · Cited by 834 · see citing works
Matrix metalloproteinases in tumor invasion and metastasis
Stamenkovic, I. (2000) · Seminars in Cancer Biology · doi:10.1006/scbi.2000.0379 · Cited by 809 · see citing works
Matrix metalloproteinase inhibitors as therapy for inflammatory and vascular diseases
Hu, J., den Steen, P. E. V., Sang, Q. A., & Opdenakker, G. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2308 · Cited by 798 · see citing works
Matrix metalloproteinases in the brain and blood–brain barrier: Versatile breakers and makers
Rempe, R. G., Hartz, A. M. S., & Bauer, B. (2016) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x16655551 · Cited by 784 · see citing works
The ADAMTS metalloproteinases
PORTER, S., CLARK, I. M., KEVORKIAN, L., & EDWARDS, D. R. (2005) · Biochemical Journal · doi:10.1042/bj20040424 · Cited by 779 · see citing works
Matrix metalloproteinases: structures, evolution, and diversification
Massova, I., Kotra, L. P., Fridman, R. A., & Mobashery, S. (1998) · The FASEB Journal · doi:10.1096/fasebj.12.12.1075 · Cited by 779 · see citing works
Biological role of matrix metalloproteinases: a critical balance
Löffek, S., Schilling, O., & Franzke, C.-W. (2010) · European Respiratory Journal · doi:10.1183/09031936.00146510 · Cited by 763 · see citing works
Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas
Freije, J. M. P., Diez‐Itza, I., Balbı́n, M., Sánchez, L. M., Blasco, R., Tolivia, J., & López-Otı́n, C. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)89457-7 · Cited by 757 · see citing works
Progress in matrix metalloproteinase research
MURPHY, G., & Nagase, H. (2008) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2008.05.002 · Cited by 755 · see citing works
The metzincins — Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a super family of zinc‐peptidases
Stöcker, W., Grams, F., Reinemer, P., Bode, W., Baumann, U., Gomis‐Rüth, F. X., & McKay, D. (1995) · Protein Science · doi:10.1002/pro.5560040502 · Cited by 725 · see citing works
Zinc in wound healing: Theoretical, experimental, and clinical aspects
Lansdown, A. B. G., Mirastschijski, U., Stubbs, N., Scanlon, E., & Ågren, M. S. (2007) · Wound Repair and Regeneration · doi:10.1111/j.1524-475x.2006.00179.x · Cited by 720 · see citing works
Ultraviolet radiation and skin aging: roles of reactive oxygen species, inflammation and protease activation, and strategies for prevention of inflammation‐induced matrix degradation – a review
Pillai, S., Oresajo, C., & Hayward, J. (2005) · International Journal of Cosmetic Science · doi:10.1111/j.1467-2494.2004.00241.x · Cited by 706 · see citing works
Tumor invasion and metastasis: an imbalance of positive and negative regulation.
Liotta, L. A., & Stetler‐Stevenson, W. G. (1991) · PubMed · Cited by 705 · see citing works
Purification and Cloning of Aggrecanase-1: A Member of the ADAMTS Family of Proteins
Tortorella, M. D., Burn, T. C., Pratta, M. A., Abbaszade, I., Hollis, J. M., Liu, R., Rosenfeld, S. A., Copeland, R. A., Decicco, C. P., Wynn, R., et al. (1999) · Science · doi:10.1126/science.284.5420.1664 · Cited by 686 · see citing works
Role of Matrix Metalloproteinases in Human Periodontal Diseases
Birkedal‐Hansen, H. (1993) · Journal of Periodontology · doi:10.1902/jop.1993.64.5s.474 · Cited by 670 · see citing works
Self-citation
Gelatinase-mediated migration and invasion of cancer cells
Björklund, M., & Koivunen, E. (2005) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2005.03.001 · Cited by 663 · see citing works
Control of matrix metalloproteinase catalytic activity
Ra, H.-J., & Parks, W. C. (2007) · Matrix Biology · doi:10.1016/j.matbio.2007.07.001 · Cited by 645 · see citing works
Zinc in Wound Healing Modulation
Lin, P.-H., Sermersheim, M., Li, H., Lee, P. H. U., Steinberg, S. M., & Ma, J. (2017) · Nutrients · doi:10.3390/nu10010016 · Cited by 643 · see citing works
Matrix metalloproteinases and diseases of the CNS
Yong, V. W., Forsyth, P. A., Bell, R. B., Krekoski, C. A., & Edwards, D. R. (1998) · Trends in Neurosciences · doi:10.1016/s0166-2236(97)01169-7 · Cited by 635 · see citing works
Role of cytokines and inflammatory mediators in tissue destruction
Birkedal‐Hansen, H. (1993) · Journal of Periodontal Research · doi:10.1111/j.1600-0765.1993.tb02113.x · Cited by 618 · see citing works
Self-citation
Hemorrhagic metalloproteinases from snake venoms
Bjarnason, J. B., & Fox, J. W. (1994) · Pharmacology & Therapeutics · doi:10.1016/0163-7258(94)90049-3 · Cited by 616 · see citing works
Matrix metalloproteinases in skin
Kähäri, V., & Saarialho‐Kere, U. (1997) · Experimental Dermatology · doi:10.1111/j.1600-0625.1997.tb00164.x · Cited by 602 · see citing works
Vascular Cell Adhesion Molecule-1 Expression and Signaling During Disease: Regulation by Reactive Oxygen Species and Antioxidants
Cook‐Mills, J. M., Marchese, M. E., & Abdala‐Valencia, H. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3522 · Cited by 597 · see citing works
Matrix metalloproteinases and their multiple roles in neurodegenerative diseases
Rosenberg, G. A. (2009) · The Lancet Neurology · doi:10.1016/s1474-4422(09)70016-x · Cited by 594 · see citing works
Bone Marrow Neovascularization, Plasma Cell Angiogenic Potential, and Matrix Metalloproteinase-2 Secretion Parallel Progression of Human Multiple Myeloma
Vacca, A., Ribatti, D., Presta, M., Minischetti, M., Iurlaro, M., Ria, R., Albini, A., Bussolino, F., & Dammacco, F. (1999) · Blood · doi:10.1182/blood.v93.9.3064 · Cited by 593 · see citing works
Matrix metalloproteinases in cancer: from new functions to improved inhibition strategies
Folgueras, A. R., Pendás, A. M., Sanchez, L. M., & López-Otı́n, C. (2004) · The International Journal of Developmental Biology · doi:10.1387/ijdb.041811af · Cited by 584 · see citing works
The TIMP2 Membrane Type 1 Metalloproteinase “Receptor” Regulates the Concentration and Efficient Activation of Progelatinase A
Butler, G. S., Butler, M. J., Atkinson, S. J., Will, H., Tamura, T., van Westrum, S. M. S., Crabbe, T., Clements, J. M., d’Ortho, M., & Murphy, G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.2.871 · Cited by 573 · see citing works
Matrix metalloproteinase-9 (MMP-9) and its inhibitors in cancer: A minireview
Mondal, S., Adhikari, N., Banerjee, S., Amin, S. A., & Jha, T. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112260 · Cited by 566 · see citing works
Gelatinase B functions as regulator and effector in leukocyte biology
Opdenakker, G., Van den Steen, P. E., Dubois, B., Nelissen, I., Van Coillie, E., Masure, S., Proost, P., & Van Damme, J. (2001) · Journal of Leukocyte Biology · doi:10.1189/jlb.69.6.851 · Cited by 553 · see citing works
Metalloprotease-disintegrins: modular proteins capable of promoting cell-cell interactions and triggering signals by protein-ectodomain shedding
Schlöndorff, J. S., & Blobel, C. (1999) · Journal of Cell Science · doi:10.1242/jcs.112.21.3603 · Cited by 545 · see citing works
Structure of Human Pro-Matrix Metalloproteinase-2: Activation Mechanism Revealed
Morgunova, E. Y., Tuuttila, A., Bergmann, U., Isupov, M. N., Lindqvist, Y., Schneider, G., & Tryggvason, K. (1999) · Science · doi:10.1126/science.284.5420.1667 · Cited by 543 · see citing works
Inhibition of the Activities of Matrix Metalloproteinases 2, 8, and 9 by Chlorhexidine
Gendron, R., Grenier, D., Sorsa, T. A., & Mayrand, D. (1999) · Clinical and Diagnostic Laboratory Immunology · doi:10.1128/cdli.6.3.437-439.1999 · Cited by 540 · see citing works
Optimizing dentin bond durability: Control of collagen degradation by matrix metalloproteinases and cysteine cathepsins
Tjäderhane, L., Nascimento, F. D., Breschi, L., Mazzoni, A., Tersariol, I. L. S., Geraldeli, S., Tezvergil‐Mutluay, A., Carrilho, M., Carvalho, R. M., Tay, F. R., et al. (2012) · Dental Materials · doi:10.1016/j.dental.2012.08.004 · Cited by 539 · see citing works
Matrix Metalloproteinases Shape the Tumor Microenvironment in Cancer Progression
Niland, S., Riscanevo, A. X., & Eble, J. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010146 · Cited by 528 · see citing works
Zymographic Techniques for the Analysis of Matrix Metalloproteinases and their Inhibitors
Snoek, P. A. M., & den Hoff, J. W. V. (2005) · BioTechniques · doi:10.2144/05381rv01 · Cited by 526 · see citing works
Interaction of 92-kDa type IV collagenase with the tissue inhibitor of metalloproteinases prevents dimerization, complex formation with interstitial collagenase, and activation of the proenzyme with stromelysin.
Goldberg, G. I., Strongin, A. Y., Collier, I. E., Genrich, L., & Marmer, B. L. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42873-6 · Cited by 513 · see citing works
Targeting matrix metalloproteinases in cancer: Bringing new life to old ideas
Cathcart, J. M., Pulkoski‐Gross, A., & Cao, J. P. (2015) · Genes & Diseases · doi:10.1016/j.gendis.2014.12.002 · Cited by 511 · see citing works
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 · see citing works
Type IV collagenases in tumor invasion and metastasis
Stetler‐Stevenson, W. G. (1990) · Cancer and Metastasis Reviews · doi:10.1007/bf00049520 · Cited by 499 · see citing works
Overview of MMP-13 as a Promising Target for the Treatment of Osteoarthritis
Hu, Q., & Ecker, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22041742 · Cited by 491 · see citing works
Cloning and Characterization of ADAMTS11 , an Aggrecanase from the ADAMTS Family
Abbaszade, I. G., Liu, R., Yang, F., Rosenfeld, S. A., Ross, O. H., Link, J. R., Ellis, D. M., Tortorella, M. D., Pratta, M. A., Hollis, J. M., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.33.23443 · Cited by 490 · see citing works
Hypochlorous Acid Oxygenates the Cysteine Switch Domain of Pro-matrilysin (MMP-7)
Fu, X., Kassim, S. Y., Parks, W. C., & Heinecke, J. W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106958200 · Cited by 482 · see citing works
Matrix metalloproteinases: Fold and function of their catalytic domains
Tallant, C., Marrero, A., & Gomis‐Rüth, F. X. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2009.04.003 · Cited by 467 · see citing works
Activation of Matrix Metalloproteinases by Peroxynitrite-induced Protein S-Glutathiolation via Disulfide S-Oxide Formation
Okamoto, T., Akaike, T., Sawa, T., Miyamoto, Y., van der Vliet, A., & Maeda, H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102417200 · Cited by 466 · see citing works
Cooperative Catalysis with First‐Row Late Transition Metals
van der Vlugt, J. I. (2011) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.201100752 · Cited by 466 · see citing works
Matrix remodeling during endochondral ossification
Ortéga, N., Behonick, D. J., & Werb, Z. (2004) · Trends in Cell Biology · doi:10.1016/j.tcb.2003.12.003 · Cited by 463 · see citing works
Molecular aspects of tumor cell invasion and metastasis
Aznavoorian, S. A., Murphy, A. N., Stetler‐Stevenson, W. G., & Liotta, L. A. (1993) · Cancer · doi:10.1002/1097-0142(19930215)71:4 · Cited by 456 · see citing works
Production and localization of 92-kilodalton gelatinase in abdominal aortic aneurysms. An elastolytic metalloproteinase expressed by aneurysm-infiltrating macrophages.
Thompson, R. W., Holmes, D. R., Mertens, R. A., Liao, S., Botney, M. D., Mecham, R. P., Welgus, H. G., & Parks, W. C. (1995) · Journal of Clinical Investigation · doi:10.1172/jci118037 · Cited by 454 · see citing works
Matrix Metalloproteinases: Inflammatory Regulators of Cell Behaviors in Vascular Formation and Remodeling
Chen, Q., Jin, M., Yang, F., Zhu, J., Xiao, Q., & Zhang, L. (2013) · Mediators of Inflammation · doi:10.1155/2013/928315 · Cited by 444 · see citing works
Reactivation of inactivated endogenous proteolytic activities in phosphoric acid-etched dentine by etch-and-rinse adhesives
Mazzoni, A., Pashley, D. H., Nishitani, Y., Breschi, L., Mannello, F., Tjäderhane, L., Toledano, M., Pashley, E. L., & Tay, F. R. (2006) · Biomaterials · doi:10.1016/j.biomaterials.2006.01.040 · Cited by 431 · see citing works
Trendsin Molecular Medicine: Matrix metalloproteinases and their inhibitors in tumour growth and invasion
Kähäri, V., & Saarialho‐Kere, U. (1999) · Annals of Medicine · doi:10.3109/07853899909019260 · Cited by 407 · see citing works
The role of honey in the management of wounds
Molan, P. C. (1999) · Journal of Wound Care · doi:10.12968/jowc.1999.8.8.25904 · Cited by 403 · see citing works
Gelatinase B: a tuner and amplifier of immune functions
Opdenakker, G., den Steen, P. E. V., & Damme, J. V. (2001) · Trends in Immunology · doi:10.1016/s1471-4906(01)02023-3 · Cited by 398 · see citing works
The Transition Metal Coordination Chemistry of Hemilabile Ligands
Slone, C. S., Weinberger, D. A., & Mirkin, C. A. (1999) · Progress in inorganic chemistry · doi:10.1002/9780470166499.ch3 · Cited by 396 · see citing works
TIMP-2 Is Required for Efficient Activation of proMMP-2 in Vivo
Wang, Z., Jüttermann, R., & Soloway, P. D. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001270200 · Cited by 388 · see citing works
Matrix Metalloproteinase Inhibition Prevents Oxidative Stress-Associated Blood–Brain Barrier Disruption after Transient Focal Cerebral Ischemia
Gasche, Y., Copin, J., Sugawara, T., Fujimura, M., & Chan, P. H. (2001) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-200112000-00003 · Cited by 388 · see citing works
Regulation of matrix metalloproteinase activity in health and disease
Hadler‐Olsen, E., Fadnes, B., Sylte, I., Uhlin‐Hansen, L., & Winberg, J. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07920.x · Cited by 387 · see citing works
The Biochemical, Biological, and Pathological Kaleidoscope of Cell Surface Substrates Processed by Matrix Metalloproteinases
Cauwe, B., den Steen, P. E. V., & Opdenakker, G. (2007) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230701340019 · Cited by 384 · see citing works
Proteolytic Degradation of Amyloid -Protein
Saido, T., & Leissring, M. A. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006379 · Cited by 368 · see citing works
The role of matrix metalloproteases and their inhibitors in tumour invasion, metastasis and angiogenesis
Ray, J., & Stetler‐Stevenson, W. G. (1994) · European Respiratory Journal · doi:10.1183/09031936.94.07112062 · Cited by 360 · see citing works
Intracellular maturation and localization of the tumour necrosis factor α convertase (TACE)
Schlöndorff, J. S., Becherer, J. D., & Blobel, C. (2000) · Biochemical Journal · doi:10.1042/bj3470131 · Cited by 357 · see citing works
The possible role of matrix metalloproteinase (MMP)-2 and MMP-9 in cancer, e.g. acute leukemia
Klein, G., Vellenga, E., Fraaije, M. W., Kamps, W. A., & de Bont, E. S. J. M. (2004) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2003.09.001 · Cited by 354 · see citing works
The Role of Matrix Metalloproteinases in Wound Healing
Armstrong, D. G., & Jude, E. B. (2002) · Journal of the American Podiatric Medical Association · doi:10.7547/87507315-92-1-12 · Cited by 347 · see citing works
The paradox of matrix metalloproteinases in infectious disease
Elkington, P. T., O’Kane, C. M., & Friedland, J. S. (2005) · Clinical & Experimental Immunology · doi:10.1111/j.1365-2249.2005.02840.x · Cited by 343 · see citing works
Matrix metalloproteinases in tumor progression: focus on basal and squamous cell skin cancer
Kerkelä, E., & Saarialho‐Kere, U. (2003) · Experimental Dermatology · doi:10.1034/j.1600-0625.2003.120201.x · Cited by 343 · see citing works
Matrix Metalloproteinases as Regulators of Periodontal Inflammation
Cavalla, F., Hernández‐Ríos, P., Timo, S., Claudia, B., & Hernández, M. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18020440 · Cited by 342 · see citing works
Early appearance of activated matrix metalloproteinase-9 and blood–brain barrier disruption in mice after focal cerebral ischemia and reperfusion
Fujimura, M., Gasche, Y., Morita‐Fujimura, Y., Massengale, J. L., 川瀬, 誠., & Chan, P. H. (1999) · Brain Research · doi:10.1016/s0006-8993(99)01843-0 · Cited by 339 · see citing works
Structural aspects of the metzincin clan of metalloendopeptidases
Gomis‐Rüth, F. X. (2003) · Molecular Biotechnology · doi:10.1385/mb:24:2:157 · Cited by 339 · see citing works
Potential of Honey in the Treatment of Wounds and Burns
Molan, P. C. (2001) · American Journal of Clinical Dermatology · doi:10.2165/00128071-200102010-00003 · Cited by 333 · see citing works
Comprehensive review of mechanisms of pathogenesis involved in Alzheimer’s disease and potential therapeutic strategies
Sharma, P., Srivastava, P., Seth, A., Tripathi, P. N., Banerjee, A. G., & Shrivastava, S. K. (2019) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.12.006 · Cited by 331 · see citing works
Matrix metalloproteinases in destructive pulmonary pathology
Elkington, P. T. (2005) · Thorax · doi:10.1136/thx.2005.051979 · Cited by 331 · see citing works
Effect of matrix metalloproteinases activity on outflow in perfused human organ culture.
Bradley, J. M., Vranka, J. A., Colvis, C. M., Conger, D. M., Alexander, J. P., Fisk, A. S., Samples, J. R., & Acott, T. S. (1998) · PubMed · Cited by 328 · see citing works
Structural properties of matrix metalloproteinases
Bode, W., Fernandez-Catalan, C., Tschesche, F. G. H., & H. Nagase, K. M. (1999) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050320 · Cited by 328 · see citing works
Collagenases in cancer
Ala‐aho, R., & Kähäri, V. (2005) · Biochimie · doi:10.1016/j.biochi.2004.12.009 · Cited by 328 · see citing works
Molecular mechanisms triggered by mercury
Guzzi, G., & Porta, C. A. M. L. (2007) · Toxicology · doi:10.1016/j.tox.2007.11.002 · Cited by 315 · see citing works

Unconventional Activation Mechanisms of MMP-26, a Human Matrix Metalloproteinase with a Unique PHCG XXD Cysteine-switch Motif
Marchenko, N. D., Marchenko, G. N., & Strongin, A. Y. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201197200 · Cited by 47 · see citing works
Molecular Structures and Dynamics of the Stepwise Activation Mechanism of a Matrix Metalloproteinase Zymogen: Challenging the Cysteine Switch Dogma
Rosenblum, G., Meroueh, S. O., Tóth, M., Fisher, J. F., Fridman, R. A., Mobashery, S., & Sagi, I. (2007) · Journal of the American Chemical Society · doi:10.1021/ja073941l · Cited by 89 · see citing works
Structure of Human Pro-Matrix Metalloproteinase-2: Activation Mechanism Revealed
Morgunova, E. Y., Tuuttila, A., Bergmann, U., Isupov, M. N., Lindqvist, Y., Schneider, G., & Tryggvason, K. (1999) · Science · doi:10.1126/science.284.5420.1667 · Cited by 543 · see citing works
Insight into the Complex and Dynamic Process of Activation of Matrix Metalloproteinases
Kotra, L. P., Cross, J. B., Shimura, Y., Fridman, R. A., Schlegel, H. B., & Mobashery, S. (2001) · Journal of the American Chemical Society · doi:10.1021/ja001896a · Cited by 29 · see citing works
Cysteine Switch
(2001) · Springer eBooks · doi:10.1007/3-540-30683-8_396

Authors: Van Wart, H. E., & Birkedal-Hansen, H.
Affiliations: Department of Chemistry, Florida State University, Tallahassee 32306-3015.
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 1990-07
Volume: 87
Issue: 14
Pages: 5578-5582
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.87.14.5578
PMC: PMC54368
OpenAlex: W2167709602
Cited by: 1,475
References: 51
Citations by year: 2026: 23 · 2025: 28 · 2024: 38 · 2023: 28 · 2022: 34 · 2021: 31 · 2020: 30 · 2019: 28 · 2018: 40 · 2017: 48 · 2016: 33 · 2015: 47 · 2014: 60 · 2013: 45 · 2012: 61
FWCI: 14.57
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r01de006028-07, 5r01de009122-05, 5r01gm027939-15)
National Institute of General Medical Sciences (GM-27939)
National Institute of Dental and Craniofacial Research (DE06028, DE09122)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
Health Sciences › Medicine › Hematology › Blood Coagulation and Thrombosis Mechanisms
Health Sciences › Medicine › Oncology › Peptidase Inhibition and Analysis
Keywords: matrix metalloproteinases, enzyme activation, latent collagenase, zinc binding site, conserved amino acid sequence
MeSH terms: Amino Acid Sequence, Animals, Microbial Collagenase, Cysteine, Multigene Family, Humans, Metalloendopeptidases, Molecular Sequence Data, Protein Binding, Rabbits, Sequence Homology, Nucleic Acid, Species Specificity, Zinc, Rats

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family.

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Cites

Cited by

Related

Record

About these checks