Zymography methods for visualizing hydrolytic enzymes

Increased expression of matrix metalloproteinases and matrix degrading activity in vulnerable regions of human atherosclerotic plaques.

Galis, Z. S., Sukhova, G. K., Lark, M. W., & Libby, P. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117619 · Cited by 2,539

Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates

Heussen, C., & Dowdle, E. B. (1980) · Analytical Biochemistry · doi:10.1016/0003-2697(80)90338-3 · Cited by 1,973

In vivo imaging of tumors with protease-activated near-infrared fluorescent probes

Weissleder, R., Tung, C.-H., Mahmood, U., & Bogdanov, A. (1999) · Nature Biotechnology · doi:10.1038/7933 · Cited by 1,591

COLLAGENOLYTIC ACTIVITY IN AMPHIBIAN TISSUES: A TISSUE CULTURE ASSAY

Gross, J., & Lapiere, C. M. (1962) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.48.6.1014 · Cited by 1,310

Serpin Structure, Mechanism, and Function

Gettins, P. G. W. (2002) · Chemical Reviews · doi:10.1021/cr010170+ · Cited by 1,226

Biochemistry and Molecular Biology of Gelatinase B or Matrix Metalloproteinase-9 (MMP-9)

Van den Steen, P. E., Dubois, B., Nelissen, I., Rudd, P. M., Dwek, R. A., & Opdenakker, G. (2002) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230290771546 · Cited by 946

Quantitative Zymography: Detection of Picogram Quantities of Gelatinases

Kleiner, D. E., & Stetlerstevenson, W. G. (1994) · Analytical Biochemistry · doi:10.1006/abio.1994.1186 · Cited by 861

A study of proteases and protease-inhibitor complexes in biological fluids

Granelli-Piperno, A., & Reich, E. (1978) · The Journal of Experimental Medicine · doi:10.1084/jem.148.1.223 · Cited by 803

Matrix metalloproteinase inhibitors as therapy for inflammatory and vascular diseases

Hu, J., Van den Steen, P. E., Sang, Q.-X. A., & Opdenakker, G. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2308 · Cited by 795

In vivo molecular target assessment of matrix metalloproteinase inhibition

Bremer, C., Tung, C.-H., & Weissleder, R. (2001) · Nature Medicine · doi:10.1038/89126 · Cited by 726

Protease degradomics: A new challenge for proteomics

López-Otín, C., & Overall, C. M. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm858 · Cited by 664

Biochemical and immunological characterization of the secreted forms of human neutrophil gelatinase.

Hibbs, M. S., Hasty, K. A., Seyer, J. M., Kang, A. H., & Mainardi, C. L. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)89580-1 · Cited by 613

Dystroglycan is selectively cleaved at the parenchymal basement membrane at sites of leukocyte extravasation in experimental autoimmune encephalomyelitis

Agrawal, S., Anderson, P., Durbeej, M., van Rooijen, N., Ivars, F., Opdenakker, G., & Sorokin, L. M. (2006) · The Journal of Experimental Medicine · doi:10.1084/jem.20051342 · Cited by 559

Zymographic Techniques for the Analysis of Matrix Metalloproteinases and their Inhibitors

Snoek-van Beurden, P. A. M., & Von den Hoff, J. W. (2005) · BioTechniques · doi:10.2144/05381rv01 · Cited by 523

Activity-based probes for the proteomic profiling of metalloproteases

Saghatelian, A., Jessani, N., Joseph, A., Humphrey, M., & Cravatt, B. F. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402784101 · Cited by 456

Proteome-derived, database-searchable peptide libraries for identifying protease cleavage sites

Schilling, O., & Overall, C. M. (2008) · Nature Biotechnology · doi:10.1038/nbt1408 · Cited by 401

Matrix metalloprotease 2 (MMP-2) and matrix metalloprotease 9 (MMP-9) type IV collagenases in colorectal cancer.

Liabakk, N., Talbot, I. C., Smith, R. A., Wilkinson, K., & Balkwill, F. R. (1996) · PubMed · Cited by 322

α 2 -macroglobulin: an evolutionarily conserved arm of the innate immune system

Armstrong, P. B., & Quigley, J. P. (1999) · Developmental & Comparative Immunology · doi:10.1016/s0145-305x(99)00018-x · Cited by 305

Intracellular substrate cleavage: a novel dimension in the biochemistry, biology and pathology of matrix metalloproteinases

Cauwe, B., & Opdenakker, G. (2010) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2010.501783 · Cited by 299

Microscopic localization of active proteases by in situ zymography: detection of matrix metalloproteinase activity in vascular tissue

Calis, Z. S., Sukhova, G. K., & Libby, P. (1995) · The FASEB Journal · doi:10.1096/fasebj.9.10.7615167 · Cited by 278

Matrix Metalloproteinase-9/Gelatinase B Is Required for Process Outgrowth by Oligodendrocytes

Oh, L. Y. S., Larsen, P. H., Krekoski, C. A., Edwards, D. R., Donovan, F., Werb, Z., & Yong, V. W. (1999) · The Journal of Neuroscience · doi:10.1523/jneurosci.19-19-08464.1999 · Cited by 267

Purification and identification of 91‐kDa neutrophil gelatinase: Release by the activating peptide interleukin‐8

MASURE, S., PROOST, P., VAN DAMME, J., & OPDENAKKER, G. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb16027.x · Cited by 254

Proteomics Discovery of Metalloproteinase Substrates in the Cellular Context by iTRAQ™ Labeling Reveals a Diverse MMP-2 Substrate Degradome

Dean, R. A., & Overall, C. M. (2007) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m600341-mcp200 · Cited by 240

Potent and Selective Mechanism-Based Inhibition of Gelatinases

Brown, S., Bernardo, M. M., Li, Z.-H., Kotra, L. P., Tanaka, Y., Fridman, R., & Mobashery, S. (2000) · Journal of the American Chemical Society · doi:10.1021/ja001461n · Cited by 197

The Hemopexin and O-Glycosylated Domains Tune Gelatinase B/MMP-9 Bioavailability via Inhibition and Binding to Cargo Receptors

Van den Steen, P. E., Van Aelst, I., Hvidberg, V., Piccard, H., Fiten, P., Jacobsen, C., Moestrup, S. K., Fry, S., Royle, L., Wormald, M. R., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512308200 · Cited by 189

Matrix metalloproteinase activity assays: Importance of zymography

Kupai, K., Szűcs, G., Cseh, S., et al. (2010) · Journal of Pharmacological and Toxicological Methods · doi:10.1016/j.vascn.2010.02.011 · Cited by 180

Matrix Metalloproteinase-9 Promotes Chronic Lymphocytic Leukemia B Cell Survival through Its Hemopexin Domain

Redondo-Muñóz, J., Ugarte-Berzal, E., Terol, M. J., den Steen, P. E. V., del Cerro, M. H., Roderfeld, M., Roeb, E., Opdenakker, G., Garcia-Marco, J. A., & Garcı́a-Pardo, A. (2010) · Cancer Cell · doi:10.1016/j.ccr.2009.12.044 · Cited by 167

Quantitative Reverse Zymography: Analysis of Picogram Amounts of Metalloproteinase Inhibitors Using Gelatinase A and B Reverse Zymograms

Oliver, G. W., Leferson, J. D., Stetler‐Stevenson, W. G., & Kleiner, D. E. (1997) · Analytical Biochemistry · doi:10.1006/abio.1996.9895 · Cited by 165

Phase I study of intrapleural batimastat (BB-94), a matrix metalloproteinase inhibitor, in the treatment of malignant pleural effusions.

Macaulay, V. M., O'Byrne, K. J., Saunders, M. P., et al. (1999) · PubMed · Cited by 161

Purification and characterization of an elastinolytic proteinase secreted by cercariae of Schistosoma mansoni.

McKerrow, J. H., Pino-Heiss, S., Lindquist, R. N., & Werb, Z. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)83680-3 · Cited by 151

Increased expression of epidermal fatty acid binding protein, cofilin, and 14-3-3-σ (stratifin) detected by two-dimensional gel electrophoresis, mass spectrometry and microsequencing of drug-resistant human adenocarcinoma of the pancreas

Sinha, P. K., Hütter, G., Köttgen, E., Dietel, M., Schadendorf, D., & Lage, H. (1999) · Electrophoresis · doi:10.1002/(sici)1522-2683(19991001)20:14<2824::aid-elps2824>3.0.co;2-h · Cited by 147

Matrix Metalloproteinase-9 in an Exploratory Trial of Intravenous Minocycline for Acute Ischemic Stroke

Switzer, J. A., Hess, D. C., Ergul, A., Waller, J. L., Machado, L. S., Portik‐Dobos, V., Pettigrew, L. C., Clark, W. M., & Fagan, S. C. (2011) · Stroke · doi:10.1161/strokeaha.111.618215 · Cited by 142

The inhibition of tissue acid proteinases by pepstatin

Barrett, A. J., & Dingle, J. T. (1972) · Biochemical Journal · doi:10.1042/bj1270439 · Cited by 139

Protease degradomics: mass spectrometry discovery of protease substrates and the CLIP-CHIP, a dedicated DNA microarray of all human proteases and inhibitors

Overall, C. M., Tam, E. M., Kappelhoff, R., Connor, A., Ewart, T., Morrison, C. J., Puente, X. S., López-Otín, C., & Seth, A. K. (2004) · Biological Chemistry · doi:10.1515/bc.2004.058 · Cited by 130

Collagen Zymography as a Sensitive and Specific Technique for the Determination of Subpicogram Levels of Interstitial Collagenase

Gogly, B., Groult, N., Hornebeck, W., et al. (1998) · Analytical Biochemistry · doi:10.1006/abio.1997.2318 · Cited by 111

HIV-1 gp120-Induced Injury to the Blood-Brain Barrier: Role of Metalloproteinases 2 and 9 and Relationship to Oxidative Stress

Louboutin, J., Agrawal, L., Reyes, B. A. S., Bockstaele, E. J. V., & Strayer, D. S. (2010) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181e8c96f · Cited by 109

The gelatinase inhibitory activity of tetracyclines and chemically modified tetracycline analogues as measured by a novel microtiter assay for inhibitors

Paemen, L. R., Martens, E., Norga, K., Masure, S., Roets, E., Hoogmartens, J., & Opdenakker, G. (1996) · Biochemical Pharmacology · doi:10.1016/0006-2952(96)00168-2 · Cited by 107

Whole-Body Optical Imaging in Animal Models to Assess Cancer Development and Progression

Kaijzel, E. L., van der Pluijm, G., & Löwik, C. W. G. M. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-07-0402 · Cited by 107

Comparison, Characterization, and Identification of Proteases and Protease Inhibitors in Epididymal Fluids of Domestic Mammals. Matrix Metalloproteinases Are Major Fluid Gelatinases1

Métayer, S., Dacheux, F., Dacheux, J. L., et al. (2002) · Biology of Reproduction · doi:10.1095/biolreprod66.5.1219 · Cited by 100

Optical Imaging of Matrix Metalloproteinase-7 Activity in Vivo Using a Proteolytic Nanobeacon

Scherer, R. L., VanSaun, M. N., McIntyre, J. O., & Matrisian, L. M. (2008) · Molecular Imaging · doi:10.2310/7290.2008.00010 · Cited by 93

Advanced glycation end products cause collagen II reduction by activating Janus kinase/signal transducer and activator of transcription 3 pathway in porcine chondrocytes

Huang, C., Lai, K.-Y., Hung, L., Wu, W.-L., Liu, F., & Ho, L. (2011) · Rheumatology · doi:10.1093/rheumatology/ker134 · Cited by 82

Matrix metalloproteinases, tissue inhibitors of MMPs and TACE in experimental cerebral malaria

den Steen, P. E. V., Aelst, I. V., Starckx, S., Maskos, K., Opdenakker, G., & Pagenstecher, A. (2006) · Laboratory Investigation · doi:10.1038/labinvest.3700454 · Cited by 78

Gelatin degradation assay reveals MMP-9 inhibitors and function of O-glycosylated domain

Vandooren, J., Geurts, N., Martens, E., den Steen, P. E. V., Jonghe, S. D., Herdewijn, P., & Opdenakker, G. (2011) · World Journal of Biological Chemistry · doi:10.4331/wjbc.v2.i1.14 · Cited by 77

Evaluation of gelatinases and IL‐6 in the cerebrospinal fluid of patients with optic neuritis, multiple sclerosis and other inflammatory neurological diseases

Paemen, L. R., Olsson, T. P., Söderström, M. B., Damme, J. V., & Opdenakker, G. (1994) · European Journal of Neurology · doi:10.1111/j.1468-1331.1994.tb00051.x · Cited by 73

Human hepatoma cells produce an 85 kDa gelatinase regulated by phorbol 12-myristate 13-acetate

Masure, S., Billiau, A., Damme, J. V., & Opdenakker, G. (1990) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(90)90103-k · Cited by 72

Real-Time Zymography and Reverse Zymography: A Method for Detecting Activities of Matrix Metalloproteinases and Their Inhibitors Using FITC-Labeled Collagen and Casein as Substrates

Hattori, S., Fujisaki, H., Kiriyama, T., Yokoyama, T., & Irie, S. (2002) · Analytical Biochemistry · doi:10.1006/abio.2001.5479 · Cited by 68

In Situ Zymography: A Molecular Pathology Technique to Localize Endogenous Protease Activity in Tissue Sections

Yan, S. J., & Blomme, E. A. G. (2003) · Veterinary Pathology · doi:10.1354/vp.40-3-227 · Cited by 66

Urinary type IV collagenase: elevated levels are associated with bladder transitional cell carcinoma.

Margulies, I., Höyhtyä, M., Evans, C., et al. (1993) · PubMed · Cited by 66

A versatile assay for gelatinases using succinylated gelatin

Baragi, V. M., Shaw, B. J., Renkiewicz, R. R., Kuipers, P. J., Welgus, H. G., Mathrubutham, M., Cohen, J. R., & Rao, S. K. (2000) · Matrix Biology · doi:10.1016/s0945-053x(00)00086-x · Cited by 56

Detection of proteases by clotting of casein after gel electrophoresis

Foltmann, B., Szecsi, P. B., & Tarasova, N. I. (1985) · Analytical Biochemistry · doi:10.1016/0003-2697(85)90551-2 · Cited by 56

Effects of Blood Collection Methods on Gelatin Zymography of Matrix Metalloproteinases

Mannello, F. (2003) · Clinical Chemistry · doi:10.1373/49.2.339 · Cited by 56

Analysis of Gelatinases in Complex Biological Fluids and Tissue Extracts

Descamps, F. J., Martens, E., & Opdenakker, G. (2002) · Laboratory Investigation · doi:10.1097/01.lab.0000038556.54069.73 · Cited by 55

Role of matrix metalloproteinase‐9 (MMP‐9) in striatal blood–brain barrier disruption in a 3‐nitropropionic acid model of Huntington's disease

Duran‐Vilaregut, J., del Valle, J., Manich, G., Camins, A., Pallàs, M., Vilaplana, J., & Pelegrí, C. (2010) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2010.01157.x · Cited by 54

Consistent Alterations of Circulating Matrix Metalloproteinases Levels in Untreated Hypertensives and in Spontaneously Hypertensive Rats: A Relevant Pharmacological Target

Fontana, V., Silva, P. S., Belo, V. D. A., Antonio, R. C., Ceron, C. S., Biagi, C., Gerlach, R. F., & Tanus-Santos, J. E. (2011) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/j.1742-7843.2011.00698.x · Cited by 53

Inhibition of gelatinolytic activity in tumor tissues by synthetic matrix metalloproteinase inhibitor: application of film in situ zymography.

Ikeda, M., Maekawa, R., Tanaka, H., Matsumoto, M., Takeda, Y., Tamura, Y., Nemori, R., & Yoshioka, T. (2000) · PubMed · Cited by 52

The Zebrafish Embryo: A Powerful Model System for Investigating Matrix Remodeling

Wyatt, R. A., Keow, J. Y., Harris, N. D., Haché, C. A., Li, D. H., & Crawford, B. D. (2009) · Zebrafish · doi:10.1089/zeb.2009.0609 · Cited by 51

Increased cellular iron levels affect matrix metalloproteinase expression and phagocytosis in activated microglia

Mairuae, N., Connor, J. R., & Cheepsunthorn, P. (2011) · Neuroscience Letters · doi:10.1016/j.neulet.2011.06.001 · Cited by 47

Expression of Genes Encoding Extracellular Matrix Macromolecules and Metalloproteinases in Avian Tibial Dyschondroplasia

Velada, I., Silva, F. C. E., Reis, F., Pires, E., Egas, C., Rodrigues‐Santos, P., & Barros, M. (2011) · Journal of Comparative Pathology · doi:10.1016/j.jcpa.2010.12.008 · Cited by 45

Ontogeny and regulation of matrix metalloproteinase activity in the zebrafish embryo by in vitro and in vivo zymography

Crawford, B. D., & Pilgrim, D. B. (2005) · Developmental Biology · doi:10.1016/j.ydbio.2005.06.035 · Cited by 39

Inhibitory effects of GL-V9 on the invasion of human breast carcinoma cells by downregulating the expression and activity of matrix metalloproteinase-2/9

Li, L., Chen, P., Ling, Y., et al. (2011) · European Journal of Pharmaceutical Sciences · doi:10.1016/j.ejps.2011.06.001 · Cited by 39

Electrophoretic transfer protein zymography

Pan, D., Hill, A. P., Kashou, A. H., et al. (2011) · Analytical Biochemistry · doi:10.1016/j.ab.2011.01.015 · Cited by 37

Quantitative Enzyme Activity Determination with Zeptomole Sensitivity by Microfluidic Gradient-Gel Zymography

Hughes, A. J., & Herr, A. E. (2010) · Analytical Chemistry · doi:10.1021/ac100201z · Cited by 36

Natural substrates of plant proteases: how can protease degradomics extend our knowledge?

Tsiatsiani, L., Gevaert, K., & Breusegem, F. V. (2011) · Physiologia Plantarum · doi:10.1111/j.1399-3054.2011.01534.x · Cited by 35

Interleukin-lβ Induces Migration of Rat Arterial Smooth Muscle Cells Through a Mechanism Involving Increased Matrix Metalloproteinase-2 Activity

Wang, Z., Kong, L., Kang, J. X., Vaughn, D. M., Bush, G. D., Walding, A. L., Grigorian, A. A., Robinson, J. S., & Nakayama, D. K. (2010) · Journal of Surgical Research · doi:10.1016/j.jss.2009.12.010 · Cited by 35

Differential regulation of gelatinase b and tissue‐type plasminogen activator expression in human bowes melanoma cells

Houde, M., Bruyne, G. D., Bracke, M., Ingelman‐Sundberg, M., Skoglund, G., Masure, S., Damme, J. V., & Opdenakker, G. (1993) · International Journal of Cancer · doi:10.1002/ijc.2910530309 · Cited by 30

Casein Zymography of Calpains Using a 4-(2-Hydroxyethyl)-1-piperazineethanesulfonic acid–Imidazole Buffer

Croall, D. E., Moffett, K., & Hatch, H. (2002) · Analytical Biochemistry · doi:10.1006/abio.2001.5606 · Cited by 29

DFT Studies of the Ring-Opening Mechanism of SB-3CT, a Potent Inhibitor of Matrix Metalloproteinase 2

Tao, P., Fisher, J. F., Mobashery, S., & Schlegel, H. B. (2009) · Organic Letters · doi:10.1021/ol9008393 · Cited by 26

2-D zymographic analysis of Broccoli (Brassica oleracea L. var. Italica) florets proteases: Follow up of cysteine protease isotypes in the course of post-harvest senescence

Rossano, R., Larocca, M., & Riccio, P. (2011) · Journal of Plant Physiology · doi:10.1016/j.jplph.2011.02.013 · Cited by 22

Effect of the plasminogen-plasmin system on hypertensive renal and cardiac damage

Knier, B., Cordasic, N., Klanke, B., Heusinger‐Ribeiro, J., Daniel, C., Veelken, R. A., Hartner, A., & Hilgers, K. F. (2011) · Journal of Hypertension · doi:10.1097/hjh.0b013e32834840e8 · Cited by 22

Differential in vivo zymography: A method for observing matrix metalloproteinase activity in the zebrafish embryo

Keow, J. Y., Herrmann, K. M., & Crawford, B. D. (2011) · Matrix Biology · doi:10.1016/j.matbio.2011.01.003 · Cited by 20

Silicate Increases the Release of MMP-9 Forms in Peripheral Blood: Why Gelatin Zymography Differs Significantly in Citrate Plasma and Serum Obtained with or without Clot Activators

Mannello, F., Tonti, G. A., Tanus-Santos, J. E., & Gerlach, R. F. (2007) · Clinical Chemistry · doi:10.1373/clinchem.2007.090548 · Cited by 19

Activity-Based Labeling of Matrix Metalloproteinases in Living Vertebrate Embryos

Keow, J. Y., Pond, E. D., Cisar, J. S., Cravatt, B. F., & Crawford, B. D. (2012) · PLoS ONE · doi:10.1371/journal.pone.0043434 · Cited by 19

“Reverse degradomics”, monitoring of proteolytic trimming by multi‐CE and confocal detection of fluorescent substrates and reaction products

Piccard, H., Hu, J., Fiten, P., Proost, P., Martens, E., den Steen, P. E. V., Damme, J. V., & Opdenakker, G. (2009) · Electrophoresis · doi:10.1002/elps.200800698 · Cited by 12

One- and two-dimensional SDS–PAGE zymography with quenched fluorogenic substrates provides identification of biological fluid proteases by direct mass spectrometry

Thimon, V., Belghazi, M., Labas, V., Dacheux, J., & Gatti, J. (2007) · Analytical Biochemistry · doi:10.1016/j.ab.2007.12.026 · Cited by 10

Kinetics of inhibition of purified bovine neutrophil matrix metalloproteinase 9 by low–molecular-weight inhibitors

Bannikov, G. A., Lakritz, J., Premanandan, C., Mattoon, J. S., & Abrahamsen, E. J. (2009) · American Journal of Veterinary Research · doi:10.2460/ajvr.70.5.633 · Cited by 4

Rapid endothelial cytoskeletal reorganization enables early blood–brain barrier disruption and long-term ischaemic reperfusion brain injury

Shi, Y., Zhang, L., Pu, H., Mao, L., Hu, X., Jiang, X., Xu, N., Stetler, R. A., Zhang, F., Liu, X., et al. (2016) · Nature Communications · doi:10.1038/ncomms10523 · Cited by 431

Enterotoxigenic Escherichia coli secretes a highly conserved mucin-degrading metalloprotease to effectively engage intestinal epithelial cells

Luo, Q., Kumar, P., Vickers, T. J., Sheikh, A., Lewis, W. G., Rasko, D. A., Sistrunk, J., & Fleckenstein, J. M. (2014) · Infection and Immunity · doi:10.1128/iai.01106-13 · Cited by 139

Accelerated migration and invasion of prostate cancer cells after a photodynamic therapy-like challenge: Role of nitric oxide

Fahey, J. M., & Girotti, A. W. (2015) · Nitric Oxide · doi:10.1016/j.niox.2015.05.006 · Cited by 77

Antagonistic Effects of Endogenous Nitric Oxide in a Glioblastoma Photodynamic Therapy Model

Fahey, J. M., Emmer, J. V., Korytowski, W., Hogg, N., & Girotti, A. W. (2016) · Photochemistry and Photobiology · doi:10.1111/php.12636 · Cited by 49

Physiological fibrin hydrogel modulates immune cells and molecules and accelerates mouse skin wound healing

Pereira, R. V. S., EzEldeen, M., Ugarte-Berzal, E., Martens, E., Malengier-Devlies, B., Vandooren, J., Vranckx, J. J., Matthys, P., & Opdenakker, G. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1170153 · Cited by 48