PublisherDOIYearVolumeIssuePageTitleAuthor(s)Link
Lung Cancer10.1016/0169-5002(94)93857-119941122TIMP 1 gene expression in resected lung cancerK.M. Fong, P.V. Zimmerman, P.J. Smithhttps://api.elsevier.com/content/article/PII:0169500294938571?httpAccept=text/xml, https://api.elsevier.com/content/article/PII:0169500294938571?httpAccept=text/plain
Acta Neurochirurgica10.1007/s00701-006-0929-820061492179-183Expression of matrix metalloproteinases (MMPs) and tissue inhibitor of metalloproteinase (TIMP) in cerebral cavernous malformations: immunohistochemical analysis of MMP-2, -9 and TIMP-2M. Fujimura, M. Watanabe, H. Shimizu, T. Tominagahttp://link.springer.com/content/pdf/10.1007/s00701-006-0929-8.pdf, http://link.springer.com/article/10.1007/s00701-006-0929-8/fulltext.html, http://link.springer.com/content/pdf/10.1007/s00701-006-0929-8
Hepatology10.1016/0270-9139(95)95202-01995224A370High TIMP-1 expression results in altered cell motility: Possible role of TIMP-1 in liver fibrosis . Med. Klinik III, RWTH Aachen, 52057 Aachen, *I. Med. Klinik, Univ. Mainz, 55101 Mainz, Germanyhttps://api.elsevier.com/content/article/PII:0270-9139(95)95202-0?httpAccept=text/xml, https://api.elsevier.com/content/article/PII:0270-9139(95)95202-0?httpAccept=text/plain
Molecular Therapy10.1016/s1525-0016(16)41184-6200375S287742. Over-Expression of TIMP-3 Causes Apoptosis in Lung Cancer Cellshttps://api.elsevier.com/content/article/PII:S1525001616411846?httpAccept=text/xml, https://api.elsevier.com/content/article/PII:S1525001616411846?httpAccept=text/plain
Biophysical Journal10.1529/biophysj.106.08407920069193465-3473Laser-Guided Assembly of Heterotypic Three-Dimensional Living Cell MicroarraysG.M. Akselrod, W. Timp, U. Mirsaidov, Q. Zhao, C. Li, R. Timp, K. Timp, P. Matsudaira, G. Timphttps://api.elsevier.com/content/article/PII:S0006349506720586?httpAccept=text/xml, https://api.elsevier.com/content/article/PII:S0006349506720586?httpAccept=text/plain
Kidney and Blood Pressure Research10.1159/0004434312016413288-297Urinary Metalloproteinases-9 and -2 and Their Inhibitors TIMP-1 and TIMP-2 are Markers of Early and Long-Term Graft Function After Renal TransplantationEwa Kwiatkowska, Leszek Domanski, Joanna Bober, Krzysztof Safranow, Maciej Romanowski, Andrzej Pawlik, Sebastian Kwiatkowski, Kazimierz Ciechanowskihttps://www.karger.com/Article/Pdf/443431, http://www.karger.com/Article/Pdf/443431
Kidney International10.1046/j.1523-1755.2003.00825.x20036331012-1020Homocysteine enhances TIMP-1 expression and cell proliferation associated with NADH oxidase in rat mesangial cellsZhi-Zhang Yang, Ai-Ping Zouhttps://api.elsevier.com/content/article/PII:S0085253815489690?httpAccept=text/xml, https://api.elsevier.com/content/article/PII:S0085253815489690?httpAccept=text/plain
Mycoses10.1111/j.1439-0507.2010.01889.x2010544325-330The effects of Candida proteinases on human proMMP-9, TIMP-1 and TIMP-2Pirjo Pärnänen, Jukka H. Meurman, Timo Sorsahttps://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1439-0507.2010.01889.x, http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1439-0507.2010.01889.x/fullpdf
Kidney International10.1046/j.1523-1755.2000.00274.x20005831186-1201TIMP-1 gene expression and PAI-1 antigen after unilateral ureteral obstruction in the adult male ratCarla Duymelinck, Simonne E.H. Dauwe, Kathleen E.J. De Greef, Dirk K. Ysebaert, Gert A. Verpooten, Marc E. De Broehttps://api.elsevier.com/content/article/PII:S0085253815472084?httpAccept=text/xml, https://api.elsevier.com/content/article/PII:S0085253815472084?httpAccept=text/plain
Developmental Dynamics10.1002/aja.100202040819952024388-39692-kDa type IV collagenase and TIMP-3, but not 72-kDa type IV collagenase or TIMP-1 or TIMP-2, are highly expressed during mouse embryo implantationPaula Reponen, Ilmo Leivo, Carin Sahlberg, Suneel S. Apte, Irma Thesleff, Björn R. Olsen, Karl Tryggvasonhttps://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Faja.1002020408, https://onlinelibrary.wiley.com/doi/full/10.1002/aja.1002020408