| Year |
Citation |
Score |
| 2022 |
Bienstein M, Minond D, Schwaneberg U, Davari MD, Yildiz D. In Silico and Experimental ADAM17 Kinetic Modeling as Basis for Future Screening System for Modulators. International Journal of Molecular Sciences. 23. PMID 35163294 DOI: 10.3390/ijms23031368 |
0.38 |
|
| 2021 |
Wang C, Diez J, Park H, Spicer TP, Scampavia LD, Becker-Pauly C, Fields GB, Minond D, Bannister TD. Discovery and Optimization of Selective Inhibitors of Meprin α (Part II). Pharmaceuticals (Basel, Switzerland). 14. PMID 33673639 DOI: 10.3390/ph14030197 |
0.565 |
|
| 2021 |
Hou S, Diez J, Wang C, Becker-Pauly C, Fields GB, Bannister T, Spicer TP, Scampavia LD, Minond D. Discovery and Optimization of Selective Inhibitors of Meprin α (Part I). Pharmaceuticals (Basel, Switzerland). 14. PMID 33671080 DOI: 10.3390/ph14030203 |
0.551 |
|
| 2019 |
Palrasu M, Knapinska AM, Diez J, Smith L, LaVoi T, Giulianotti M, Houghten RA, Fields GB, Minond D. A Novel Probe for Spliceosomal Proteins that Induces Autophagy and Death of Melanoma Cells Reveals New Targets for Melanoma Drug Discovery. Cellular Physiology and Biochemistry : International Journal of Experimental Cellular Physiology, Biochemistry, and Pharmacology. 53: 656-686. PMID 31573152 DOI: 10.33594/000000164 |
0.472 |
|
| 2017 |
Schaal JB, Tran DQ, Subramanian A, Patel R, Laragione T, Roberts KD, Trinh K, Tongaonkar P, Tran PA, Minond D, Fields GB, Beringer P, Ouellette AJ, Gulko PS, Selsted ME. Suppression and resolution of autoimmune arthritis by rhesus θ-defensin-1, an immunomodulatory macrocyclic peptide. Plos One. 12: e0187868. PMID 29145473 DOI: 10.1371/Journal.Pone.0187868 |
0.544 |
|
| 2017 |
Amar S, Minond D, Fields GB. Clinical implications of compounds designed to inhibit ECM-modifying metalloproteinases. Proteomics. PMID 28613012 DOI: 10.1002/Pmic.201600389 |
0.626 |
|
| 2016 |
Madoux F, Dreymuller D, Pettiloud JP, Santos R, Becker-Pauly C, Ludwig A, Fields GB, Bannister T, Spicer TP, Cudic M, Scampavia LD, Minond D. Discovery of an enzyme and substrate selective inhibitor of ADAM10 using an exosite-binding glycosylated substrate. Scientific Reports. 6: 11. PMID 28442704 DOI: 10.1038/S41598-016-0013-4 |
0.648 |
|
| 2016 |
Madoux F, Dreymuller D, Pettiloud JP, Santos R, Becker-Pauly C, Ludwig A, Fields GB, Bannister T, Spicer TP, Cudic M, Scampavia LD, Minond D. Discovery of an enzyme and substrate selective inhibitor of ADAM10 using an exosite-binding glycosylated substrate. Scientific Reports. 6: 11. PMID 27920432 DOI: 10.1038/s41598-016-0013-4 |
0.617 |
|
| 2016 |
Moss ML, Minond D, Yoneyama T, Hansen HP, Vujanovic N, Rasmussen FH. An improved fluorescent substrate for assaying soluble and membrane associated ADAM family member activities. Analytical Biochemistry. PMID 27177841 DOI: 10.1016/J.Ab.2016.05.001 |
0.382 |
|
| 2015 |
Jeedimalla N, Flint M, Smith L, Haces A, Minond D, Roche SP. Multicomponent assembly of 4-aza-podophyllotoxins: A fast entry to highly selective and potent anti-leukemic agents. European Journal of Medicinal Chemistry. 106: 167-179. PMID 26547055 DOI: 10.1016/J.Ejmech.2015.10.009 |
0.347 |
|
| 2015 |
Knapinska AM, Dreymuller D, Ludwig A, Smith L, Golubkov V, Sohail A, Fridman R, Giulianotti M, LaVoi TM, Houghten RA, Fields GB, Minond D. SAR Studies of Exosite-Binding Substrate-Selective Inhibitors of A Disintegrin And Metalloprotease 17 (ADAM17) and Application as Selective in Vitro Probes. Journal of Medicinal Chemistry. 58: 5808-24. PMID 26192023 DOI: 10.1021/Acs.Jmedchem.5B00354 |
0.643 |
|
| 2014 |
Spicer TP, Jiang J, Taylor AB, Choi JY, Hart PJ, Roush WR, Fields GB, Hodder PS, Minond D. Characterization of selective exosite-binding inhibitors of matrix metalloproteinase 13 that prevent articular cartilage degradation in vitro. Journal of Medicinal Chemistry. 57: 9598-611. PMID 25330343 DOI: 10.1021/Jm501284E |
0.667 |
|
| 2014 |
Madoux F, Tredup C, Spicer TP, Scampavia L, Chase PS, Hodder PS, Fields GB, Becker-Pauly C, Minond D. Development of high throughput screening assays and pilot screen for inhibitors of metalloproteases meprin α and β. Biopolymers. 102: 396-406. PMID 25048711 DOI: 10.1002/Bip.22527 |
0.582 |
|
| 2014 |
Wang H, Nefzi A, Fields GB, Lakshmana MK, Minond D. AlphaLISA-based high-throughput screening assay to measure levels of soluble amyloid precursor protein α. Analytical Biochemistry. 459: 24-30. PMID 24857774 DOI: 10.1016/J.Ab.2014.05.007 |
0.54 |
|
| 2014 |
Onwuha-Ekpete L, Tack L, Knapinska A, Smith L, Kaushik G, Lavoi T, Giulianotti M, Houghten RA, Fields GB, Minond D. Novel pyrrolidine diketopiperazines selectively inhibit melanoma cells via induction of late-onset apoptosis. Journal of Medicinal Chemistry. 57: 1599-608. PMID 24471466 DOI: 10.1021/Jm4019542 |
0.561 |
|
| 2014 |
Chavaroche A, Cudic M, Giulianotti M, Houghten RA, Fields GB, Minond D. Glycosylation of a disintegrin and metalloprotease 17 affects its activity and inhibition. Analytical Biochemistry. 449: 68-75. PMID 24361716 DOI: 10.1016/J.Ab.2013.12.018 |
0.63 |
|
| 2013 |
Richard DJ, Lena R, Bannister T, Blake N, Pierceall WE, Carlson NE, Keller CE, Koenig M, He Y, Minond D, Mishra J, Cameron M, Spicer T, Hodder P, Cardone MH. Hydroxyquinoline-derived compounds and analoguing of selective Mcl-1 inhibitors using a functional biomarker. Bioorganic & Medicinal Chemistry. 21: 6642-9. PMID 23993674 DOI: 10.1016/J.Bmc.2013.08.017 |
0.415 |
|
| 2013 |
Stawikowska R, Cudic M, Giulianotti M, Houghten RA, Fields GB, Minond D. Activity of ADAM17 (a disintegrin and metalloprotease 17) is regulated by its noncatalytic domains and secondary structure of its substrates. The Journal of Biological Chemistry. 288: 22871-9. PMID 23779109 DOI: 10.1074/Jbc.M113.462267 |
0.623 |
|
| 2013 |
Yegorova S, Chavaroche AE, Rodriguez MC, Minond D, Cudic M. Development of an AlphaScreen assay for discovery of inhibitors of low-affinity glycan-lectin interactions. Analytical Biochemistry. 439: 123-31. PMID 23685052 DOI: 10.1016/J.Ab.2013.04.028 |
0.44 |
|
| 2012 |
Minond D, Cudic M, Bionda N, Giulianotti M, Maida L, Houghten RA, Fields GB. Discovery of novel inhibitors of a disintegrin and metalloprotease 17 (ADAM17) using glycosylated and non-glycosylated substrates. The Journal of Biological Chemistry. 287: 36473-87. PMID 22927435 DOI: 10.1074/Jbc.M112.389114 |
0.669 |
|
| 2011 |
Roth J, Minond D, Darout E, Liu Q, Lauer J, Hodder P, Fields GB, Roush WR. Identification of novel, exosite-binding matrix metalloproteinase-13 inhibitor scaffolds. Bioorganic & Medicinal Chemistry Letters. 21: 7180-4. PMID 22018790 DOI: 10.1016/J.Bmcl.2011.09.077 |
0.682 |
|
| 2011 |
Chou TF, Brown SJ, Minond D, Nordin BE, Li K, Jones AC, Chase P, Porubsky PR, Stoltz BM, Schoenen FJ, Patricelli MP, Hodder P, Rosen H, Deshaies RJ. Reversible inhibitor of p97, DBeQ, impairs both ubiquitin-dependent and autophagic protein clearance pathways. Proceedings of the National Academy of Sciences of the United States of America. 108: 4834-9. PMID 21383145 DOI: 10.1073/Pnas.1015312108 |
0.399 |
|
| 2010 |
Weide T, Saldanha SA, Minond D, Spicer TP, Fotsing JR, Spaargaren M, Frère JM, Bebrone C, Sharpless KB, Hodder PS, Fokin VV. NH-1,2,3-Triazole-based Inhibitors of the VIM-2 Metallo-β-Lactamase: Synthesis and Structure-Activity Studies. Acs Medicinal Chemistry Letters. 1: 150-154. PMID 20625539 DOI: 10.1021/Ml900022Q |
0.343 |
|
| 2009 |
Lauer-Fields JL, Chalmers MJ, Busby SA, Minond D, Griffin PR, Fields GB. Identification of specific hemopexin-like domain residues that facilitate matrix metalloproteinase collagenolytic activity. The Journal of Biological Chemistry. 284: 24017-24. PMID 19574232 DOI: 10.1074/Jbc.M109.016873 |
0.658 |
|
| 2009 |
Minond D, Saldanha SA, Subramaniam P, Spaargaren M, Spicer T, Fotsing JR, Weide T, Fokin VV, Sharpless KB, Galleni M, Bebrone C, Lassaux P, Hodder P. Inhibitors of VIM-2 by screening pharmacologically active and click-chemistry compound libraries. Bioorganic & Medicinal Chemistry. 17: 5027-37. PMID 19553129 DOI: 10.1016/J.Bmc.2009.05.070 |
0.406 |
|
| 2009 |
Lauer-Fields JL, Minond D, Chase PS, Baillargeon PE, Saldanha SA, Stawikowska R, Hodder P, Fields GB. High throughput screening of potentially selective MMP-13 exosite inhibitors utilizing a triple-helical FRET substrate. Bioorganic & Medicinal Chemistry. 17: 990-1005. PMID 18358729 DOI: 10.1016/J.Bmc.2008.03.004 |
0.686 |
|
| 2008 |
Schröter T, Minond D, Weiser A, Dao C, Habel J, Spicer T, Chase P, Baillargeon P, Scampavia L, Schürer S, Chung C, Mader C, Southern M, Tsinoremas N, LoGrasso P, et al. Comparison of miniaturized time-resolved fluorescence resonance energy transfer and enzyme-coupled luciferase high-throughput screening assays to discover inhibitors of Rho-kinase II (ROCK-II). Journal of Biomolecular Screening. 13: 17-28. PMID 18227223 DOI: 10.1177/1087057107310806 |
0.374 |
|
| 2007 |
Lauer-Fields JL, Minond D, Brew K, Fields GB. Application of topologically constrained mini-proteins as ligands, substrates, and inhibitors. Methods in Molecular Biology (Clifton, N.J.). 386: 125-66. PMID 18604945 DOI: 10.1007/978-1-59745-430-8_5 |
0.607 |
|
| 2007 |
Minond D, Lauer-Fields JL, Cudic M, Overall CM, Pei D, Brew K, Moss ML, Fields GB. Differentiation of secreted and membrane-type matrix metalloproteinase activities based on substitutions and interruptions of triple-helical sequences. Biochemistry. 46: 3724-33. PMID 17338550 DOI: 10.1021/Bi062199J |
0.657 |
|
| 2007 |
Lauer-Fields JL, Minond D, Sritharan T, Kashiwagi M, Nagase H, Fields GB. Substrate conformation modulates aggrecanase (ADAMTS-4) affinity and sequence specificity. Suggestion of a common topological specificity for functionally diverse proteases. The Journal of Biological Chemistry. 282: 142-50. PMID 17095512 DOI: 10.1074/Jbc.M605236200 |
0.582 |
|
| 2006 |
Minond D, Lauer-Fields JL, Cudic M, Overall CM, Pei D, Brew K, Visse R, Nagase H, Fields GB. The roles of substrate thermal stability and P2 and P1' subsite identity on matrix metalloproteinase triple-helical peptidase activity and collagen specificity. The Journal of Biological Chemistry. 281: 38302-13. PMID 17065155 DOI: 10.1074/Jbc.M606004200 |
0.648 |
|
| 2004 |
Minond D, Lauer-Fields JL, Nagase H, Fields GB. Matrix metalloproteinase triple-helical peptidase activities are differentially regulated by substrate stability. Biochemistry. 43: 11474-81. PMID 15350133 DOI: 10.1021/Bi048938I |
0.652 |
|
| 2004 |
Baronas-Lowell D, Lauer-Fields JL, Borgia JA, Sferrazza GF, Al-Ghoul M, Minond D, Fields GB. Differential modulation of human melanoma cell metalloproteinase expression by alpha2beta1 integrin and CD44 triple-helical ligands derived from type IV collagen. The Journal of Biological Chemistry. 279: 43503-13. PMID 15292257 DOI: 10.1074/Jbc.M405979200 |
0.663 |
|
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