| Year |
Citation |
Score |
| 2024 |
Wang H, Lakshmana MK, Fields GB. Identification of binding partners that facilitate membrane-type 5 matrix metalloproteinase (MT5-MMP) processing of amyloid precursor protein. Journal of Cellular Physiology. PMID 38345408 DOI: 10.1002/jcp.31218 |
0.343 |
|
| 2023 |
Knapinska AM, Drotleff G, Chai C, Twohill D, Ernce A, Tokmina-Roszyk D, Grande I, Rodriguez M, Larson B, Fields GB. Screening MT1-MMP Activity and Inhibition in Three-Dimensional Tumor Spheroids. Biomedicines. 11. PMID 36831098 DOI: 10.3390/biomedicines11020562 |
0.355 |
|
| 2022 |
Fuerst R, Yong Choi J, Knapinska AM, Cameron MD, Ruiz C, Delmas A, Sundrud MS, Fields GB, Roush WR. Development of a putative Zn-chelating but highly selective MMP-13 inhibitor. Bioorganic & Medicinal Chemistry Letters. 129014. PMID 36202189 DOI: 10.1016/j.bmcl.2022.129014 |
0.31 |
|
| 2022 |
Waheed SO, Varghese A, DiCastri I, Kaski B, LaRouche C, Fields GB, Karabencheva-Christova TG. Mechanism of the Early Catalytic Events in the Collagenolysis by Matrix Metalloproteinase-1. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. e202200649. PMID 36161746 DOI: 10.1002/cphc.202200649 |
0.314 |
|
| 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 |
0.677 |
|
| 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 |
0.665 |
|
| 2021 |
Lo CH, Shay G, McGuire J, Li T, Shain K, Choi JY, Fuerst R, Roush WR, Knapinska AM, Fields GB, Lynch CC. Host-derived Matrix Metalloproteinase-13 Activity Promotes Multiple Myeloma-induced Osteolysis and Reduces Overall Survival. Cancer Research. PMID 33526510 DOI: 10.1158/0008-5472.CAN-20-2705 |
0.331 |
|
| 2020 |
Fields G, Knapinska AM, Singh C, Drotleff G, Blanco D, Chai C, Schwab J, Herd A. Matrix Metalloproteinase 13 Inhibitors for Modulation of Osteoclastogenesis: Enhancement of Solubility and Stability. Chemmedchem. PMID 33331147 DOI: 10.1002/cmdc.202000911 |
0.344 |
|
| 2019 |
Knapinska AM, Hart M, Drotleff G, Fields GB. Matrix Metalloproteinase Triple-Helical Peptide Inhibitors: Potential Cross-Reactivity with Caspase-11. Molecules (Basel, Switzerland). 24. PMID 31795279 DOI: 10.3390/Molecules24234355 |
0.425 |
|
| 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 |
0.667 |
|
| 2019 |
Fields GB. The Rebirth of Matrix Metalloproteinase Inhibitors: Moving Beyond the Dogma. Cells. 8. PMID 31461880 DOI: 10.3390/Cells8090984 |
0.446 |
|
| 2019 |
Fields GB. Mechanisms of Action of Novel Drugs Targeting Angiogenesis-Promoting Matrix Metalloproteinases. Frontiers in Immunology. 10: 1278. PMID 31214203 DOI: 10.3389/Fimmu.2019.01278 |
0.473 |
|
| 2019 |
Knapinska AM, Fields GB. The Expanding Role of MT1-MMP in Cancer Progression. Pharmaceuticals (Basel, Switzerland). 12. PMID 31137480 DOI: 10.3390/Ph12020077 |
0.438 |
|
| 2019 |
Fields GB. Methods for the Construction of Collagen-Based Triple-Helical Peptides Designed as Matrix Metalloproteinase Inhibitors. Methods in Molecular Biology (Clifton, N.J.). 1944: 229-252. PMID 30840247 DOI: 10.1007/978-1-4939-9095-5_17 |
0.463 |
|
| 2018 |
Pahwa S, Bhowmick M, Amar S, Cao J, Strongin AY, Fridman R, Weiss SJ, Fields GB. Characterization and regulation of MT1-MMP cell surface-associated activity. Chemical Biology & Drug Design. PMID 30480376 DOI: 10.1111/Cbdd.13450 |
0.428 |
|
| 2018 |
Marcink TC, Simoncic JA, An B, Knapinska AM, Fulcher YG, Akkaladevi N, Fields GB, Van Doren SR. MT1-MMP Binds Membranes by Opposite Tips of Its β Propeller to Position It for Pericellular Proteolysis. Structure (London, England : 1993). PMID 30471921 DOI: 10.2210/Pdb6Clz/Pdb |
0.447 |
|
| 2018 |
Fuerst R, Yong Choi J, Knapinska AM, Smith L, Cameron MD, Ruiz C, Fields GB, Roush WR. Development of matrix metalloproteinase-13 inhibitors - A structure-activity/structure-property relationship study. Bioorganic & Medicinal Chemistry. PMID 30249495 DOI: 10.1016/J.Bmc.2018.08.020 |
0.384 |
|
| 2018 |
Tokmina-Roszyk M, Fields GB. Dissecting MMP P' and P' subsite sequence preferences, utilizing a positional scanning, combinatorial triple-helical peptide library. The Journal of Biological Chemistry. PMID 30185620 DOI: 10.1074/Jbc.Ra118.003266 |
0.494 |
|
| 2018 |
Giricz O, Mo Y, Dahlman KB, Cotto-Rios XM, Vardabasso C, Nguyen H, Matusow B, Bartenstein M, Polishchuk V, Johnson DB, Bhagat TD, Shellooe R, Burton E, Tsai J, Zhang C, ... ... Fields GB, et al. The RUNX1/IL-34/CSF-1R axis is an autocrinally regulated modulator of resistance to BRAF-V600E inhibition in melanoma. Jci Insight. 3. PMID 30046005 DOI: 10.1172/Jci.Insight.120422 |
0.654 |
|
| 2018 |
Stawikowski MJ, Fields GB. Tricine as a convenient scaffold for the synthesis of-terminally branched collagen-model peptides. Tetrahedron Letters. 59: 130-134. PMID 29545652 DOI: 10.1016/J.Tetlet.2017.12.008 |
0.403 |
|
| 2017 |
Karabencheva-Christova TG, Christov CZ, Fields GB. Conformational Dynamics of Matrix Metalloproteinase-1•Triple-helical Peptide Complexes. The Journal of Physical Chemistry. B. PMID 29161042 DOI: 10.1021/Acs.Jpcb.7B09771 |
0.441 |
|
| 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 |
0.687 |
|
| 2017 |
Karabencheva-Christova TG, Christov CZ, Fields GB. Collagenolytic Matrix Metalloproteinase Structure-Function Relationships: Insights From Molecular Dynamics Studies. Advances in Protein Chemistry and Structural Biology. 109: 1-24. PMID 28683915 DOI: 10.1016/Bs.Apcsb.2017.04.001 |
0.43 |
|
| 2017 |
Knapinska AM, Estrada CA, Fields GB. The Roles of Matrix Metalloproteinases in Pancreatic Cancer. Progress in Molecular Biology and Translational Science. 148: 339-354. PMID 28662827 DOI: 10.1016/Bs.Pmbts.2017.03.004 |
0.374 |
|
| 2017 |
Choi JY, Fuerst R, Knapinska AM, Taylor AB, Smith L, Cao X, Hart PJ, Fields GB, Roush WR. Structure-Based Design and Synthesis of Potent and Selective Matrix Metalloproteinase 13 Inhibitors. Journal of Medicinal Chemistry. PMID 28653849 DOI: 10.1021/Acs.Jmedchem.7B00514 |
0.452 |
|
| 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 |
0.741 |
|
| 2017 |
Amar S, Smith L, Fields GB. Matrix metalloproteinase collagenolysis in health and disease. Biochimica Et Biophysica Acta. PMID 28456643 DOI: 10.1016/J.Bbamcr.2017.04.015 |
0.438 |
|
| 2017 |
Bhowmick M, Tokmina-Roszyk D, Onwuha-Ekpete L, Harmon K, Robichaud TK, Fürst R, Stawikowska R, Steffensen B, Roush WR, Wong HR, Fields GB. Second Generation Triple-Helical Peptide Inhibitors of Matrix Metalloproteinases. Journal of Medicinal Chemistry. PMID 28394608 DOI: 10.1021/Acs.Jmedchem.7B00018 |
0.468 |
|
| 2017 |
Stawikowski MJ, Knapinska AM, Fields GB. Determining the Substrate Specificity of Matrix Metalloproteases using Fluorogenic Peptide Substrates. Methods in Molecular Biology (Clifton, N.J.). 1579: 137-183. PMID 28299736 DOI: 10.1007/978-1-4939-6863-3_8 |
0.451 |
|
| 2017 |
Fields GB. Structure-guided design of selective matrix metalloproteinase (MMP) inhibitors and their application in animal models of multiple sclerosis, sepsis, and osteoarthritis Journal of Biotechnology & Biomaterials. 7. DOI: 10.4172/2155-952X.C1.069 |
0.305 |
|
| 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 |
0.714 |
|
| 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 |
0.694 |
|
| 2016 |
Chen Y, Guo H, Terajima M, Banerjee P, Liu X, Yu J, Momin A, Katayama H, Hanash S, Burns A, Fields G, Yamauchi M, Kurie J. Lysyl Hydroxylase 2 Is Secreted By Tumor Cells and Can Modify Collagen in the Extracellular Space. The Journal of Biological Chemistry. PMID 27803159 DOI: 10.1074/Jbc.M116.759803 |
0.331 |
|
| 2016 |
Singh W, Fields GB, Christov CZ, Karabencheva-Christova TG. Effects of Mutations on Structure-Function Relationships of Matrix Metalloproteinase-1. International Journal of Molecular Sciences. 17. PMID 27754420 DOI: 10.3390/Ijms17101727 |
0.409 |
|
| 2016 |
Iyer RP, de Castro Brás LE, Patterson NL, Bhowmick M, Flynn ER, Asher M, Cannon PL, Deleon-Pennell KY, Fields GB, Lindsey ML. Early matrix metalloproteinase-9 inhibition post-myocardial infarction worsens cardiac dysfunction by delaying inflammation resolution. Journal of Molecular and Cellular Cardiology. PMID 27746126 DOI: 10.1016/J.Yjmcc.2016.10.005 |
0.404 |
|
| 2016 |
Knapinska AM, Amar S, He Z, Matosevic S, Zylberberg C, Fields GB. Matrix metalloproteinases as reagents for cell isolation. Enzyme and Microbial Technology. 93: 29-43. PMID 27702483 DOI: 10.1016/J.Enzmictec.2016.07.009 |
0.379 |
|
| 2016 |
Cerofolini L, Amar S, Lauer JL, Martelli T, Fragai M, Luchinat C, Fields GB. Bilayer Membrane Modulation of Membrane Type 1 Matrix Metalloproteinase (MT1-MMP) Structure and Proteolytic Activity. Scientific Reports. 6: 29511. PMID 27405411 DOI: 10.1038/Srep29511 |
0.421 |
|
| 2016 |
Singh W, Fields GB, Christov CZ, Karabencheva-Christova TG. Importance of the Linker Region in Matrix Metalloproteinase-1 Domain Interactions. Rsc Advances. 6: 23223-23232. PMID 26998255 DOI: 10.1039/C6Ra03033E |
0.44 |
|
| 2016 |
Prior SH, Byrne TS, Tokmina-Roszyk D, Fields GB, Van Doren SR. Path to Collagenolysis: Collagen V Triple-Helix Model Bound Productively and in Encounters by Matrix Metalloproteinase-12. The Journal of Biological Chemistry. PMID 26887942 DOI: 10.1074/Jbc.M115.703124 |
0.443 |
|
| 2016 |
Fields GB, Stawikowski MJ. Imaging Matrix Metalloproteinase Activity Implicated in Breast Cancer Progression. Methods in Molecular Biology (Clifton, N.J.). 1406: 303-29. PMID 26820965 DOI: 10.1007/978-1-4939-3444-7_25 |
0.372 |
|
| 2015 |
Lindsey ML, Iyer RP, Zamilpa R, Yabluchanskiy A, DeLeon-Pennell KY, Hall ME, Kaplan A, Zouein FA, Bratton D, Flynn ER, Cannon PL, Tian Y, Jin YF, Lange RA, Tokmina-Roszyk D, ... Fields GB, et al. A Novel Collagen Matricryptin Reduces Left Ventricular Dilation Post-Myocardial Infarction by Promoting Scar Formation and Angiogenesis. Journal of the American College of Cardiology. 66: 1364-74. PMID 26383724 DOI: 10.1016/J.Jacc.2015.07.035 |
0.37 |
|
| 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 |
0.712 |
|
| 2015 |
Amar S, Fields GB. Potential clinical implications of recent matrix metalloproteinase inhibitor design strategies. Expert Review of Proteomics. 12: 445-7. PMID 26174966 DOI: 10.1586/14789450.2015.1069190 |
0.471 |
|
| 2015 |
Stawikowski MJ, Stawikowska R, Fields GB. Collagenolytic Matrix Metalloproteinase Activities toward Peptomeric Triple-Helical Substrates. Biochemistry. 54: 3110-21. PMID 25897652 DOI: 10.1021/Acs.Biochem.5B00110 |
0.473 |
|
| 2015 |
Bhowmick M, Stawikowska R, Tokmina-Roszyk D, Fields GB. Matrix metalloproteinase inhibition by heterotrimeric triple-helical Peptide transition state analogues. Chembiochem : a European Journal of Chemical Biology. 16: 1084-92. PMID 25766890 DOI: 10.1002/Cbic.201402716 |
0.493 |
|
| 2015 |
Knapinska AM, Tokmina-Roszyk D, Amar S, Tokmina-Roszyk M, Mochalin VN, Gogotsi Y, Cosme P, Terentis AC, Fields GB. Solid-phase synthesis, characterization, and cellular activities of collagen-model nanodiamond-peptide conjugates. Biopolymers. 104: 186-95. PMID 25753561 DOI: 10.1002/Bip.22636 |
0.371 |
|
| 2015 |
Zhao Y, Marcink TC, Sanganna Gari RR, Marsh BP, King GM, Stawikowska R, Fields GB, Van Doren SR. Transient collagen triple helix binding to a key metalloproteinase in invasion and development. Structure (London, England : 1993). 23: 257-69. PMID 25651059 DOI: 10.1016/J.Str.2014.11.021 |
0.426 |
|
| 2015 |
Fields GB. New strategies for targeting matrix metalloproteinases. Matrix Biology : Journal of the International Society For Matrix Biology. 44: 239-46. PMID 25595836 DOI: 10.1016/J.Matbio.2015.01.002 |
0.479 |
|
| 2015 |
Smith SJ, Gu L, Phipps EA, Dobrolecki LE, Mabrey KS, Gulley P, Dillehay KL, Dong Z, Fields GB, Chen YR, Ann D, Hickey RJ, Malkas LH. A Peptide mimicking a region in proliferating cell nuclear antigen specific to key protein interactions is cytotoxic to breast cancer. Molecular Pharmacology. 87: 263-76. PMID 25480843 DOI: 10.1124/Mol.114.093211 |
0.333 |
|
| 2015 |
Gao Y, Amar S, Pahwa S, Fields G, Kodadek T. Rapid lead discovery through iterative screening of one bead one compound libraries. Acs Combinatorial Science. 17: 49-59. PMID 25434974 DOI: 10.1021/Co500154E |
0.304 |
|
| 2014 |
Fields GB. Biophysical studies of matrix metalloproteinase/triple-helix complexes. Advances in Protein Chemistry and Structural Biology. 97: 37-48. PMID 25458354 DOI: 10.1016/Bs.Apcsb.2014.09.001 |
0.422 |
|
| 2014 |
Dielmann-Gessner J, Grossman M, Conti Nibali V, Born B, Solomonov I, Fields GB, Havenith M, Sagi I. Enzymatic turnover of macromolecules generates long-lasting protein-water-coupled motions beyond reaction steady state. Proceedings of the National Academy of Sciences of the United States of America. 111: 17857-62. PMID 25425663 DOI: 10.1073/Pnas.1410144111 |
0.314 |
|
| 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 |
0.737 |
|
| 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 |
0.682 |
|
| 2014 |
Zhang X, Bresee J, Fields GB, Edwards WB. Near-infrared triple-helical peptide with quenched fluorophores for optical imaging of MMP-2 and MMP-9 proteolytic activity in vivo. Bioorganic & Medicinal Chemistry Letters. 24: 3786-90. PMID 25047578 DOI: 10.1016/J.Bmcl.2014.06.072 |
0.418 |
|
| 2014 |
Zhang X, Bresee J, Cheney PP, Xu B, Bhowmick M, Cudic M, Fields GB, Edwards WB. Evaluation of a triple-helical peptide with quenched FluorSophores for optical imaging of MMP-2 and MMP-9 proteolytic activity. Molecules (Basel, Switzerland). 19: 8571-88. PMID 24959683 DOI: 10.3390/Molecules19068571 |
0.476 |
|
| 2014 |
Stawikowski MJ, Aukszi B, Stawikowska R, Cudic M, Fields GB. Glycosylation modulates melanoma cell α2β1 and α3β1 integrin interactions with type IV collagen. The Journal of Biological Chemistry. 289: 21591-604. PMID 24958723 DOI: 10.1074/Jbc.M114.572073 |
0.785 |
|
| 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 |
0.665 |
|
| 2014 |
Gu L, Smith S, Li C, Hickey RJ, Stark JM, Fields GB, Lang WH, Sandoval JA, Malkas LH. A PCNA-derived cell permeable peptide selectively inhibits neuroblastoma cell growth. Plos One. 9: e94773. PMID 24728180 DOI: 10.1371/Journal.Pone.0094773 |
0.353 |
|
| 2014 |
Tokmina-Roszyk M, Tokmina-Roszyk D, Bhowmick M, Fields GB. Development of a Förster resonance energy transfer assay for monitoring bacterial collagenase triple-helical peptidase activity. Analytical Biochemistry. 453: 61-9. PMID 24608089 DOI: 10.1016/J.Ab.2014.02.024 |
0.352 |
|
| 2014 |
Pahwa S, Stawikowski MJ, Fields GB. Monitoring and Inhibiting MT1-MMP during Cancer Initiation and Progression. Cancers. 6: 416-35. PMID 24549119 DOI: 10.3390/Cancers6010416 |
0.452 |
|
| 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 |
0.672 |
|
| 2014 |
de Castro Brás LE, Cates CA, DeLeon-Pennell KY, Ma Y, Iyer RP, Halade GV, Yabluchanskiy A, Fields GB, Weintraub ST, Lindsey ML. Citrate synthase is a novel in vivo matrix metalloproteinase-9 substrate that regulates mitochondrial function in the postmyocardial infarction left ventricle. Antioxidants & Redox Signaling. 21: 1974-85. PMID 24382150 DOI: 10.1089/Ars.2013.5411 |
0.397 |
|
| 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 |
0.715 |
|
| 2014 |
Lauer JL, Bhowmick M, Tokmina-Roszyk D, Lin Y, Van Doren SR, Fields GB. The role of collagen charge clusters in the modulation of matrix metalloproteinase activity. The Journal of Biological Chemistry. 289: 1981-92. PMID 24297171 DOI: 10.1074/Jbc.M113.513408 |
0.478 |
|
| 2013 |
Cerofolini L, Fields GB, Fragai M, Geraldes CF, Luchinat C, Parigi G, Ravera E, Svergun DI, Teixeira JM. Examination of matrix metalloproteinase-1 in solution: a preference for the pre-collagenolysis state. The Journal of Biological Chemistry. 288: 30659-71. PMID 24025334 DOI: 10.1074/Jbc.M113.477240 |
0.416 |
|
| 2013 |
Bhowmick M, Fields GB. Stabilization of collagen-model, triple-helical peptides for in vitro and in vivo applications. Methods in Molecular Biology (Clifton, N.J.). 1081: 167-94. PMID 24014440 DOI: 10.1007/978-1-62703-652-8_11 |
0.38 |
|
| 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 |
0.716 |
|
| 2013 |
Fu HL, Sohail A, Valiathan RR, Wasinski BD, Kumarasiri M, Mahasenan KV, Bernardo MM, Tokmina-Roszyk D, Fields GB, Mobashery S, Fridman R. Shedding of discoidin domain receptor 1 by membrane-type matrix metalloproteinases. The Journal of Biological Chemistry. 288: 12114-29. PMID 23519472 DOI: 10.1074/Jbc.M112.409599 |
0.453 |
|
| 2013 |
Tokmina-Roszyk M, Tokmina-Roszyk D, Fields GB. The synthesis and application of Fmoc-Lys(5-Fam) building blocks. Biopolymers. 100: 347-55. PMID 23444261 DOI: 10.1002/Bip.22222 |
0.47 |
|
| 2013 |
Fields GB. Interstitial collagen catabolism. The Journal of Biological Chemistry. 288: 8785-93. PMID 23430258 DOI: 10.1074/Jbc.R113.451211 |
0.384 |
|
| 2013 |
Pahwa S, Fields G. Abstract 5059: Quantitative analysis of MT1-MMP activity on cell surface: A FRET assay model. Cancer Research. 73: 5059-5059. DOI: 10.1158/1538-7445.Am2013-5059 |
0.468 |
|
| 2012 |
Bhowmick M, Fields GB. Synthesis of Fmoc-Gly-Ile Phosphinic Pseudodipeptide: Residue Specific Conditions for Construction of Matrix Metalloproteinase Inhibitor Building Blocks. International Journal of Peptide Research and Therapeutics. 18: 335-339. PMID 24496015 DOI: 10.1007/S10989-012-9307-Y |
0.352 |
|
| 2012 |
Ndinguri MW, Zheleznyak A, Lauer JL, Anderson CJ, Fields GB. Application of Collagen-Model Triple-Helical Peptide-Amphiphiles for CD44-Targeted Drug Delivery Systems. Journal of Drug Delivery. 2012: 592602. PMID 23213537 DOI: 10.1155/2012/592602 |
0.325 |
|
| 2012 |
Ndinguri MW, Bhowmick M, Tokmina-Roszyk D, Robichaud TK, Fields GB. Peptide-based selective inhibitors of matrix metalloproteinase-mediated activities. Molecules (Basel, Switzerland). 17: 14230-48. PMID 23201642 DOI: 10.3390/Molecules171214230 |
0.506 |
|
| 2012 |
Mikhailova M, Xu X, Robichaud TK, Pal S, Fields GB, Steffensen B. Identification of collagen binding domain residues that govern catalytic activities of matrix metalloproteinase-2 (MMP-2). Matrix Biology : Journal of the International Society For Matrix Biology. 31: 380-8. PMID 23085623 DOI: 10.1016/J.Matbio.2012.10.001 |
0.498 |
|
| 2012 |
Knapinska A, Fields GB. Chemical biology for understanding matrix metalloproteinase function. Chembiochem : a European Journal of Chemical Biology. 13: 2002-20. PMID 22933318 DOI: 10.1002/Cbic.201200298 |
0.429 |
|
| 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 |
0.739 |
|
| 2012 |
Iyer RP, Patterson NL, Fields GB, Lindsey ML. The history of matrix metalloproteinases: milestones, myths, and misperceptions. American Journal of Physiology. Heart and Circulatory Physiology. 303: H919-30. PMID 22904159 DOI: 10.1152/Ajpheart.00577.2012 |
0.425 |
|
| 2012 |
Akers WJ, Xu B, Lee H, Sudlow GP, Fields GB, Achilefu S, Edwards WB. Detection of MMP-2 and MMP-9 activity in vivo with a triple-helical peptide optical probe. Bioconjugate Chemistry. 23: 656-63. PMID 22309692 DOI: 10.1021/Bc300027Y |
0.454 |
|
| 2012 |
Bertini I, Fragai M, Luchinat C, Melikian M, Toccafondi M, Lauer JL, Fields GB. Structural basis for matrix metalloproteinase 1-catalyzed collagenolysis. Journal of the American Chemical Society. 134: 2100-10. PMID 22239621 DOI: 10.1021/Ja208338J |
0.436 |
|
| 2012 |
Schnaar R, Paulson JC, Macauley MS, Nycholat C, Pfrengle F, Rademacher C, Mahan A, Dionne K, Suscovich T, Alter G, Katoh T, Kiwamoto T, Brummet M, Bochner B, Tiemeyer M, ... ... Fields G, et al. Program and abstracts for the 2012 Joint Meeting of the Society for Glycobiology & American Society for Matrix Biology Glycobiology. 22: 1518-1650. DOI: 10.1093/Glycob/Cws127 |
0.316 |
|
| 2011 |
Arnold LH, Butt LE, Prior SH, Read CM, Fields GB, Pickford AR. The interface between catalytic and hemopexin domains in matrix metalloproteinase-1 conceals a collagen binding exosite. The Journal of Biological Chemistry. 286: 45073-82. PMID 22030392 DOI: 10.1074/Jbc.M111.285213 |
0.449 |
|
| 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 |
0.747 |
|
| 2011 |
Grossman M, Born B, Heyden M, Tworowski D, Fields GB, Sagi I, Havenith M. Correlated structural kinetics and retarded solvent dynamics at the metalloprotease active site. Nature Structural & Molecular Biology. 18: 1102-8. PMID 21926991 DOI: 10.1038/Nsmb.2120 |
0.304 |
|
| 2011 |
Robichaud TK, Steffensen B, Fields GB. Exosite interactions impact matrix metalloproteinase collagen specificities. The Journal of Biological Chemistry. 286: 37535-42. PMID 21896477 DOI: 10.1074/Jbc.M111.273391 |
0.478 |
|
| 2011 |
Giricz O, Lauer JL, Fields GB. Comparison of metalloproteinase protein and activity profiling. Analytical Biochemistry. 409: 37-45. PMID 20920458 DOI: 10.1016/J.Ab.2010.09.040 |
0.743 |
|
| 2010 |
Giricz O, Lauer JL, Fields GB. Variability in melanoma metalloproteinase expression profiling. Journal of Biomolecular Techniques : Jbt. 21: 194-204. PMID 21119930 |
0.716 |
|
| 2010 |
Xiao J, Addabbo RM, Lauer JL, Fields GB, Baum J. Local conformation and dynamics of isoleucine in the collagenase cleavage site provide a recognition signal for matrix metalloproteinases. The Journal of Biological Chemistry. 285: 34181-90. PMID 20679339 DOI: 10.1074/Jbc.M110.128355 |
0.428 |
|
| 2010 |
Palmier MO, Fulcher YG, Bhaskaran R, Duong VQ, Fields GB, Van Doren SR. NMR and bioinformatics discovery of exosites that tune metalloelastase specificity for solubilized elastin and collagen triple helices. The Journal of Biological Chemistry. 285: 30918-30. PMID 20663866 DOI: 10.1074/Jbc.M110.136903 |
0.453 |
|
| 2010 |
Fields GB. Synthesis and biological applications of collagen-model triple-helical peptides. Organic & Biomolecular Chemistry. 8: 1237-58. PMID 20204190 DOI: 10.1039/B920670A |
0.415 |
|
| 2010 |
Fields GB. Using fluorogenic peptide substrates to assay matrix metalloproteinases. Methods in Molecular Biology (Clifton, N.J.). 622: 393-433. PMID 20135296 DOI: 10.1007/978-1-60327-299-5_24 |
0.433 |
|
| 2010 |
Ye J, Fox SA, Cudic M, Rezler EM, Lauer JL, Fields GB, Terentis AC. Determination of penetratin secondary structure in live cells with Raman microscopy. Journal of the American Chemical Society. 132: 980-8. PMID 20041639 DOI: 10.1021/Ja9043196 |
0.326 |
|
| 2009 |
Cudic M, Burstein GD, Fields GB, Lauer-Fields J. Analysis of flavonoid-based pharmacophores that inhibit aggrecanases (ADAMTS-4 and ADAMTS-5) and matrix metalloproteinases through the use of topologically constrained peptide substrates. Chemical Biology & Drug Design. 74: 473-82. PMID 19793184 DOI: 10.1111/J.1747-0285.2009.00885.X |
0.456 |
|
| 2009 |
Cudic M, Fields GB. Extracellular proteases as targets for drug development. Current Protein & Peptide Science. 10: 297-307. PMID 19689354 DOI: 10.2174/138920309788922207 |
0.393 |
|
| 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 |
0.757 |
|
| 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 |
0.75 |
|
| 2008 |
Al-Ghoul M, Brück TB, Lauer-Fields JL, Asirvatham VS, Zapata C, Kerr RG, Fields GB. Comparative proteomic analysis of matched primary and metastatic melanoma cell lines. Journal of Proteome Research. 7: 4107-18. PMID 18698805 DOI: 10.1021/Pr800174K |
0.756 |
|
| 2008 |
Giricz O, Lauer-Fields JL, Fields GB. The normalization of gene expression data in melanoma: investigating the use of glyceraldehyde 3-phosphate dehydrogenase and 18S ribosomal RNA as internal reference genes for quantitative real-time PCR. Analytical Biochemistry. 380: 137-9. PMID 18554498 DOI: 10.1016/J.Ab.2008.05.024 |
0.653 |
|
| 2008 |
Bhaskaran R, Palmier MO, Lauer-Fields JL, Fields GB, Van Doren SR. MMP-12 catalytic domain recognizes triple helical peptide models of collagen V with exosites and high activity. The Journal of Biological Chemistry. 283: 21779-88. PMID 18539597 DOI: 10.1074/Jbc.M709966200 |
0.448 |
|
| 2008 |
Lauer-Fields JL, Whitehead JK, Li S, Hammer RP, Brew K, Fields GB. Selective modulation of matrix metalloproteinase 9 (MMP-9) functions via exosite inhibition. The Journal of Biological Chemistry. 283: 20087-95. PMID 18499673 DOI: 10.1074/Jbc.M801438200 |
0.502 |
|
| 2008 |
Khan DR, Rezler EM, Lauer-Fields J, Fields GB. Effects of drug hydrophobicity on liposomal stability. Chemical Biology & Drug Design. 71: 3-7. PMID 18086150 DOI: 10.1111/J.1747-0285.2007.00610.X |
0.654 |
|
| 2008 |
Gooljarsingh LT, Lakdawala A, Coppo F, Luo L, Fields GB, Tummino PJ, Gontarek RR. Characterization of an exosite binding inhibitor of matrix metalloproteinase 13. Protein Science : a Publication of the Protein Society. 17: 66-71. PMID 18042679 DOI: 10.1110/Ps.073130208 |
0.472 |
|
| 2008 |
Lauer-Fields JL, Spicer TP, Chase PS, Cudic M, Burstein GD, Nagase H, Hodder P, Fields GB. Screening of potential a disintegrin and metalloproteinase with thrombospondin motifs-4 inhibitors using a collagen model fluorescence resonance energy transfer substrate. Analytical Biochemistry. 373: 43-51. PMID 17949675 DOI: 10.1016/J.Ab.2007.09.014 |
0.444 |
|
| 2008 |
Cudic M, Patel DA, Lauer-Fields JL, Brew K, Fields GB. Development of a convenient peptide-based assay for lysyl hydroxylase. Biopolymers. 90: 330-8. PMID 17610258 DOI: 10.1002/Bip.20799 |
0.34 |
|
| 2007 |
Rezler EM, Khan DR, Tu R, Tirrell M, Fields GB. Peptide-mediated targeting of liposomes to tumor cells. Methods in Molecular Biology (Clifton, N.J.). 386: 269-98. PMID 18604950 DOI: 10.1007/978-1-59745-430-8_10 |
0.704 |
|
| 2007 |
Baronas-Lowell D, Lauer-Fields JL, Al-Ghoul M, Fields GB. Proteolytic profiling of the extracellular matrix degradome. Methods in Molecular Biology (Clifton, N.J.). 386: 167-202. PMID 18604946 DOI: 10.1007/978-1-59745-430-8_6 |
0.767 |
|
| 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 |
0.729 |
|
| 2007 |
Lauer-Fields J, Brew K, Whitehead JK, Li S, Hammer RP, Fields GB. Triple-helical transition state analogues: a new class of selective matrix metalloproteinase inhibitors. Journal of the American Chemical Society. 129: 10408-17. PMID 17672455 DOI: 10.1021/Ja0715849 |
0.494 |
|
| 2007 |
Lauer-Fields JL, Cudic M, Wei S, Mari F, Fields GB, Brew K. Engineered sarafotoxins as tissue inhibitor of metalloproteinases-like matrix metalloproteinase inhibitors. The Journal of Biological Chemistry. 282: 26948-55. PMID 17626018 DOI: 10.1074/Jbc.M611612200 |
0.485 |
|
| 2007 |
Rezler EM, Khan DR, Lauer-Fields J, Cudic M, Baronas-Lowell D, Fields GB. Targeted drug delivery utilizing protein-like molecular architecture. Journal of the American Chemical Society. 129: 4961-72. PMID 17397150 DOI: 10.1021/Ja066929M |
0.689 |
|
| 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 |
0.751 |
|
| 2007 |
Bix G, Iozzo RA, Woodall B, Burrows M, McQuillan A, Campbell S, Fields GB, Iozzo RV. Endorepellin, the C-terminal angiostatic module of perlecan, enhances collagen-platelet responses via the alpha2beta1-integrin receptor. Blood. 109: 3745-8. PMID 17197432 DOI: 10.1182/Blood-2006-08-039925 |
0.314 |
|
| 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 |
0.711 |
|
| 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 |
0.748 |
|
| 2005 |
Möller C, Rahmankhah S, Lauer-Fields J, Bubis J, Fields GB, Marí F. A novel conotoxin framework with a helix-loop-helix (Cs alpha/alpha) fold. Biochemistry. 44: 15986-96. PMID 16331958 DOI: 10.1021/Bi0511181 |
0.334 |
|
| 2004 |
Lauer-Fields JL, Nagase H, Fields GB. Development of a solid-phase assay for analysis of matrix metalloproteinase activity. Journal of Biomolecular Techniques : Jbt. 15: 305-16. PMID 15585827 |
0.35 |
|
| 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 |
0.748 |
|
| 2004 |
Xu X, Wang Y, Lauer-Fields JL, Fields GB, Steffensen B. Contributions of the MMP-2 collagen binding domain to gelatin cleavage. Substrate binding via the collagen binding domain is required for hydrolysis of gelatin but not short peptides. Matrix Biology : Journal of the International Society For Matrix Biology. 23: 171-81. PMID 15296945 DOI: 10.1016/J.Matbio.2004.05.002 |
0.503 |
|
| 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 |
0.785 |
|
| 2004 |
Chung L, Dinakarpandian D, Yoshida N, Lauer-Fields JL, Fields GB, Visse R, Nagase H. Collagenase unwinds triple-helical collagen prior to peptide bond hydrolysis. The Embo Journal. 23: 3020-30. PMID 15257288 DOI: 10.1038/Sj.Emboj.7600318 |
0.483 |
|
| 2004 |
Li Z, Yasuda Y, Li W, Bogyo M, Katz N, Gordon RE, Fields GB, Brömme D. Regulation of collagenase activities of human cathepsins by glycosaminoglycans. The Journal of Biological Chemistry. 279: 5470-9. PMID 14645229 DOI: 10.1074/Jbc.M310349200 |
0.372 |
|
| 2004 |
Baronas-Lowell D, Lauer-Fields JL, Fields GB. Induction of endothelial cell activation by a triple helical alpha2beta integrin ligand, derived from type I collagen alpha1(I)496-507. The Journal of Biological Chemistry. 279: 952-62. PMID 14581484 DOI: 10.1074/Jbc.M305989200 |
0.385 |
|
| 2004 |
Hurst DR, Schwartz MA, Ghaffari MA, Jin Y, Tschesche H, Fields GB, Sang QX. Catalytic- and ecto-domains of membrane type 1-matrix metalloproteinase have similar inhibition profiles but distinct endopeptidase activities. The Biochemical Journal. 377: 775-9. PMID 14533979 DOI: 10.1042/Bj20031067 |
0.45 |
|
| 2003 |
Lauer-Fields JL, Kele P, Sui G, Nagase H, Leblanc RM, Fields GB. Analysis of matrix metalloproteinase triple-helical peptidase activity with substrates incorporating fluorogenic L- or D-amino acids. Analytical Biochemistry. 321: 105-15. PMID 12963061 DOI: 10.1016/S0003-2697(03)00460-3 |
0.457 |
|
| 2003 |
Sweeney SM, DiLullo G, Slater SJ, Martinez J, Iozzo RV, Lauer-Fields JL, Fields GB, San Antonio JD. Angiogenesis in collagen I requires alpha2beta1 ligation of a GFP*GER sequence and possibly p38 MAPK activation and focal adhesion disassembly. The Journal of Biological Chemistry. 278: 30516-24. PMID 12788934 DOI: 10.1074/Jbc.M304237200 |
0.383 |
|
| 2003 |
Malkar NB, Lauer-Fields JL, Juska D, Fields GB. Characterization of peptide-amphiphiles possessing cellular activation sequences. Biomacromolecules. 4: 518-28. PMID 12741765 DOI: 10.1021/Bm0256597 |
0.364 |
|
| 2003 |
Lutolf MP, Lauer-Fields JL, Schmoekel HG, Metters AT, Weber FE, Fields GB, Hubbell JA. Synthetic matrix metalloproteinase-sensitive hydrogels for the conduction of tissue regeneration: engineering cell-invasion characteristics. Proceedings of the National Academy of Sciences of the United States of America. 100: 5413-8. PMID 12686696 DOI: 10.1073/Pnas.0737381100 |
0.425 |
|
| 2003 |
Lauer-Fields JL, Sritharan T, Stack MS, Nagase H, Fields GB. Selective hydrolysis of triple-helical substrates by matrix metalloproteinase-2 and -9. The Journal of Biological Chemistry. 278: 18140-5. PMID 12642591 DOI: 10.1074/Jbc.M211330200 |
0.359 |
|
| 2003 |
Lauer-Fields JL, Malkar NB, Richet G, Drauz K, Fields GB. Melanoma cell CD44 interaction with the alpha 1(IV)1263-1277 region from basement membrane collagen is modulated by ligand glycosylation. The Journal of Biological Chemistry. 278: 14321-30. PMID 12574156 DOI: 10.1074/Jbc.M212246200 |
0.37 |
|
| 2003 |
Baronas-Lowell D, Lauer-Fields JL, Fields GB. Defining the roles of collagen and collagen-like proteins within the proteome Journal of Liquid Chromatography and Related Technologies. 26: 2225-2254. DOI: 10.1081/Jlc-120023245 |
0.39 |
|
| 2002 |
Fields GB. Introduction to peptide synthesis. Current Protocols in Immunology / Edited by John E. Coligan ... [Et Al.]. Unit 9.1. PMID 18432893 DOI: 10.1002/0471142735.Im0901S47 |
0.317 |
|
| 2002 |
Fields GB. Introduction to peptide synthesis. Current Protocols in Protein Science / Editorial Board, John E. Coligan ... [Et Al.]. Unit 18.1. PMID 18429226 DOI: 10.1002/0471140864.Ps1801S26 |
0.317 |
|
| 2002 |
Fields GB. Introduction to peptide synthesis. Current Protocols in Molecular Biology / Edited by Frederick M. Ausubel ... [Et Al.]. Unit 11.15. PMID 18265296 DOI: 10.1002/0471142727.Mb1115S59 |
0.304 |
|
| 2002 |
Lauer-Fields JL, Fields GB. Triple-helical peptide analysis of collagenolytic protease activity. Biological Chemistry. 383: 1095-105. PMID 12437092 DOI: 10.1515/Bc.2002.118 |
0.488 |
|
| 2002 |
Lauer-Fields JL, Juska D, Fields GB. Matrix metalloproteinases and collagen catabolism. Biopolymers. 66: 19-32. PMID 12228918 DOI: 10.1002/Bip.10201 |
0.464 |
|
| 2002 |
Malkar NB, Lauer-Fields JL, Borgia JA, Fields GB. Modulation of triple-helical stability and subsequent melanoma cellular responses by single-site substitution of fluoroproline derivatives. Biochemistry. 41: 6054-64. PMID 11994000 DOI: 10.1021/Bi012071W |
0.356 |
|
| 2001 |
Edwards WB, Anderson CJ, Fields GB, Welch MJ. Evaluation of radiolabeled type IV collagen fragments as potential tumor imaging agents. Bioconjugate Chemistry. 12: 1057-65. PMID 11716700 DOI: 10.1021/Bc015520D |
0.302 |
|
| 2001 |
Dillo AK, Ochsenhirt SE, McCarthy JB, Fields GB, Tirrell M. Adhesion of alpha5beta1 receptors to biomimetic substrates constructed from peptide amphiphiles. Biomaterials. 22: 1493-505. PMID 11374448 DOI: 10.1016/S0142-9612(00)00304-5 |
0.377 |
|
| 2001 |
Lauer-Fields JL, Broder T, Sritharan T, Chung L, Nagase H, Fields GB. Kinetic analysis of matrix metalloproteinase activity using fluorogenic triple-helical substrates Biochemistry. 40: 5795-5803. PMID 11341845 DOI: 10.1021/Bi0101190 |
0.478 |
|
| 2001 |
Malkar NB, Fields GB. Synthesis of N α -(Fluoren-9-ylmethoxycarbonyl)- N ε -[(7- methoxycoumarin-4-yl)-acetyl]-L-lysine for Use in Solid-Phase Synthesis of Fluorogenic Substrates Letters in Peptide Science. 7: 48-49. DOI: 10.1007/978-94-010-0464-0_18 |
0.341 |
|
| 2000 |
Forns P, Lauer-Fields JL, Gao S, Fields GB. Induction of protein-like molecular architecture by monoalkyl hydrocarbon chains Biopolymers. 54: 531-546. PMID 10984405 DOI: 10.1002/1097-0282(200012)54:7<531::Aid-Bip60>3.0.Co;2-X |
0.322 |
|
| 2000 |
Lauer-Fields JL, Nagase H, Fields GB. Use of Edman degradation sequence analysis and matrix-assisted laser desorption/ionization mass spectrometry in designing substrates for matrix metalloproteinases Journal of Chromatography A. 890: 117-125. PMID 10976799 DOI: 10.1016/S0021-9673(00)00396-4 |
0.479 |
|
| 2000 |
Chung L, Shimokawa K, Dinakarpandian D, Grams F, Fields GB, Nagase H. Identification of the (183)RWTNNFREY(191) region as a critical segment of matrix metalloproteinase 1 for the expression of collagenolytic activity. The Journal of Biological Chemistry. 275: 29610-7. PMID 10871619 DOI: 10.1074/Jbc.M004039200 |
0.449 |
|
| 2000 |
Lauer-Fields JL, Tuzinski KA, Shimokawa KI, Nagase H, Fields GB. Hydrolysis of triple-helical collagen peptide models by matrix metalloproteinases Journal of Biological Chemistry. 275: 13282-13290. PMID 10788434 DOI: 10.1074/Jbc.275.18.13282 |
0.473 |
|
| 2000 |
Dori Y, Bianco-Peled H, Satija SK, Fields GB, McCarthy JB, Tirrell M. Ligand accessibility as means to control cell response to bioactive bilayer membranes. Journal of Biomedical Materials Research. 50: 75-81. PMID 10644966 DOI: 10.1002/(Sici)1097-4636(200004)50:1<75::Aid-Jbm11>3.0.Co;2-A |
0.313 |
|
| 2000 |
Lauer-Fields JL, Fields GB. Matrix metalloproteinase inhibitors and cancer Expert Opinion On Therapeutic Patents. 10: 1873-1884. DOI: 10.1517/13543776.10.12.1873 |
0.442 |
|
| 1999 |
Pakalns T, Haverstick KL, Fields GB, McCarthy JB, Mooradian DL, Tirrell M. Cellular recognition of synthetic peptide amphiphiles in self-assembled monolayer films. Biomaterials. 20: 2265-79. PMID 10614933 DOI: 10.1016/S0142-9612(99)00157-X |
0.336 |
|
| 1999 |
Fields GB. Induction of protein-like molecular architecture by self-assembly processes Bioorganic and Medicinal Chemistry. 7: 75-81. PMID 10199658 DOI: 10.1016/S0968-0896(98)00216-8 |
0.329 |
|
| 1999 |
Yu YC, Roontga V, Daragan VA, Mayo KH, Tirrell M, Fields GB. Structure and dynamics of peptide-amphiphiles incorporating triple-helical proteinlike molecular architecture. Biochemistry. 38: 1659-68. PMID 9931034 DOI: 10.1021/Bi982315L |
0.338 |
|
| 1998 |
Fields GB, Lauer JL, Dori Y, Forns P, Yu YC, Tirrell M. Protein-like molecular architecture: biomaterial applications for inducing cellular receptor binding and signal transduction. Biopolymers. 47: 143-51. PMID 9703769 DOI: 10.1002/(Sici)1097-0282(1998)47:2<143::Aid-Bip3>3.0.Co;2-U |
0.382 |
|
| 1998 |
Sweeney SM, Guy CA, Fields GB, San Antonio JD. Defining the domains of type I collagen involved in heparin- binding and endothelial tube formation. Proceedings of the National Academy of Sciences of the United States of America. 95: 7275-80. PMID 9636139 DOI: 10.1073/Pnas.95.13.7275 |
0.392 |
|
| 1998 |
Lauer JL, Gendron CM, Fields GB. Effect of ligand conformation on melanoma cell α3β1 integrin- mediated signal transduction events: Implications for a collagen structural modulation mechanism of tumor cell invasion Biochemistry. 37: 5279-5287. PMID 9548759 DOI: 10.1021/Bi972958L |
0.383 |
|
| 1998 |
Li C, McCarthy JB, Furcht LT, Fields GB. An all-D amino acid peptide model of alpha1(IV)531-543 from type IV collagen binds the alpha3beta1 integrin and mediates tumor cell adhesion, spreading, and motility. Biochemistry. 36: 15404-10. PMID 9398270 DOI: 10.1021/Bi971817G |
0.364 |
|
| 1998 |
Fields GB. Integrins: Cell adhesion molecules in cancer Expert Opinion On Therapeutic Patents. 8: 633-644. DOI: 10.1517/13543776.8.6.633 |
0.406 |
|
| 1998 |
Yu Y, Tirrell M, Fields GB. Minimal Lipidation Stabilizes Protein-Like Molecular Architecture Journal of the American Chemical Society. 120: 9979-9987. DOI: 10.1021/Ja981654Z |
0.319 |
|
| 1997 |
Lauer JL, Furcht LT, Fields GB. Inhibition of melanoma cell binding to type IV collagen by analogs of cell adhesion regulator Journal of Medicinal Chemistry. 40: 3077-3084. PMID 9301671 DOI: 10.1021/Jm970206J |
0.438 |
|
| 1997 |
Mayo KH, Fields GB. Peptides as Models for Understanding Protein Folding Advances in Molecular and Cell Biology. 22: 567-612. DOI: 10.1016/S1569-2558(08)60486-5 |
0.334 |
|
| 1997 |
Angeletti RH, Bibbs L, Bonewald LF, Fields GB, Kelly JW, McMurray JS, Moore WT, Weintraub ST. Analysis of racemization during "Standard" solid phase peptide synthesis: a multicenter study Techniques in Protein Chemistry. 8: 875-890. DOI: 10.1016/S1080-8914(97)80084-1 |
0.325 |
|
| 1996 |
Knutson JR, Iida J, Fields GB, McCarthy JB. CD44/chondroitin sulfate proteoglycan and alpha 2 beta 1 integrin mediate human melanoma cell migration on type IV collagen and invasion of basement membranes. Molecular Biology of the Cell. 7: 383-96. PMID 8868467 DOI: 10.1091/Mbc.7.3.383 |
0.36 |
|
| 1996 |
Huebsch JB, Fields GB, Triebes TG, Mooradian DL. Photoreactive analog of peptide FN-C/H-V from the carboxy-terminal heparin-binding domains of fibronectin supports endothelial cell adhesion and spreading on biomaterial surfaces. Journal of Biomedical Materials Research. 31: 555-67. PMID 8836853 DOI: 10.1002/(Sici)1097-4636(199608)31:4<555::Aid-Jbm16>3.0.Co;2-F |
0.326 |
|
| 1996 |
Nagase H, Fields GB. Human matrix metalloproteinase specificity studies using collagen sequence-based synthetic peptides Biopolymers. 40: 399-416. PMID 8765610 DOI: 10.1002/(Sici)1097-0282(1996)40:4<399::Aid-Bip5>3.0.Co;2-R |
0.481 |
|
| 1996 |
Fields GB, Prockop DJ. Perspectives on the synthesis and application of triple-helical, collagen-model peptides Biopolymers - Peptide Science Section. 40: 345-357. PMID 8765606 DOI: 10.1002/(Sici)1097-0282(1996)40:4<345::Aid-Bip1>3.0.Co;2-W |
0.36 |
|
| 1996 |
Grab B, Miles AJ, Furcht LT, Fields GB. Promotion of fibroblast adhesion by triple-helical peptide models of type I collagen-derived sequences. The Journal of Biological Chemistry. 271: 12234-40. PMID 8647820 DOI: 10.1074/Jbc.271.21.12234 |
0.305 |
|
| 1996 |
Yu Y, Berndt P, Tirrell M, Fields GB. Self-Assembling Amphiphiles for Construction of Protein Molecular Architecture Journal of the American Chemical Society. 118: 12515-12520. DOI: 10.1021/Ja9627656 |
0.323 |
|
| 1996 |
Hogue Angeletti R, Bibbs L, Bonewald LF, Fields GB, McMurray JS, Moore WT, Stults JT. Formation of a disulfide bond in an octreotide-like peptide: A multicenter study Techniques in Protein Chemistry. 7: 261-274. DOI: 10.1016/S1080-8914(96)80030-5 |
0.315 |
|
| 1996 |
Fields CG, Grab B, Lauer JL, Miles AJ, Yu Y, Fields GB. Solid-phase synthesis of triple-helical collagen-model peptides Letters in Peptide Science. 3: 3-16. DOI: 10.1007/Bf00131080 |
0.402 |
|
| 1995 |
Fields GB. The collagen triple-helix: Correlation of conformation with biological activities Connective Tissue Research. 31: 235-243. PMID 15609631 DOI: 10.3109/03008209509010815 |
0.462 |
|
| 1995 |
Miles AJ, Knutson JR, Skubitz AP, Furcht LT, McCarthy JB, Fields GB. A peptide model of basement membrane collagen alpha 1 (IV) 531-543 binds the alpha 3 beta 1 integrin. The Journal of Biological Chemistry. 270: 29047-50. PMID 7493922 DOI: 10.1074/Jbc.270.49.29047 |
0.36 |
|
| 1995 |
Berndt P, Fields GB, Tirrell M. Synthetic lipidation of peptides and amino acids: Monolayer structure and properties Journal of the American Chemical Society. 117: 9515-9522. DOI: 10.1021/Ja00142A019 |
0.361 |
|
| 1995 |
Fields GB, Angeletti RH, Bonewald LF, Moore WT, Smith AJ, Stults JT, Williams LC. Correlation of cleavage techniques with side-reactions following solid-phase peptide synthesis Techniques in Protein Chemistry. 6: 539-546. DOI: 10.1016/S1080-8914(06)80065-7 |
0.337 |
|
| 1995 |
Lauer JL, Fields CG, Fields GB. Sequence dependence of aspartimide formation during 9-fluorenylmethoxycarbonyl solid-phase peptide synthesis Letters in Peptide Science. 1: 197-205. DOI: 10.1007/Bf00117955 |
0.322 |
|
| 1994 |
Fields CG, Lovdahl CM, Miles AJ, Hagen VL, Fields GB. Solid-phase synthesis and stability of triple-helical peptides incorporating native collagen sequences. Biopolymers. 33: 1695-707. PMID 8241428 DOI: 10.1002/Bip.360331107 |
0.356 |
|
| 1994 |
Edwards WB, Fields CG, Anderson CJ, Pajeau TS, Welch MJ, Fields GB. Generally applicable, convenient solid-phase synthesis and receptor affinities of octreotide analogs. Journal of Medicinal Chemistry. 37: 3749-57. PMID 7966134 DOI: 10.1021/Jm00048A011 |
0.31 |
|
| 1994 |
Fields GB, Angeletti RH, Carr SA, Smith AJ, Stults JT, Williams LC, Young JD. Variable Success of Peptide-Resin Cleavage and Deprotection Following Solid-Phase Synthesis Techniques in Protein Chemistry. 5: 501-507. DOI: 10.1016/B978-0-12-194710-1.50061-8 |
0.306 |
|
| 1994 |
Miles A, Fields C, Furcht L, Knutson J, McCarthy J, Skubitz A, Fields G. Cellular recognition processes and type IV collagen conformation Matrix Biology. 14: 361. DOI: 10.1016/0945-053X(94)90054-X |
0.302 |
|
| 1993 |
Fields CG, Fields GB. Minimization of tryptophan alkylation following 9-fluorenylmethoxycarbonyl solid-phase peptide synthesis Tetrahedron Letters. 34: 6661-6664. DOI: 10.1016/S0040-4039(00)61669-6 |
0.302 |
|
| 1993 |
Fields GB, Carr SA, Marshak DR, Smith AJ, Stults JT, Williams LC, Williams KR, Young JD. Evaluation of Peptide Synthesis As Practiced in 53 Different Laboratories Techniques in Protein Chemistry. 229-238. DOI: 10.1016/B978-0-12-058757-5.50030-5 |
0.323 |
|
| 1992 |
Netzel-Arnett SJ, Fields GB, Nagase H, Suzuki K, Moore WG, Birkedal-Hansen H, Van Wart HE. Comparative sequence specificities of human fibroblast and neutrophil matrix metalloproteinases. Matrix (Stuttgart, Germany). Supplement. 1: 74-5. PMID 1480093 |
0.63 |
|
| 1992 |
Goli UB, Fields GB, Van Wart HE. Synthetic triple helical models for the collagen cleavage site in interstitial collagens. Matrix (Stuttgart, Germany). Supplement. 1: 71-2. PMID 1480091 |
0.616 |
|
| 1992 |
Fields GB, Van Wart HE. Unique features of the tissue collagenase cleavage site in interstitial collagens Matrix (Stuttgart, Germany). Supplement. 1: 68-70. PMID 1480090 |
0.58 |
|
| 1991 |
Netzel-Arnett S, Fields GB, Birkedal-Hansen H, Van Wart HE, Fields G. Sequence specificities of human fibroblast and neutrophil collagenases. The Journal of Biological Chemistry. 266: 6747-55. PMID 1849891 |
0.596 |
|
| 1991 |
Fields GB. A model for interstitial collagen catabolism by mammalian collagenases Journal of Theoretical Biology. 153: 585-602. PMID 1666905 DOI: 10.1016/S0022-5193(05)80157-2 |
0.34 |
|
| 1990 |
King DS, Fields CG, Fields GB. A cleavage method which minimizes side reactions following Fmoc solid phase peptide synthesis International Journal of Peptide and Protein Research. 36: 255-266. PMID 2279849 DOI: 10.1111/J.1399-3011.1990.Tb00976.X |
0.308 |
|
| 1990 |
Fields GB, Noble RL. Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids International Journal of Peptide and Protein Research. 35: 161-214. PMID 2191922 DOI: 10.1111/J.1399-3011.1990.Tb00939.X |
0.31 |
|
| 1989 |
Fields CG, Fields GB, Noble RL, Cross TA. Solid phase peptide synthesis of 15N-gramicidins A, B, and C and high performance liquid chromatographic purification. International Journal of Peptide and Protein Research. 33: 298-303. PMID 2473960 DOI: 10.1111/J.1399-3011.1989.Tb01285.X |
0.3 |
|
| 1988 |
Fields GB, Fields CG, Petefish J, Van Wart HE, Cross TA. Solid-phase peptide synthesis and solid-state NMR spectroscopy of [Ala3-15N][Val1]gramicidin A Proceedings of the National Academy of Sciences of the United States of America. 85: 1384-1388. PMID 2449690 |
0.573 |
|
| 1987 |
Fields GB, Van Wart HE, Birkedal-Hansen H. Sequence specificity of human skin fibroblast collagenase. Evidence for the role of collagen structure in determining the collagenase cleavage site. The Journal of Biological Chemistry. 262: 6221-6. PMID 3032960 |
0.604 |
|
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