| Year |
Citation |
Score |
| 2015 |
Ramanathan A, Karuri N. Proteolysis of decellularized extracellular matrices results in loss of fibronectin and cell binding activity. Biochemical and Biophysical Research Communications. 459: 246-51. PMID 25724944 DOI: 10.1016/J.Bbrc.2015.02.092 |
0.612 |
|
| 2015 |
Zhang C, Ramanathan A, Karuri NW. Proteolytically stabilizing fibronectin without compromising cell and gelatin binding activity. Biotechnology Progress. 31: 277-88. PMID 25394993 DOI: 10.1002/Btpr.2018 |
0.605 |
|
| 2014 |
Zhang C, Desai R, Perez-Luna V, Karuri N. PEGylation of lysine residues improves the proteolytic stability of fibronectin while retaining biological activity Biotechnology Journal. 9: 1033-1043. PMID 24803071 DOI: 10.1002/Biot.201400115 |
0.544 |
|
| 2014 |
Ramanathan A, Karuri N. Fibronectin alters the rate of formation and structure of the fibrin matrix. Biochemical and Biophysical Research Communications. 443: 395-9. PMID 24309108 DOI: 10.1016/J.Bbrc.2013.11.090 |
0.535 |
|
| 2014 |
Zhang C, Hekmatfer S, Karuri NW. A comparative study of polyethylene glycol hydrogels derivatized with the RGD peptide and the cell-binding domain of fibronectin. Journal of Biomedical Materials Research. Part A. 102: 170-9. PMID 23613303 DOI: 10.1002/Jbm.A.34687 |
0.524 |
|
| 2013 |
Zhang C, Hekmatfar S, Ramanathan A, Karuri NW. PEGylated human plasma fibronectin is proteolytically stable, supports cell adhesion, cell migration, focal adhesion assembly, and fibronectin fibrillogenesis. Biotechnology Progress. 29: 493-504. PMID 23319204 DOI: 10.1002/Btpr.1689 |
0.647 |
|
| 2012 |
Kshatriya PP, Karuri SW, Chiang C, Karuri NW. A combinatorial approach for directing the amount of fibronectin fibrils assembled by cells that uses surfaces derivatized with mixtures of fibronectin and cell binding domains. Biotechnology Progress. 28: 862-71. PMID 22467639 DOI: 10.1002/Btpr.1537 |
0.414 |
|
| 2012 |
Chiang C, Karuri SW, Kshatriya PP, Schwartz J, Schwarzbauer JE, Karuri NW. Surface derivatization strategy for combinatorial analysis of cell response to mixtures of protein domains. Langmuir : the Acs Journal of Surfaces and Colloids. 28: 548-56. PMID 22103809 DOI: 10.1021/La202053K |
0.606 |
|
| 2009 |
Karuri NW, Lin Z, Rye HS, Schwarzbauer JE. Probing the conformation of the fibronectin III1-2 domain by fluorescence resonance energy transfer. The Journal of Biological Chemistry. 284: 3445-52. PMID 19064996 DOI: 10.1074/Jbc.M805025200 |
0.54 |
|
| 2008 |
Karuri NW, Nealey PF, Murphy CJ, Albrecht RM. Structural organization of the cytoskeleton in SV40 human corneal epithelial cells cultured on nano- and microscale grooves. Scanning. 30: 405-13. PMID 18626907 DOI: 10.1002/Sca.20123 |
0.663 |
|
| 2008 |
Schwarzbauer JE, Karuri NW, Lin Z, Rye HS. Dissecting a fibronectin matrix assembly domain using FRET Matrix Biology. 27: 30-31. DOI: 10.1016/J.Matbio.2008.09.303 |
0.517 |
|
| 2006 |
Karuri NW, Porri TJ, Albrecht RM, Murphy CJ, Nealey PF. Nano- and microscale holes modulate cell-substrate adhesion, cytoskeletal organization, and -beta1 integrin localization in SV40 human corneal epithelial cells. Ieee Transactions On Nanobioscience. 5: 273-80. PMID 17181027 DOI: 10.1109/Tnb.2006.886570 |
0.584 |
|
| 2005 |
Karuri NW, Nealey PF, Murphy CJ, Albrecht RM. Structural organization of the cytoskeleton in SV40 human corneal epithelial cells cultured on nano- and microscale topography Microscopy and Microanalysis. 11: 182-183. DOI: 10.1017/S1431927605506366 |
0.582 |
|
| 2004 |
Karuri NW, Liliensiek S, Teixeira AI, Abrams G, Campbell S, Nealey PF, Murphy CJ. Biological length scale topography enhances cell-substratum adhesion of human corneal epithelial cells. Journal of Cell Science. 117: 3153-64. PMID 15226393 DOI: 10.1242/Jcs.01146 |
0.704 |
|
| 2004 |
Karuri NW, Liliensiek SJ, Diehl KA, Foley JD, Abrams GA, Campbell S, Nealey PF, Murphy CJ. Biologic length scale topographic features modulate human corneal epithelial cell adhesion and migration Transactions - 7th World Biomaterials Congress. 115. |
0.393 |
|
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