-
1
-
-
0027595948
-
-
0036-8075 10.1126/science.8493529.
-
R. Langer and J. P. Vacanti, Science 0036-8075 10.1126/science.8493529 260, 920 (1993).
-
(1993)
Science
, vol.260
, pp. 920
-
-
Langer, R.1
Vacanti, J.P.2
-
2
-
-
0034646334
-
-
0027-8424 10.1073/pnas.040562297.
-
D. T. Chiu, N. L. Jeon, S. Huang, R. S. Kane, C. J. Wargo, I. S. Choi, D. E. Ingber, and G. M. Whitesides, Proc. Natl. Acad. Sci. U.S.A. 0027-8424 10.1073/pnas.040562297 97, 2408 (2000).
-
(2000)
Proc. Natl. Acad. Sci. U.S.A.
, vol.97
, pp. 2408
-
-
Chiu, D.T.1
Jeon, N.L.2
Huang, S.3
Kane, R.S.4
Wargo, C.J.5
Choi, I.S.6
Ingber, D.E.7
Whitesides, G.M.8
-
3
-
-
12344280978
-
-
1473-0197 10.1039/b403091e.
-
S. W. Rhee, A. M. Taylor, C. H. Tu, D. H. Cribbs, C. W. Cotman, and N. L. Jeon, Lab Chip 1473-0197 10.1039/b403091e 5, 102 (2005).
-
(2005)
Lab Chip
, vol.5
, pp. 102
-
-
Rhee, S.W.1
Taylor, A.M.2
Tu, C.H.3
Cribbs, D.H.4
Cotman, C.W.5
Jeon, N.L.6
-
4
-
-
0037563810
-
-
1076-3279 10.1089/107632703764664729.
-
W. Tan and T. A. Desai, Tissue Eng. 1076-3279 10.1089/107632703764664729 9, 255 (2003).
-
(2003)
Tissue Eng.
, vol.9
, pp. 255
-
-
Tan, W.1
Desai, T.A.2
-
7
-
-
0031947320
-
-
1433-7851 10.1002/(SICI)1521-3773(19980316)37:5<550::AID-ANIE550>3. 3.CO;2-7.
-
Y. Xia and G. M. Whitesides, Angew. Chem., Int. Ed. 1433-7851 10.1002/(SICI)1521-3773(19980316)37:5<550::AID-ANIE550>3.3.CO;2-7 37, 550 (1998).
-
(1998)
Angew. Chem., Int. Ed.
, vol.37
, pp. 550
-
-
Xia, Y.1
Whitesides, G.M.2
-
11
-
-
34250642011
-
-
0935-9648 10.1002/adma.200600882.
-
L. J. Guo, Adv. Mater. (Weinheim, Ger.) 0935-9648 10.1002/adma.200600882 19, 495 (2007).
-
(2007)
Adv. Mater. (Weinheim, Ger.)
, vol.19
, pp. 495
-
-
Guo, L.J.1
-
13
-
-
17244366080
-
-
0935-9648 10.1002/adma.200400547.
-
S. M. Bhangale, V. Tjong, L. Wu, N. Yakovlev, and P. M. Moran, Adv. Mater. (Weinheim, Ger.) 0935-9648 10.1002/adma.200400547 17, 809 (2005).
-
(2005)
Adv. Mater. (Weinheim, Ger.)
, vol.17
, pp. 809
-
-
Bhangale, S.M.1
Tjong, V.2
Wu, L.3
Yakovlev, N.4
Moran, P.M.5
-
15
-
-
0035353376
-
-
0743-7463
-
E. Ostuni, C. S. Chen, D. E. Ingber, and G. M. Whitesides, Langmuir 17, 2828 (2001). 0743-7463
-
(2001)
Langmuir
, vol.17
, pp. 2828
-
-
Ostuni, E.1
Chen, C.S.2
Ingber, D.E.3
Whitesides, G.M.4
-
16
-
-
55149107580
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-
This is a 10× solution that contains 500 mM KCl, 20 mM MgCl2, and 10 mM ATP.
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This is a 10× solution that contains 500 mM KCl, 20 mM MgCl2, and 10 mM ATP.
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Cell Culture. NIH 3T3 fibroblasts were washed once with PBS and then exposed to trypsin-ethylenediamine-tetraacetate for 5 min. After dissociation from the tissue culture plates, the cells were seeded on the pattern that we fabricated through the proposed method. The cells were cultured at 37 ° C under 5% carbon dioxide in Dulbecco's modified Eagle's medium that was supplemented with 10% calf serum, glutamine (0.3 mg/ml), streptomycin (100 μg/ml), penicillin (100 U/ml), and 20 mM N-2-hydroxyethylpiperazine- N′ 2 -ethanesulfonic acid at a pH of 7.4. After seeding, the cells were subsequently incubated for at least 6 h to allow attachment and spreading.
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Cell Culture. NIH 3T3 fibroblasts were washed once with PBS and then exposed to trypsin-ethylenediamine-tetraacetate for 5 min. After dissociation from the tissue culture plates, the cells were seeded on the pattern that we fabricated through the proposed method. The cells were cultured at 37 ° C under 5% carbon dioxide in Dulbecco's modified Eagle's medium that was supplemented with 10% calf serum, glutamine (0.3 mg/ml), streptomycin (100 μg/ml), penicillin (100 U/ml), and 20 mM N-2-hydroxyethylpiperazine- N′ 2 -ethanesulfonic acid at a pH of 7.4. After seeding, the cells were subsequently incubated for at least 6 h to allow attachment and spreading.
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11144238907
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J. Kubicek, S. Brelsford, P. Ahluwalia, and P. R. LeDuc, Langmuir 20, 11552 (2004).
-
(2004)
Langmuir
, vol.20
, pp. 11552
-
-
Kubicek, J.1
Brelsford, S.2
Ahluwalia, P.3
Leduc, P.R.4
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19
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0032067704
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Due to the limitations of profile measurement systems, such as an atomic force microscope and our relatively large patterns, we analyzed the three-dimensional profile of a single pattern through the software "NIH IMAGEJ," which is in the public domain, from the National Institute of Health (software resource;). This method might not provide the exact three-dimensional size of a single pattern but it allows for approximate size comparisons., 0890-6955 10.1016/S0890-6955(97)00118-1.
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Due to the limitations of profile measurement systems, such as an atomic force microscope and our relatively large patterns, we analyzed the three-dimensional profile of a single pattern through the software "NIH IMAGEJ," which is in the public domain, from the National Institute of Health (software resource; http://rsbweb.nih.gov/ij/). This method might not provide the exact three-dimensional size of a single pattern but it allows for approximate size comparisons. M. B. Kiran, B. Ramamoorthy, and V. Radhakrishnan, Int. J. Mach. Tools Manuf. 0890-6955 10.1016/S0890-6955(97)00118-1 38, 685 (1998).
-
(1998)
Int. J. Mach. Tools Manuf.
, vol.38
, pp. 685
-
-
Kiran, M.B.1
Ramamoorthy, B.2
Radhakrishnan, V.3
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20
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34047173079
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0034-6748 10.1063/1.2712870.
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C. M. Cesa, N. KirchgeΒner, D. Mayer, U. S. Schwarz, B. Hoffmann, and R. Merkel, Rev. Sci. Instrum. 0034-6748 10.1063/1.2712870 78, 034301 (2007).
-
(2007)
Rev. Sci. Instrum.
, vol.78
, pp. 034301
-
-
Cesa, C.M.1
Kirchgeßner, N.2
Mayer, D.3
Schwarz, U.S.4
Hoffmann, B.5
Merkel, R.6
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This buffer contains 5 mM tris-HCl (pH 0.8) and 0.2 mM CaCl2.
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This buffer contains 5 mM tris-HCl (pH 0.8) and 0.2 mM CaCl2.
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Actin filament preparation. We prepared filamentous actin in an ATP buffer (general actin buffer, from Cytoskeleton; No. BSA01) (Ref.) or PBS solution. This required several steps: (1) combine 1 ml of ATP buffer with 2 μl pure ATP (100 mM), (2) suspend G-actin to obtain a concentration of 0.4 mg/ml for 1 h at 24 °C, and (3) mix and incubate this solution for 1 h at 24 °C while adding 66 μl of ATP polymerization buffer (Ref.). Finally, we stained actin filaments using 6 μM Alexa Fluor 488 phalloidin (from Molecular Probes, No. A12379).
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Actin filament preparation. We prepared filamentous actin in an ATP buffer (general actin buffer, from Cytoskeleton; No. BSA01) (Ref.) or PBS solution. This required several steps: (1) combine 1 ml of ATP buffer with 2 μl pure ATP (100 mM), (2) suspend G-actin to obtain a concentration of 0.4 mg/ml for 1 h at 24 °C, and (3) mix and incubate this solution for 1 h at 24 °C while adding 66 μl of ATP polymerization buffer (Ref.). Finally, we stained actin filaments using 6 μM Alexa Fluor 488 phalloidin (from Molecular Probes, No. A12379).
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