| Year |
Citation |
Score |
| 2016 |
Deamer D, Akeson M, Branton D. Three decades of nanopore sequencing. Nature Biotechnology. 34: 518-24. PMID 27153285 DOI: 10.1038/Nbt.3423 |
0.301 |
|
| 2016 |
Branton D. Fracture faces of frozen membranes: 50th anniversary. Molecular Biology of the Cell. 27: 421-3. PMID 26823391 DOI: 10.1091/mbc.E15-05-0287 |
0.322 |
|
| 2013 |
Garaj S, Liu S, Golovchenko JA, Branton D. Molecule-hugging graphene nanopores. Proceedings of the National Academy of Sciences of the United States of America. 110: 12192-6. PMID 23836648 DOI: 10.1073/Pnas.1220012110 |
0.549 |
|
| 2012 |
Han A, Kuan A, Golovchenko J, Branton D. Nanopatterning on nonplanar and fragile substrates with ice resists. Nano Letters. 12: 1018-21. PMID 22229744 DOI: 10.1021/Nl204198W |
0.526 |
|
| 2011 |
Han A, Chervinsky J, Branton D, Golovchenko JA. An ice lithography instrument. The Review of Scientific Instruments. 82: 065110. PMID 21721733 DOI: 10.1063/1.3601005 |
0.507 |
|
| 2011 |
Sadki ES, Garaj S, Vlassarev D, Golovchenko JA, Branton D. Embedding a carbon nanotube across the diameter of a solid state nanopore Journal of Vacuum Science and Technology B:Nanotechnology and Microelectronics. 29. DOI: 10.1116/1.3628602 |
0.546 |
|
| 2010 |
Han A, Vlassarev D, Wang J, Golovchenko JA, Branton D. Ice lithography for nanodevices. Nano Letters. 10: 5056-9. PMID 21038857 DOI: 10.1021/Nl1032815 |
0.516 |
|
| 2010 |
Garaj S, Hubbard W, Reina A, Kong J, Branton D, Golovchenko JA. Graphene as a subnanometre trans-electrode membrane. Nature. 467: 190-3. PMID 20720538 DOI: 10.1038/Nature09379 |
0.538 |
|
| 2009 |
Albertorio F, Hughes ME, Golovchenko JA, Branton D. Base dependent DNA-carbon nanotube interactions: activation enthalpies and assembly-disassembly control. Nanotechnology. 20: 395101. PMID 19724110 DOI: 10.1088/0957-4484/20/39/395101 |
0.543 |
|
| 2006 |
Park SY, Russo CJ, Branton D, Stone HA. Eddies in a bottleneck: an arbitrary Debye length theory for capillary electroosmosis. Journal of Colloid and Interface Science. 297: 832-9. PMID 16376361 DOI: 10.1016/J.Jcis.2005.11.045 |
0.522 |
|
| 2005 |
King GM, Schürmann G, Branton D, Golovchenko JA. Nanometer patterning with ice. Nano Letters. 5: 1157-60. PMID 15943460 DOI: 10.1021/Nl050405N |
0.517 |
|
| 2004 |
Chen P, Gu J, Brandin E, Kim YR, Wang Q, Branton D. PROBING SINGLE DNA MOLECULE TRANSPORT USING FABRICATED NANOPORES. Nano Letters. 4: 2293-2298. PMID 25221441 DOI: 10.1021/Nl048654J |
0.313 |
|
| 2004 |
Chen P, Mitsui T, Farmer DB, Golovchenko J, Gordon RG, Branton D. Atomic Layer Deposition to Fine-Tune the Surface Properties and Diameters of Fabricated Nanopores. Nano Letters. 4: 1333-1337. PMID 24991194 DOI: 10.1021/Nl0494001 |
0.526 |
|
| 2004 |
Mitsui T, Gershow M, Brandin E, Kim Y, Chen P, Farmer DB, Branton D, Golovchenko J. New method for detection of single DNA molecules using Si-based nano-scale pore The Japan Society of Applied Physics. 2004: 372-373. DOI: 10.7567/Ssdm.2004.I-5-1 |
0.522 |
|
| 2003 |
Sauer-Budge AF, Nyamwanda JA, Lubensky DK, Branton D. Unzipping kinetics of double-stranded DNA in a nanopore. Physical Review Letters. 90: 238101. PMID 12857290 DOI: 10.1103/Physrevlett.90.238101 |
0.669 |
|
| 2001 |
Li J, Stein D, McMullan C, Branton D, Aziz MJ, Golovchenko JA. Ion-beam sculpting at nanometre length scales. Nature. 412: 166-9. PMID 11449268 DOI: 10.1038/35084037 |
0.546 |
|
| 2001 |
Wang H, Branton D. Nanopores with a spark for single-molecule detection. Nature Biotechnology. 19: 622-3. PMID 11433269 DOI: 10.1038/90216 |
0.302 |
|
| 2000 |
Meller A, Nivon L, Brandin E, Golovchenko J, Branton D. Rapid nanopore discrimination between single polynucleotide molecules. Proceedings of the National Academy of Sciences of the United States of America. 97: 1079-84. PMID 10655487 DOI: 10.1073/Pnas.97.3.1079 |
0.558 |
|
| 1999 |
Branton D, Golovchenko J. Biochemical sensors. Adapting to nanoscale events. Nature. 398: 660-1. PMID 10227284 DOI: 10.1038/19412 |
0.553 |
|
| 1998 |
Viel A, Gee MS, Tomooka L, Branton D. Motifs involved in interchain binding at the tail-end of spectrin. Biochimica Et Biophysica Acta. 1384: 396-404. PMID 9659401 DOI: 10.1016/S0167-4838(98)00036-3 |
0.311 |
|
| 1997 |
Lee JK, Brandin E, Branton D, Goldstein LS. alpha-Spectrin is required for ovarian follicle monolayer integrity in Drosophila melanogaster. Development (Cambridge, England). 124: 353-62. PMID 9053311 |
0.537 |
|
| 1996 |
Lue RA, Brandin E, Chan EP, Branton D. Two independent domains of hDlg are sufficient for subcellular targeting: the PDZ1-2 conformational unit and an alternatively spliced domain. The Journal of Cell Biology. 135: 1125-37. PMID 8922391 DOI: 10.1083/Jcb.135.4.1125 |
0.33 |
|
| 1996 |
Viel A, Branton D. Spectrin: on the path from structure to function. Current Opinion in Cell Biology. 8: 49-55. PMID 8791400 DOI: 10.1016/S0955-0674(96)80048-2 |
0.359 |
|
| 1995 |
Zhang P, Talluri S, Deng H, Branton D, Wagner G. Solution structure of the pleckstrin homology domain of Drosophila beta-spectrin. Structure (London, England : 1993). 3: 1185-95. PMID 8591029 DOI: 10.1016/S0969-2126(01)00254-4 |
0.318 |
|
| 1995 |
Deng H, Lee JK, Goldstein LS, Branton D. Drosophila development requires spectrin network formation. The Journal of Cell Biology. 128: 71-9. PMID 7822424 DOI: 10.1083/Jcb.128.1.71 |
0.567 |
|
| 1995 |
Marfatia SM, Leu RA, Branton D, Chishti AH. Identification of the protein 4.1 binding interface on glycophorin C and p55, a homologue of the Drosophila discs-large tumor suppressor protein. The Journal of Biological Chemistry. 270: 715-9. PMID 7822301 DOI: 10.1074/jbc.270.2.715 |
0.601 |
|
| 1994 |
Viel A, Branton D. Interchain binding at the tail end of the Drosophila spectrin molecule. Proceedings of the National Academy of Sciences of the United States of America. 91: 10839-43. PMID 7971971 DOI: 10.1073/Pnas.91.23.10839 |
0.387 |
|
| 1994 |
Lue RA, Marfatia SM, Branton D, Chishti AH. Cloning and characterization of hdlg: the human homologue of the Drosophila discs large tumor suppressor binds to protein 4.1. Proceedings of the National Academy of Sciences of the United States of America. 91: 9818-22. PMID 7937897 DOI: 10.1073/pnas.91.21.9818 |
0.593 |
|
| 1993 |
Lee JK, Coyne RS, Dubreuil RR, Goldstein LS, Branton D. Cell shape and interaction defects in alpha-spectrin mutants of Drosophila melanogaster. The Journal of Cell Biology. 123: 1797-809. PMID 8276898 DOI: 10.1083/jcb.123.6.1797 |
0.761 |
|
| 1993 |
Yan Y, Winograd E, Viel A, Cronin T, Harrison SC, Branton D. Crystal structure of the repetitive segments of spectrin. Science (New York, N.Y.). 262: 2027-30. PMID 8266097 DOI: 10.1126/Science.8266097 |
0.365 |
|
| 1992 |
Byers TJ, Brandin E, Lue RA, Winograd E, Branton D. The complete sequence of Drosophila beta-spectrin reveals supra-motifs comprising eight 106-residue segments. Proceedings of the National Academy of Sciences of the United States of America. 89: 6187-91. PMID 1631106 DOI: 10.1073/pnas.89.13.6187 |
0.334 |
|
| 1992 |
Svoboda K, Schmidt CF, Branton D, Block SM. Conformation and elasticity of the isolated red blood cell membrane skeleton. Biophysical Journal. 63: 784-93. PMID 1420914 DOI: 10.1016/S0006-3495(92)81644-2 |
0.318 |
|
| 1991 |
Dubreuil RR, Brandin E, Reisberg JH, Goldstein LS, Branton D. Structure, calmodulin-binding, and calcium-binding properties of recombinant alpha spectrin polypeptides. The Journal of Biological Chemistry. 266: 7189-93. PMID 2016322 |
0.771 |
|
| 1991 |
Winograd E, Hume D, Branton D. Phasing the conformational unit of spectrin. Proceedings of the National Academy of Sciences of the United States of America. 88: 10788-91. PMID 1961746 DOI: 10.1073/Pnas.88.23.10788 |
0.353 |
|
| 1989 |
Dubreuil RR, Byers TJ, Sillman AL, Bar-Zvi D, Goldstein LS, Branton D. The complete sequence of Drosophila alpha-spectrin: conservation of structural domains between alpha-spectrins and alpha-actinin. The Journal of Cell Biology. 109: 2197-205. PMID 2808524 DOI: 10.1083/Jcb.109.5.2197 |
0.761 |
|
| 1989 |
Byers TJ, Husain-Chishti A, Dubreuil RR, Branton D, Goldstein LS. Sequence similarity of the amino-terminal domain of Drosophila beta spectrin to alpha actinin and dystrophin. The Journal of Cell Biology. 109: 1633-41. PMID 2677025 DOI: 10.1083/Jcb.109.4.1633 |
0.762 |
|
| 1989 |
Pesacreta TC, Byers TJ, Dubreuil R, Kiehart DP, Branton D. Drosophila spectrin: the membrane skeleton during embryogenesis. The Journal of Cell Biology. 108: 1697-709. PMID 2497103 DOI: 10.1083/Jcb.108.5.1697 |
0.752 |
|
| 1988 |
Husain-Chishti A, Levin A, Branton D. Abolition of actin-bundling by phosphorylation of human erythrocyte protein 4.9. Nature. 334: 718-21. PMID 2842686 DOI: 10.1038/334718a0 |
0.323 |
|
| 1987 |
Dubreuil R, Byers TJ, Branton D, Goldstein LS, Kiehart DP. Drosophilia spectrin. I. Characterization of the purified protein. The Journal of Cell Biology. 105: 2095-102. PMID 3680372 DOI: 10.1083/Jcb.105.5.2095 |
0.75 |
|
| 1987 |
Byers TJ, Dubreuil R, Branton D, Kiehart DP, Goldstein LS. Drosophila spectrin. II. Conserved features of the alpha-subunit are revealed by analysis of cDNA clones and fusion proteins. The Journal of Cell Biology. 105: 2103-10. PMID 2824526 DOI: 10.1083/Jcb.105.5.2103 |
0.767 |
|
| 1986 |
Elgsaeter A, Stokke BT, Mikkelsen A, Branton D. The molecular basis of erythrocyte shape. Science (New York, N.Y.). 234: 1217-23. PMID 3775380 DOI: 10.1126/Science.3775380 |
0.354 |
|
| 1985 |
Siegel DL, Branton D. Partial purification and characterization of an actin-bundling protein, band 4.9, from human erythrocytes. The Journal of Cell Biology. 100: 775-85. PMID 3882722 DOI: 10.1083/Jcb.100.3.775 |
0.301 |
|
| 1985 |
Byers TJ, Branton D. Visualization of the protein associations in the erythrocyte membrane skeleton. Proceedings of the National Academy of Sciences of the United States of America. 82: 6153-7. PMID 3862123 DOI: 10.1073/Pnas.82.18.6153 |
0.358 |
|
| 1982 |
Cohen CM, Branton D, Tyler J. Mapping functional sites on biological macromolecules. Ultramicroscopy. 8: 185-90. PMID 6211811 DOI: 10.1016/0304-3991(82)90287-X |
0.356 |
|
| 1981 |
Unanue ER, Ungewickell E, Branton D. The binding of clathrin triskelions to membranes from coated vesicles. Cell. 26: 439-46. PMID 7034962 DOI: 10.1016/0092-8674(81)90213-0 |
0.332 |
|
| 1981 |
Luna EJ, Fowler VM, Swanson J, Branton D, Taylor DL. A membrane cytoskeleton from Dictyostelium discoideum. I. Identification and partial characterization of an actin-binding activity. The Journal of Cell Biology. 88: 396-409. PMID 6894148 DOI: 10.1083/Jcb.88.2.396 |
0.602 |
|
| 1981 |
Fowler VM, Luna EJ, Hargreaves WR, Taylor DL, Branton D. Spectrin promotes the association of F-actin with the cytoplasmic surface of the human erythrocyte membrane. The Journal of Cell Biology. 88: 388-95. PMID 6894147 DOI: 10.1083/Jcb.88.2.388 |
0.563 |
|
| 1981 |
Branton D, Cohen CM, Tyler J. Interaction of cytoskeletal proteins on the human erythrocyte membrane. Cell. 24: 24-32. PMID 6453651 DOI: 10.1016/0092-8674(81)90497-9 |
0.329 |
|
| 1980 |
Cohen CM, Kramer RM, Branton D. Transbilayer mapping of membrane proteins using membranes isolated on polylysine-coated polyacrylamide beads. Biochimica Et Biophysica Acta. 597: 29-40. PMID 7370245 DOI: 10.1016/0005-2736(80)90147-9 |
0.345 |
|
| 1979 |
Kramer RM, Branton D. Retention of lipid asymmetry in membranes on polylysine-coated polyacrylamide beads. Biochimica Et Biophysica Acta. 556: 219-32. PMID 534625 DOI: 10.1016/0005-2736(79)90044-0 |
0.328 |
|
| 1979 |
Shotton DM, Burke BE, Branton D. The molecular structure of human erythrocyte spectrin. Biophysical and electron microscopic studies. Journal of Molecular Biology. 131: 303-29. PMID 490648 DOI: 10.1016/0022-2836(79)90078-0 |
0.325 |
|
| 1979 |
Cohen CM, Branton D. The role of spectrin in erythrocyte membrane-stimulated actin polymerisation. Nature. 279: 163-5. PMID 440423 DOI: 10.1038/279163A0 |
0.341 |
|
| 1979 |
Tyler JM, Hargreaves WR, Branton D. Purification of two spectrin-binding proteins: biochemical and electron microscopic evidence for site-specific reassociation between spectrin and bands 2.1 and 4.1. Proceedings of the National Academy of Sciences of the United States of America. 76: 5192-6. PMID 291934 DOI: 10.1073/Pnas.76.10.5192 |
0.337 |
|
| 1978 |
Shotton D, Thompson K, Wofsy L, Branton D. Appearance and distribution of surface proteins of the human erythrocyte membrane. An electron microscope and immunochemical labeling study. The Journal of Cell Biology. 76: 512-31. PMID 10605454 DOI: 10.1083/Jcb.76.2.512 |
0.346 |
|
| 1978 |
Cohen CM, Jackson PL, Branton D. Actin--membrane interactions: association of G-actin with the red cell membrane. Journal of Supramolecular Structure. 9: 113-24. PMID 732309 DOI: 10.1002/Jss.400090111 |
0.32 |
|
| 1978 |
Goodman SR, Branton D. Spectrin binding and the control of membrane protein mobility. Journal of Supramolecular Structure. 8: 455-63. PMID 723278 DOI: 10.1002/jss.400080408 |
0.38 |
|
| 1978 |
Shotton D, Burke B, Branton D. The shape of spectrin molecules from human erythrocyte membranes. Biochimica Et Biophysica Acta. 536: 313-7. PMID 708771 DOI: 10.1016/0005-2795(78)90079-X |
0.342 |
|
| 1978 |
Kalish DI, Cohen CM, Jacobson BS, Branton D. Membrane isolation on polylysine-coated glass beads. Asymmetry of bound membrane. Biochimica Et Biophysica Acta. 506: 97-110. PMID 620024 DOI: 10.1016/0005-2736(78)90437-6 |
0.326 |
|
| 1978 |
Jacobson BS, Cronin J, Branton D. Coupling polylysine to glass beads for plasma membrane isolation. Biochimica Et Biophysica Acta. 506: 81-96. PMID 620023 DOI: 10.1016/0005-2736(78)90436-4 |
0.32 |
|
| 1977 |
Fowler V, Branton D. Lateral mobility of human erythrocyte integral membrane proteins. Nature. 268: 23-6. PMID 887143 DOI: 10.1038/268023A0 |
0.582 |
|
| 1977 |
Jacobson BS, Branton D. Plasma membrane: rapid isolation and exposure of the cytoplasmic surface by use of positively charged beads. Science (New York, N.Y.). 195: 302-4. PMID 831278 DOI: 10.1126/Science.831278 |
0.327 |
|
| 1977 |
Cohen CM, Kalish DI, Jacobson BS, Branton D. Membrane isolation on polylysine-coated beads. Plasma membrane from HeLa cells. The Journal of Cell Biology. 75: 119-34. PMID 21192 DOI: 10.1083/Jcb.75.1.119 |
0.335 |
|
| 1977 |
Bennett V, Branton D. Selective association of spectrin with the cytoplasmic surface of human erythrocyte plasma membranes. Quantitative determination with purified (32P)spectrin. The Journal of Biological Chemistry. 252: 2753-63. PMID 15998 |
0.507 |
|
| 1976 |
Yu J, Branton D. Reconstitution of intramembrane particles in recombinants of erythrocyte protein band 3 and lipid: effects of spectrin-actin association. Proceedings of the National Academy of Sciences of the United States of America. 73: 3891-5. PMID 1069273 DOI: 10.1073/Pnas.73.11.3891 |
0.32 |
|
| 1976 |
Elgsaeter A, Shotton DM, Branton D. Intramembrane particle aggregation in erythrocyte ghosts. II. The influence of spectrin aggregation. Biochimica Et Biophysica Acta. 426: 101-22. PMID 2324 DOI: 10.1016/0005-2736(76)90433-8 |
0.313 |
|
| 1975 |
Branton D, Bullivant S, Gilula NB, Karnovsky MJ, Moor H, Mühlethaler K, Northcote DH, Packer L, Satir B, Satir P, Speth V, Staehlin LA, Steere RL, Weinstein RS. Freeze-etching nomenclature. Science (New York, N.Y.). 190: 54-6. PMID 1166299 DOI: 10.1126/Science.1166299 |
0.724 |
|
| 1973 |
James R, Branton D. Lipid- and temperature-dependent structural changes in Acholeplasma laidlawii cell membranes. Biochimica Et Biophysica Acta. 323: 378-90. PMID 4357019 DOI: 10.1016/0005-2736(73)90183-1 |
0.309 |
|
| 1971 |
Waaland JR, Waaland SD, Branton D. Gas vacuoles. Light shielding in blue-green algae. The Journal of Cell Biology. 48: 212-5. PMID 4993483 DOI: 10.1083/jcb.48.1.212 |
0.633 |
|
| 1970 |
Gilula NB, Branton D, Satir P. The septate junction: a structural basis for intercellular coupling. Proceedings of the National Academy of Sciences of the United States of America. 67: 213-20. PMID 5272312 DOI: 10.1073/Pnas.67.1.213 |
0.321 |
|
| 1970 |
Pinto da Silva P, Branton D. Membrane splitting in freeze-ethching. Covalently bound ferritin as a membrane marker. The Journal of Cell Biology. 45: 598-605. PMID 4918216 DOI: 10.1083/Jcb.45.3.598 |
0.317 |
|
| 1970 |
Tourtellotte ME, Branton D, Keith A. Membrane structure: spin labeling and freeze etching of Mycoplasma laidawii. Proceedings of the National Academy of Sciences of the United States of America. 66: 909-16. PMID 4316683 DOI: 10.1073/Pnas.66.3.909 |
0.314 |
|
| 1969 |
Waaland JR, Branton D. Gas vacuole development in a blue-green alga. Science (New York, N.Y.). 163: 1339-41. PMID 17807814 DOI: 10.1126/science.163.3873.1339 |
0.657 |
|
| 1967 |
Branton D, Park RB. Subunits in chloroplast lamellae. Journal of Ultrastructure Research. 19: 283-303. PMID 4167849 DOI: 10.1016/S0022-5320(67)80222-3 |
0.316 |
|
| 1962 |
Branton D, Jacobson L. Iron Localization in Pea Plants. Plant Physiology. 37: 546-51. PMID 16655692 DOI: 10.1104/Pp.37.4.546 |
0.491 |
|
| 1962 |
Branton D, Jacobson L. Iron Transport in Pea Plants. Plant Physiology. 37: 539-45. PMID 16655691 DOI: 10.1104/Pp.37.4.539 |
0.486 |
|
| 1962 |
BRANTON D, JACOBSON L. Dry, high resolution autoradiography. Stain Technology. 37: 239-42. PMID 13872530 DOI: 10.3109/10520296209117744 |
0.512 |
|
| 1961 |
Branton D, Jacobson L. Freeze-drying of plant material Experimental Cell Research. 22: 559-568. DOI: 10.1016/0014-4827(61)90132-X |
0.494 |
|
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