Year |
Citation |
Score |
2023 |
Bremer KV, Wu C, Patel AA, He KL, Grunfeld AM, Chanfreau GF, Quinlan ME. Formin tails act as a switch, inhibiting or enhancing processive actin elongation. The Journal of Biological Chemistry. 300: 105557. PMID 38097186 DOI: 10.1016/j.jbc.2023.105557 |
0.337 |
|
2021 |
Valencia DA, Quinlan ME. Formins. Current Biology : Cb. 31: R517-R522. PMID 34033783 DOI: 10.1016/j.cub.2021.02.047 |
0.433 |
|
2019 |
Bradley AO, Vizcarra CL, Bailey HM, Quinlan ME. Spire stimulates nucleation by Cappuccino and binds both ends of actin filaments. Molecular Biology of the Cell. mbcE19090550. PMID 31877067 DOI: 10.1091/Mbc.E19-09-0550 |
0.488 |
|
2018 |
Kudryashova E, Heisler DB, Williams B, Harker AJ, Shafer K, Quinlan ME, Kovar DR, Vavylonis D, Kudryashov DS. Actin Cross-Linking Toxin Is a Universal Inhibitor of Tandem-Organized and Oligomeric G-Actin Binding Proteins. Current Biology : Cb. PMID 29731300 DOI: 10.1016/J.Cub.2018.03.065 |
0.544 |
|
2018 |
Patel AA, Oztug Durer ZA, van Loon AP, Bremer KV, Quinlan ME. The Drosophila Formin FHOD Nucleates Actin Filaments Biophysical Journal. 114: 144a-145a. DOI: 10.1016/J.Bpj.2017.11.811 |
0.507 |
|
2018 |
Quinlan ME. Cytoskeletal Control of Cell Polarity in the Drosophila Oocyte Biophysical Journal. 114: 9a. DOI: 10.1016/J.Bpj.2017.11.089 |
0.369 |
|
2017 |
Silkworth WT, Kunes KL, Nickel GC, Phillips ML, Quinlan ME, Vizcarra CL. The Neuron Specific Formin Delphilin Nucleates Non-Muscle Actin but Does Not Enhance Elongation. Molecular Biology of the Cell. PMID 29282276 DOI: 10.1091/Mbc.E17-06-0363 |
0.473 |
|
2017 |
Patel AA, Oztug Durer ZA, van Loon AP, Bremer KV, Quinlan ME. Drosophila and human FHOD family formins nucleate actin filaments. The Journal of Biological Chemistry. PMID 29127202 DOI: 10.1074/Jbc.M117.800888 |
0.525 |
|
2017 |
Vizcarra CL, Quinlan ME. Actin filament assembly by bacterial factors VopL/F: Which end is up? The Journal of Cell Biology. PMID 28416477 DOI: 10.1083/Jcb.201702165 |
0.456 |
|
2016 |
Quinlan ME. Cytoplasmic Streaming in the Drosophila Oocyte. Annual Review of Cell and Developmental Biology. PMID 27362645 DOI: 10.1146/Annurev-Cellbio-111315-125416 |
0.32 |
|
2015 |
Oztug Durer ZA, McGillivary RM, Kang H, Elam WA, Vizcarra CL, Hanein D, De La Cruz EM, Reisler E, Quinlan ME. Metavinculin Tunes the Flexibility and the Architecture of Vinculin-Induced Bundles of Actin Filaments. Journal of Molecular Biology. 427: 2782-98. PMID 26168869 DOI: 10.1016/J.Jmb.2015.07.005 |
0.565 |
|
2015 |
Yoo H, Roth-Johnson EA, Bor B, Quinlan ME. Drosophila Cappuccino alleles provide insight into formin mechanism and role in oogenesis. Molecular Biology of the Cell. 26: 1875-86. PMID 25788286 DOI: 10.1091/Mbc.E14-11-1558 |
0.486 |
|
2015 |
Bor B, Bois JS, Quinlan ME. Regulation of the formin Cappuccino is critical for polarity of Drosophila oocytes. Cytoskeleton (Hoboken, N.J.). 72: 1-15. PMID 25557988 DOI: 10.1002/Cm.21205 |
0.415 |
|
2015 |
Fattouh R, Kwon H, Czuczman MA, Copeland JW, Pelletier L, Quinlan ME, Muise AM, Higgins DE, Brumell JH. The diaphanous-related formins promote protrusion formation and cell-to-cell spread of Listeria monocytogenes. The Journal of Infectious Diseases. 211: 1185-95. PMID 25281757 DOI: 10.1093/Infdis/Jiu546 |
0.341 |
|
2015 |
Rasson AS, Bois JS, Pham DS, Yoo H, Quinlan ME. Filament assembly by Spire: key residues and concerted actin binding. Journal of Molecular Biology. 427: 824-39. PMID 25234086 DOI: 10.1016/J.Jmb.2014.09.002 |
0.457 |
|
2015 |
Quinlan M. Two Types of Actin Nucleators, Three Ways to Make Actin Filaments? Biophysical Journal. 108: 188a. DOI: 10.1016/J.Bpj.2014.11.1041 |
0.499 |
|
2014 |
Vizcarra CL, Bor B, Quinlan ME. The role of formin tails in actin nucleation, processive elongation, and filament bundling. The Journal of Biological Chemistry. 289: 30602-13. PMID 25246531 DOI: 10.1074/Jbc.M114.588368 |
0.477 |
|
2014 |
Roth-Johnson EA, Vizcarra CL, Bois JS, Quinlan ME. Interaction between microtubules and the Drosophila formin Cappuccino and its effect on actin assembly. The Journal of Biological Chemistry. 289: 4395-404. PMID 24362037 DOI: 10.1074/Jbc.M113.499921 |
0.514 |
|
2014 |
Durer ZA, Vizcarra C, McGillivary RA, Hanein D, Reisler E, Quinlan ME. Metavinculin Induced Changes at the Actin Interprotomer Contacts and the Mechanism of Resulting Severing Biophysical Journal. 106: 164a. DOI: 10.1016/J.Bpj.2013.11.935 |
0.536 |
|
2013 |
Quinlan ME. Direct interaction between two actin nucleators is required in Drosophila oogenesis. Development (Cambridge, England). 140: 4417-25. PMID 24089467 DOI: 10.1242/Jcs.143909 |
0.473 |
|
2012 |
Bor B, Vizcarra CL, Phillips ML, Quinlan ME. Autoinhibition of the formin Cappuccino in the absence of canonical autoinhibitory domains. Molecular Biology of the Cell. 23: 3801-13. PMID 22875983 DOI: 10.1091/Mbc.E12-04-0288 |
0.352 |
|
2012 |
Beausang JF, Sun Y, Quinlan ME, Forkey JN, Goldman YE. The polarized total internal reflection fluorescence microscopy (polTIRFM) processive motility assay for myosin V. Cold Spring Harbor Protocols. 2012: 716-8. PMID 22661446 DOI: 10.1101/Pdb.Prot069393 |
0.817 |
|
2012 |
Beausang JF, Sun Y, Quinlan ME, Forkey JN, Goldman YE. Construction of flow chambers for polarized total internal reflection fluorescence microscopy (polTIRFM) motility assays. Cold Spring Harbor Protocols. 2012: 712-5. PMID 22661445 DOI: 10.1101/Pdb.Prot069385 |
0.755 |
|
2012 |
Beausang JF, Sun Y, Quinlan ME, Forkey JN, Goldman YE. The acquisition and analysis of polarized total internal reflection fluorescence microscopy (polTIRFM) data. Cold Spring Harbor Protocols. 2012: 722-5. PMID 22661430 DOI: 10.1101/Pdb.Prot069419 |
0.792 |
|
2012 |
Beausang JF, Sun Y, Quinlan ME, Forkey JN, Goldman YE. The polarized total internal reflection fluorescence microscopy (polTIRFM) twirling filament assay. Cold Spring Harbor Protocols. 2012: 719-21. PMID 22661429 DOI: 10.1101/Pdb.Prot069401 |
0.816 |
|
2012 |
Beausang JF, Sun Y, Quinlan ME, Forkey JN, Goldman YE. Preparation of filamentous actin for polarized total internal reflection fluorescence microscopy (polTIRFM) motility assays. Cold Spring Harbor Protocols. 2012. PMID 22550306 DOI: 10.1101/Pdb.Prot069377 |
0.799 |
|
2012 |
Beausang JF, Sun Y, Quinlan ME, Forkey JN, Goldman YE. Fluorescent labeling of myosin V for polarized total internal reflection fluorescence microscopy (polTIRFM) motility assays. Cold Spring Harbor Protocols. 2012. PMID 22550305 DOI: 10.1101/Pdb.Prot069369 |
0.801 |
|
2012 |
Beausang JF, Sun Y, Quinlan ME, Forkey JN, Goldman YE. Fluorescent labeling of calmodulin with bifunctional rhodamine. Cold Spring Harbor Protocols. 2012. PMID 22550304 DOI: 10.1101/Pdb.Prot069351 |
0.775 |
|
2012 |
Beausang JF, Sun Y, Quinlan ME, Forkey JN, Goldman YE. Orientation and rotational motions of single molecules by polarized total internal reflection fluorescence microscopy (polTIRFM). Cold Spring Harbor Protocols. 2012. PMID 22550303 DOI: 10.1101/Pdb.Top069344 |
0.793 |
|
2012 |
Chen CK, Sawaya MR, Phillips ML, Reisler E, Quinlan ME. Multiple forms of Spire-actin complexes and their functional consequences. The Journal of Biological Chemistry. 287: 10684-92. PMID 22334675 DOI: 10.1074/Jbc.M111.317792 |
0.491 |
|
2011 |
Vizcarra CL, Kreutz B, Rodal AA, Toms AV, Lu J, Zheng W, Quinlan ME, Eck MJ. Structure and function of the interacting domains of Spire and Fmn-family formins. Proceedings of the National Academy of Sciences of the United States of America. 108: 11884-9. PMID 21730168 DOI: 10.1073/Pnas.1105703108 |
0.373 |
|
2009 |
Zuchero JB, Coutts AS, Quinlan ME, Thangue NB, Mullins RD. p53-cofactor JMY is a multifunctional actin nucleation factor. Nature Cell Biology. 11: 451-9. PMID 19287377 DOI: 10.1038/Ncb1852 |
0.755 |
|
2008 |
Quinlan ME, Kerkhoff E. Actin nucleation: bacteria get in-Spired. Nature Cell Biology. 10: 13-5. PMID 18172428 DOI: 10.1038/Ncb0108-13 |
0.487 |
|
2007 |
Quinlan ME, Hilgert S, Bedrossian A, Mullins RD, Kerkhoff E. Regulatory interactions between two actin nucleators, Spire and Cappuccino. The Journal of Cell Biology. 179: 117-28. PMID 17923532 DOI: 10.1083/Jcb.200706196 |
0.661 |
|
2005 |
Rosenberg SA, Quinlan ME, Forkey JN, Goldman YE. Rotational motions of macro-molecules by single-molecule fluorescence microscopy. Accounts of Chemical Research. 38: 583-93. PMID 16028893 DOI: 10.1021/Ar040137K |
0.683 |
|
2005 |
Forkey JN, Quinlan ME, Goldman YE. Measurement of single macromolecule orientation by total internal reflection fluorescence polarization microscopy. Biophysical Journal. 89: 1261-71. PMID 15894632 DOI: 10.1529/Biophysj.104.053470 |
0.676 |
|
2005 |
Quinlan ME, Forkey JN, Goldman YE. Orientation of the myosin light chain region by single molecule total internal reflection fluorescence polarization microscopy. Biophysical Journal. 89: 1132-42. PMID 15894631 DOI: 10.1529/Biophysj.104.053496 |
0.731 |
|
2005 |
Quinlan ME, Heuser JE, Kerkhoff E, Mullins RD. Drosophila Spire is an actin nucleation factor. Nature. 433: 382-8. PMID 15674283 DOI: 10.1038/Nature03241 |
0.7 |
|
2003 |
Forkey JN, Quinlan ME, Shaw MA, Corrie JE, Goldman YE. Three-dimensional structural dynamics of myosin V by single-molecule fluorescence polarization. Nature. 422: 399-404. PMID 12660775 DOI: 10.1038/Nature01529 |
0.704 |
|
2001 |
Quinlan ME, Forkey JN, Goldman YE. Kinesin-ADP: whole lotta shakin' goin' on. Nature Structural Biology. 8: 478-80. PMID 11373608 DOI: 10.1038/88522 |
0.669 |
|
2000 |
Forkey JN, Quinlan ME, Goldman YE. Protein structural dynamics by single-molecule fluorescence polarization. Progress in Biophysics and Molecular Biology. 74: 1-35. PMID 11106805 DOI: 10.1016/S0079-6107(00)00015-8 |
0.683 |
|
1999 |
Forkey JN, Quinlan ME, Corrie JET, Goldman YE. Single molecule polarization microscopy for investigating real time structural dynamics of biological macromolecules Annual International Conference of the Ieee Engineering in Medicine and Biology - Proceedings. 1: 77. |
0.591 |
|
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