Year |
Citation |
Score |
2024 |
DAmico KA, Stanton AE, Shirkey JD, Travis SM, Jeffrey PD, Hughson FM. Structure of a membrane tethering complex incorporating multiple SNAREs. Nature Structural & Molecular Biology. PMID 38196032 DOI: 10.1038/s41594-023-01164-8 |
0.499 |
|
2023 |
Stanton AE, Hughson FM. The machinery of vesicle fusion. Current Opinion in Cell Biology. 83: 102191. PMID 37421936 DOI: 10.1016/j.ceb.2023.102191 |
0.438 |
|
2023 |
DAmico KA, Stanton AE, Shirkey JD, Travis SM, Jeffrey PD, Hughson FM. Structure of a Membrane Tethering Complex Incorporating Multiple SNAREs. Biorxiv : the Preprint Server For Biology. PMID 36778436 DOI: 10.1101/2023.01.30.526244 |
0.49 |
|
2021 |
Zhang Y, Hughson FM. Chaperoning SNARE Folding and Assembly. Annual Review of Biochemistry. PMID 33823650 DOI: 10.1146/annurev-biochem-081820-103615 |
0.385 |
|
2020 |
Wong S, Hepowit NL, Port SA, Yau RG, Peng Y, Azad N, Habib A, Harpaz N, Schuldiner M, Hughson FM, MacGurn JA, Weisman LS. Cargo Release from Myosin V Requires the Convergence of Parallel Pathways that Phosphorylate and Ubiquitylate the Cargo Adaptor. Current Biology : Cb. PMID 32916113 DOI: 10.1016/J.Cub.2020.08.062 |
0.414 |
|
2020 |
Eisemann TJ, Allen F, Lau K, Shimamura GR, Jeffrey PD, Hughson FM. The Sec1/Munc18 protein Vps45 holds the Qa-SNARE Tlg2 in an open conformation. Elife. 9. PMID 32804076 DOI: 10.7554/Elife.60724 |
0.587 |
|
2020 |
Travis SM, DAmico K, Yu IM, McMahon C, Hamid S, Ramirez-Arellano G, Jeffrey PD, Hughson FM. Structural basis for the binding of SNAREs to the multisubunit tethering complex Dsl1. The Journal of Biological Chemistry. PMID 32409579 DOI: 10.1074/Jbc.Ra120.013654 |
0.81 |
|
2020 |
Eisemann TJ, Allen F, Lau K, Shimamura GR, Jeffrey PD, Hughson FM. Author response: The Sec1/Munc18 protein Vps45 holds the Qa-SNARE Tlg2 in an open conformation Elife. DOI: 10.7554/Elife.60724.Sa2 |
0.347 |
|
2019 |
Travis SM, Kokona B, Fairman R, Hughson FM. Roles of singleton tryptophan motifs in COPI coat stability and vesicle tethering. Proceedings of the National Academy of Sciences of the United States of America. PMID 31712447 DOI: 10.2210/Pdb6Tzt/Pdb |
0.677 |
|
2019 |
Paczkowski JE, McCready AR, Cong JP, Li Z, Jeffrey PD, Smith CD, Henke BR, Hughson FM, Bassler BL. An autoinducer analog reveals an alternative mode of ligand binding for the LasR quorum-sensing receptor. Acs Chemical Biology. PMID 30763066 DOI: 10.1021/Acschembio.8B00971 |
0.327 |
|
2019 |
Jiao J, He M, Port S, Richard B, Xu Y, Qu H, Xiong Y, Wang Y, Jin H, Eisemann T, Hughson FM, Zhang Y. Sec1/Munc18-Family Proteins Catalyze Directional SNARE Assembly by Templating SNARE Folding and Association Biophysical Journal. 116: 527a. DOI: 10.1016/J.Bpj.2018.11.2842 |
0.373 |
|
2018 |
Jiao J, He M, Port SA, Baker RW, Xu Y, Qu H, Xiong Y, Wang Y, Jin H, Eisemann TJ, Hughson FM, Zhang Y. Munc18-1 catalyzes neuronal SNARE assembly by templating SNARE association. Elife. 7. PMID 30540253 DOI: 10.7554/Elife.41771 |
0.561 |
|
2017 |
Hughson F. Know when to Hold ‘Em, Know when to Fold ‘Em; SM Proteins as Templates for SNARE Assembly Biophysical Journal. 112: 158a. DOI: 10.1016/J.Bpj.2016.11.871 |
0.559 |
|
2016 |
Ha JY, Chou HT, Ungar D, Yip CK, Walz T, Hughson FM. Molecular architecture of the complete COG tethering complex. Nature Structural & Molecular Biology. PMID 27428773 DOI: 10.1038/Nsmb.3263 |
0.45 |
|
2016 |
Baker RW, Hughson FM. Chaperoning SNARE assembly and disassembly. Nature Reviews. Molecular Cell Biology. PMID 27301672 DOI: 10.1038/Nrm.2016.65 |
0.54 |
|
2016 |
Boyaci H, Shah T, Hurley A, Kokona B, Li Z, Ventocilla C, Jeffrey PD, Semmelhack MF, Fairman R, Bassler BL, Hughson FM. Structure, Regulation, and Inhibition of the Quorum-Sensing Signal Integrator LuxO. Plos Biology. 14: e1002464. PMID 27219477 DOI: 10.1371/Journal.Pbio.1002464 |
0.652 |
|
2015 |
Suckling RJ, Poon PP, Travis SM, Majoul IV, Hughson FM, Evans PR, Duden R, Owen DJ. Structural basis for the binding of tryptophan-based motifs by δ-COP. Proceedings of the National Academy of Sciences of the United States of America. 112: 14242-7. PMID 26578768 DOI: 10.1073/Pnas.1506186112 |
0.433 |
|
2015 |
Baker RW, Jeffrey PD, Zick M, Phillips BP, Wickner WT, Hughson FM. A direct role for the Sec1/Munc18-family protein Vps33 as a template for SNARE assembly. Science (New York, N.Y.). 349: 1111-4. PMID 26339030 DOI: 10.1126/Science.Aac7906 |
0.571 |
|
2014 |
Ha JY, Pokrovskaya ID, Climer LK, Shimamura GR, Kudlyk T, Jeffrey PD, Lupashin VV, Hughson FM. Cog5-Cog7 crystal structure reveals interactions essential for the function of a multisubunit tethering complex. Proceedings of the National Academy of Sciences of the United States of America. 111: 15762-7. PMID 25331899 DOI: 10.1073/Pnas.1414829111 |
0.555 |
|
2014 |
Rogers JV, McMahon C, Baryshnikova A, Hughson FM, Rose MD. ER-associated retrograde SNAREs and the Dsl1 complex mediate an alternative, Sey1p-independent homotypic ER fusion pathway. Molecular Biology of the Cell. 25: 3401-12. PMID 25187651 DOI: 10.1091/Mbc.E14-07-1220 |
0.74 |
|
2013 |
Bharucha N, Liu Y, Papanikou E, McMahon C, Esaki M, Jeffrey PD, Hughson FM, Glick BS. Sec16 influences transitional ER sites by regulating rather than organizing COPII. Molecular Biology of the Cell. 24: 3406-19. PMID 24006484 DOI: 10.1091/Mbc.E13-04-0185 |
0.737 |
|
2013 |
Baker RW, Jeffrey PD, Hughson FM. Crystal Structures of the Sec1/Munc18 (SM) Protein Vps33, Alone and Bound to the Homotypic Fusion and Vacuolar Protein Sorting (HOPS) Subunit Vps16* Plos One. 8: e67409. PMID 23840694 DOI: 10.1371/Journal.Pone.0067409 |
0.561 |
|
2013 |
Hughson FM. Neuroscience. Chaperones that SNARE neurotransmitter release. Science (New York, N.Y.). 339: 406-7. PMID 23349281 DOI: 10.1126/Science.1233801 |
0.426 |
|
2012 |
McMahon C, Studer SM, Clendinen C, Dann GP, Jeffrey PD, Hughson FM. The structure of Sec12 implicates potassium ion coordination in Sar1 activation. The Journal of Biological Chemistry. 287: 43599-606. PMID 23109340 DOI: 10.1074/Jbc.M112.420141 |
0.767 |
|
2011 |
Chen G, Swem LR, Swem DL, Stauff DL, O'Loughlin CT, Jeffrey PD, Bassler BL, Hughson FM. A strategy for antagonizing quorum sensing. Molecular Cell. 42: 199-209. PMID 21504831 DOI: 10.1016/J.Molcel.2011.04.003 |
0.386 |
|
2010 |
Lees JA, Yip CK, Walz T, Hughson FM. Molecular organization of the COG vesicle tethering complex. Nature Structural & Molecular Biology. 17: 1292-7. PMID 20972446 DOI: 10.1038/Nsmb.1917 |
0.705 |
|
2010 |
Hughson FM. Copy coats: COPI mimics clathrin and COPII. Cell. 142: 19-21. PMID 20603010 DOI: 10.1016/J.Cell.2010.06.031 |
0.376 |
|
2010 |
Ren Q, Wimmer C, Chicka MC, Ye S, Ren Y, Hughson FM, Whiteheart SW. Munc13-4 is a limiting factor in the pathway required for platelet granule release and hemostasis. Blood. 116: 869-77. PMID 20435885 DOI: 10.1182/Blood-2010-02-270934 |
0.428 |
|
2010 |
Hughson FM, Reinisch KM. Structure and mechanism in membrane trafficking. Current Opinion in Cell Biology. 22: 454-60. PMID 20418086 DOI: 10.1016/J.Ceb.2010.03.011 |
0.738 |
|
2010 |
Yen WL, Shintani T, Nair U, Cao Y, Richardson BC, Li Z, Hughson FM, Baba M, Klionsky DJ. The conserved oligomeric Golgi complex is involved in double-membrane vesicle formation during autophagy. The Journal of Cell Biology. 188: 101-14. PMID 20065092 DOI: 10.1083/Jcb.200904075 |
0.738 |
|
2010 |
Yu IM, Hughson FM. Tethering factors as organizers of intracellular vesicular traffic. Annual Review of Cell and Developmental Biology. 26: 137-56. PMID 19575650 DOI: 10.1146/Annurev.Cellbio.042308.113327 |
0.444 |
|
2009 |
Ren Y, Yip CK, Tripathi A, Huie D, Jeffrey PD, Walz T, Hughson FM. A structure-based mechanism for vesicle capture by the multisubunit tethering complex Dsl1. Cell. 139: 1119-29. PMID 20005805 DOI: 10.1016/J.Cell.2009.11.002 |
0.746 |
|
2009 |
Kelly RC, Bolitho ME, Higgins DA, Lu W, Ng WL, Jeffrey PD, Rabinowitz JD, Semmelhack MF, Hughson FM, Bassler BL. The Vibrio cholerae quorum-sensing autoinducer CAI-1: analysis of the biosynthetic enzyme CqsA. Nature Chemical Biology. 5: 891-5. PMID 19838203 DOI: 10.1038/Nchembio.237 |
0.613 |
|
2009 |
Richardson BC, Smith RD, Ungar D, Nakamura A, Jeffrey PD, Lupashin VV, Hughson FM. Structural basis for a human glycosylation disorder caused by mutation of the COG4 gene. Proceedings of the National Academy of Sciences of the United States of America. 106: 13329-34. PMID 19651599 DOI: 10.1073/Pnas.0901966106 |
0.733 |
|
2009 |
Tripathi A, Ren Y, Jeffrey PD, Hughson FM. Structural characterization of Tip20p and Dsl1p, subunits of the Dsl1p vesicle tethering complex. Nature Structural & Molecular Biology. 16: 114-23. PMID 19151722 DOI: 10.1038/Nsmb.1548 |
0.742 |
|
2007 |
Neiditch MB, Hughson FM. The regulation of histidine sensor kinase complexes by quorum sensing signal molecules. Methods in Enzymology. 423: 250-63. PMID 17609135 DOI: 10.1016/S0076-6879(07)23011-3 |
0.335 |
|
2007 |
Cavanaugh LF, Chen X, Richardson BC, Ungar D, Pelczer I, Rizo J, Hughson FM. Structural analysis of conserved oligomeric Golgi complex subunit 2. The Journal of Biological Chemistry. 282: 23418-26. PMID 17565980 DOI: 10.1074/Jbc.M703716200 |
0.773 |
|
2007 |
Cavanaugh L, Chen X, Pelczer I, Rizo J, Hughson F. Solution structure of Saccharomyces cerevisiae conserved oligomeric Golgi subunit 2 protein (Cog2p) Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb2Jqq/Pdb |
0.742 |
|
2006 |
Togneri J, Cheng YS, Munson M, Hughson FM, Carr CM. Specific SNARE complex binding mode of the Sec1/Munc-18 protein, Sec1p. Proceedings of the National Academy of Sciences of the United States of America. 103: 17730-5. PMID 17090679 DOI: 10.1073/Pnas.0605448103 |
0.753 |
|
2006 |
Neiditch MB, Federle MJ, Pompeani AJ, Kelly RC, Swem DL, Jeffrey PD, Bassler BL, Hughson FM. Ligand-induced asymmetry in histidine sensor kinase complex regulates quorum sensing. Cell. 126: 1095-108. PMID 16990134 DOI: 10.1016/J.Cell.2006.07.032 |
0.669 |
|
2006 |
Ungar D, Oka T, Krieger M, Hughson FM. Retrograde transport on the COG railway. Trends in Cell Biology. 16: 113-20. PMID 16406524 DOI: 10.1016/J.Tcb.2005.12.004 |
0.436 |
|
2005 |
Oka T, Vasile E, Penman M, Novina CD, Dykxhoorn DM, Ungar D, Hughson FM, Krieger M. Genetic analysis of the subunit organization and function of the conserved oligomeric golgi (COG) complex: studies of COG5- and COG7-deficient mammalian cells. The Journal of Biological Chemistry. 280: 32736-45. PMID 16051600 DOI: 10.1074/Jbc.M505558200 |
0.446 |
|
2005 |
Ungar D, Oka T, Vasile E, Krieger M, Hughson FM. Subunit architecture of the conserved oligomeric Golgi complex. The Journal of Biological Chemistry. 280: 32729-35. PMID 16020545 DOI: 10.1074/Jbc.M504590200 |
0.459 |
|
2005 |
Neiditch MB, Federle MJ, Miller ST, Bassler BL, Hughson FM. Regulation of LuxPQ receptor activity by the quorum-sensing signal autoinducer-2. Molecular Cell. 18: 507-18. PMID 15916958 DOI: 10.1016/J.Molcel.2005.04.020 |
0.409 |
|
2004 |
Miller ST, Xavier KB, Campagna SR, Taga ME, Semmelhack MF, Bassler BL, Hughson FM. Salmonella typhimurium recognizes a chemically distinct form of the bacterial quorum-sensing signal AI-2. Molecular Cell. 15: 677-87. PMID 15350213 DOI: 10.1016/J.Molcel.2004.07.020 |
0.334 |
|
2004 |
Oka T, Ungar D, Hughson FM, Krieger M. The COG and COPI complexes interact to control the abundance of GEARs, a subset of Golgi integral membrane proteins. Molecular Biology of the Cell. 15: 2423-35. PMID 15004235 DOI: 10.1091/Mbc.E03-09-0699 |
0.482 |
|
2003 |
Zweifel ME, Leahy DJ, Hughson FM, Barrick D. Structure and stability of the ankyrin domain of the Drosophila Notch receptor. Protein Science : a Publication of the Protein Society. 12: 2622-32. PMID 14573873 DOI: 10.1110/Ps.03279003 |
0.606 |
|
2003 |
Ungar D, Hughson FM. SNARE protein structure and function. Annual Review of Cell and Developmental Biology. 19: 493-517. PMID 14570579 DOI: 10.1146/Annurev.Cellbio.19.110701.155609 |
0.552 |
|
2002 |
Chen X, Schauder S, Potier N, Van Dorsselaer A, Pelczer I, Bassler BL, Hughson FM. Structural identification of a bacterial quorum-sensing signal containing boron. Nature. 415: 545-9. PMID 11823863 DOI: 10.1038/415545A |
0.344 |
|
2002 |
Barrick D, Hughson FM. Irreversible assembly of membrane fusion machines. Nature Structural Biology. 9: 78-80. PMID 11813007 DOI: 10.1038/Nsb0202-78 |
0.631 |
|
2002 |
Munson M, Hughson FM. Conformational regulation of SNARE assembly and disassembly in vivo. The Journal of Biological Chemistry. 277: 9375-81. PMID 11777922 DOI: 10.1074/Jbc.M111729200 |
0.748 |
|
2000 |
Waters MG, Hughson FM. Membrane tethering and fusion in the secretory and endocytic pathways. Traffic (Copenhagen, Denmark). 1: 588-97. PMID 11208146 DOI: 10.1034/J.1600-0854.2000.010802.X |
0.53 |
|
2000 |
Munson M, Chen X, Cocina AE, Schultz SM, Hughson FM. Interactions within the yeast t-SNARE Sso1p that control SNARE complex assembly. Nature Structural Biology. 7: 894-902. PMID 11017200 DOI: 10.1038/79659 |
0.757 |
|
2000 |
Lerman JC, Robblee J, Fairman R, Hughson FM. Structural analysis of the neuronal SNARE protein syntaxin-1A. Biochemistry. 39: 8470-9. PMID 10913252 DOI: 10.1021/Bi0003994 |
0.802 |
|
1999 |
Carr CM, Grote E, Munson M, Hughson FM, Novick PJ. Sec1p binds to SNARE complexes and concentrates at sites of secretion. The Journal of Cell Biology. 146: 333-44. PMID 10427089 DOI: 10.1083/Jcb.146.2.333 |
0.748 |
|
1999 |
Hughson FM. Membrane fusion: structure snared at last. Current Biology : Cb. 9: R49-52. PMID 10021356 DOI: 10.1016/S0960-9822(99)80008-6 |
0.542 |
|
1998 |
Nicholson KL, Munson M, Miller RB, Filip TJ, Fairman R, Hughson FM. Regulation of SNARE complex assembly by an N-terminal domain of the t-SNARE Sso1p. Nature Structural Biology. 5: 793-802. PMID 9731774 DOI: 10.1038/1834 |
0.809 |
|
1997 |
Hughson FM. Enveloped viruses: a common mode of membrane fusion?. Current Biology : Cb. 7: R565-9. PMID 9285698 DOI: 10.1016/S0960-9822(06)00283-1 |
0.398 |
|
1997 |
Hughson FM. Penetrating insights into pore formation. Nature Structural Biology. 4: 89-92. PMID 9033582 DOI: 10.1038/Nsb0297-89 |
0.374 |
|
1995 |
Skehel JJ, Bizebard T, Bullough PA, Hughson FM, Knossow M, Steinhauer DA, Wharton SA, Wiley DC. Membrane fusion by influenza hemagglutinin. Cold Spring Harbor Symposia On Quantitative Biology. 60: 573-80. PMID 8824430 |
0.52 |
|
1995 |
Chen J, Wharton SA, Weissenhorn W, Calder LJ, Hughson FM, Skehel JJ, Wiley DC. A soluble domain of the membrane-anchoring chain of influenza virus hemagglutinin (HA2) folds in Escherichia coli into the low-pH-induced conformation. Proceedings of the National Academy of Sciences of the United States of America. 92: 12205-9. PMID 8618870 DOI: 10.1073/Pnas.92.26.12205 |
0.658 |
|
1995 |
Hughson FM. Molecular mechanisms of protein-mediated membrane fusion. Current Opinion in Structural Biology. 5: 507-13. PMID 8528767 DOI: 10.1016/0959-440X(95)80036-0 |
0.394 |
|
1995 |
Hughson FM. Structural characterization of viral fusion proteins. Current Biology : Cb. 5: 265-74. PMID 7780737 DOI: 10.1016/S0960-9822(95)00057-1 |
0.464 |
|
1994 |
Barrick D, Hughson FM, Baldwin RL. Molecular mechanisms of acid denaturation. The role of histidine residues in the partial unfolding of apomyoglobin. Journal of Molecular Biology. 237: 588-601. PMID 8158639 DOI: 10.1006/Jmbi.1994.1257 |
0.647 |
|
1994 |
Bullough PA, Hughson FM, Treharne AC, Ruigrok RW, Skehel JJ, Wiley DC. Crystals of a fragment of influenza haemagglutinin in the low pH induced conformation. Journal of Molecular Biology. 236: 1262-5. PMID 8120902 DOI: 10.1016/0022-2836(94)90027-2 |
0.485 |
|
1994 |
Bullough PA, Hughson FM, Skehel JJ, Wiley DC. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature. 371: 37-43. PMID 8072525 DOI: 10.1038/371037A0 |
0.6 |
|
1991 |
Hughson FM, Barrick D, Baldwin RL. Probing the stability of a partly folded apomyoglobin intermediate by site-directed mutagenesis. Biochemistry. 30: 4113-8. PMID 2021603 DOI: 10.1021/Bi00231A001 |
0.5 |
|
1990 |
Hughson FM, Wright PE, Baldwin RL. Structural characterization of a partly folded apomyoglobin intermediate. Science (New York, N.Y.). 249: 1544-8. PMID 2218495 DOI: 10.1126/Science.2218495 |
0.575 |
|
1989 |
Hughson FM, Baldwin RL. Use of site-directed mutagenesis to destabilize native apomyoglobin relative to folding intermediates. Biochemistry. 28: 4415-22. PMID 2765493 DOI: 10.1021/Bi00436A044 |
0.527 |
|
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