Brefeldin A Acts to Stabilize an Abortive ARF–GDP–Sec7 Domain Protein Complex

Methods in yeast genetics

Sherman, F., Fink, G. R., & Hicks, J. B. (1979) · Cold Spring Harbor Laboratory eBooks · Cited by 7,430

Brefeldin A: insights into the control of membrane traffic and organelle structure.

Klausner, R. D., Donaldson, J. G., & Lippincott‐Schwartz, J. (1992) · The Journal of Cell Biology · doi:10.1083/jcb.116.5.1071 · Cited by 1,843

Methods in yeast genetics : a Cold Spring Harbor Laboratory course manual

Amberg, D. C., Burke, D. J., & Strathern, J. N. (2005) · Cited by 1,803

Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: Evidence for membrane cycling from Golgi to ER

Lippincott‐Schwartz, J., Yuan, L. C., Bonifacino, J. S., & Klausner, R. D. (1989) · Cell · doi:10.1016/0092-8674(89)90685-5 · Cited by 1,688

Brefeldin A inhibits Golgi membrane-catalysed exchange of guanine nucleotide onto ARF protein

Donaldson, J. G., Finazzi, D., & Klausner, R. D. (1992) · Nature · doi:10.1038/360350a0 · Cited by 754

Inhibition by brefeldin A of a Golgi membrane enzyme that catalyses exchange of guanine nucleotide bound to ARF

Helms, J. B., & Rothman, J. E. (1992) · Nature · doi:10.1038/360352a0 · Cited by 746

ADP-Ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: A novel role for a GTP-binding protein

Serafini, T. A., Orci, L., AMHERDT, M., Brunner, M., Kahn, R., & Rothmant, J. E. (1991) · Cell · doi:10.1016/0092-8674(91)90176-y · Cited by 609

Structural Basis for Activation of ARF GTPase

Goldberg, J. D. (1998) · Cell · doi:10.1016/s0092-8674(00)81754-7 · Cited by 549

A human exchange factor for ARF contains Sec7- and pleckstrin-homology domains

Chardin, P., Paris, S., Antonny, B., Robineau, S., Béraud-Dufour, S., Jackson, C. L., & Chabre, M. (1996) · Nature · doi:10.1038/384481a0 · Cited by 482

Brefeldin A, a drug that blocks secretion, prevents the assembly of non-clathrin-coated buds on Golgi cisternae

Orcl, L., Tagaya, M., AMHERDT, M., Perrelet, A., Donaldson, J. G., Lippincott‐Schwartz, J., Klausner, R. D., & Rothman, J. E. (1991) · Cell · doi:10.1016/0092-8674(91)90273-2 · Cited by 463

Signaling by Phosphoinositide-3,4,5-Trisphosphate Through Proteins Containing Pleckstrin and Sec7 Homology Domains

Klarlund, J. K., Guilherme, A., Holik, J. J., Virbasius, J. V., Chawla, A., & Czech, M. (1997) · Science · doi:10.1126/science.275.5308.1927 · Cited by 415

Binding of ARF and β-COP to Golgi Membranes: Possible Regulation by a Trimeric G Protein

Donaldson, J. G., Kahn, R., Lippincott‐Schwartz, J., & Klausner, R. D. (1991) · Science · doi:10.1126/science.1957170 · Cited by 358

N-Terminal Hydrophobic Residues of the G-Protein ADP-Ribosylation Factor-1 Insert into Membrane Phospholipids upon GDP to GTP Exchange

Antonny, B., Béraud-Dufour, S., Chardin, P., & Chabre, M. (1997) · Biochemistry · doi:10.1021/bi962252b · Cited by 358

EMB30 is essential for normal cell division, cell expansion, and cell adhesion in Arabidopsis and encodes a protein that has similarity to Sec7

Shevell, D. E. (1994) · Cell · doi:10.1016/0092-8674(94)90444-8 · Cited by 313

Nucleotide exchange on ARF mediated by yeast Geal protein

Peyroche, A., Paris, S., & Jackson, C. L. (1996) · Nature · doi:10.1038/384479a0 · Cited by 280

The amino terminus of ADP-ribosylation factor (ARF) is a critical determinant of ARF activities and is a potent and specific inhibitor of protein transport.

Kahn, R., Randazzo, P. A., Serafini, T. A., Weiss, O., Rulka, C., Clark, J., AMHERDT, M., Roller, P. P., Orci, L., & Rothman, J. E. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42378-2 · Cited by 259

Localization of components involved in protein transport and processing through the yeast Golgi apparatus.

Franzusoff, A., Redding, K., Crosby, J., Fuller, R. S., & Schekman, R. W. (1991) · The Journal of Cell Biology · doi:10.1083/jcb.112.1.27 · Cited by 248

Arf proteins: the membrane traffic police?

Boman, A. L., & KAHN, R. (1995) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)88991-4 · Cited by 241

Myristoylation of ADP-ribosylation Factor 1 Facilitates Nucleotide Exchange at Physiological Mg 2+ Levels

Franco, M., Chardin, P., Chabre, M., & Paris, S. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.3.1337 · Cited by 192

COPI-independent Anterograde Transport: Cargo-selective ER to Golgi Protein Transport in Yeast COPI Mutants

Gaynor, E. C., & Emr, S. D. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.136.4.789 · Cited by 192

Structure of the Guanine Nucleotide Exchange Factor Sec7 Domain of Human Arno and Analysis of the Interaction with ARF GTPase

Mossessova, E., Gulbis, J. M., & Goldberg, J. D. (1998) · Cell · doi:10.1016/s0092-8674(00)80933-2 · Cited by 190

Structure of the Sec7 domain of the Arf exchange factor ARNO

Cherfils, J., Ménétrey, J., Mathieu, M., Bras, G. L., Robineau, S., Béraud-Dufour, S., Antonny, B., & Chardin, P. (1998) · Nature · doi:10.1038/32210 · Cited by 185

A glutamic finger in the guanine nucleotide exchange factor ARNO displaces Mg2+ and the β‐phosphate to destabilize GDP on ARF1

Béraud-Dufour, S., Robineau, S., Chardin, P., Paris, S., Chabre, M., Cherfils, J., & Antonny, B. (1998) · The EMBO Journal · doi:10.1093/emboj/17.13.3651 · Cited by 183

Role of Protein-Phospholipid Interactions in the Activation of ARF1 by the Guanine Nucleotide Exchange Factor Arno

Paris, S., Béraud-Dufour, S., Robineau, S., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.35.22221 · Cited by 176

Cytohesin-1, a cytosolic guanine nucleotide-exchange protein for ADP-ribosylation factor

Meacci, E., Tsai, S. C., Adamik, R., Moss, J., & Vaughan, M. M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.5.1745 · Cited by 147

Decumbin, a New Compound from a Species of Penicillium

Singleton, V. L., Bohonos, N., & Ullstrup, A. J. (1958) · Nature · doi:10.1038/1811072a0 · Cited by 144

ARF Is Required for Maintenance of Yeast Golgi and Endosome Structure and Function

Gaynor, E. C., Chen, C., Emr, S. D., & Graham, T. R. (1998) · Molecular Biology of the Cell · doi:10.1091/mbc.9.3.653 · Cited by 133

Brefeldin A reversibly blocks early but not late protein transport steps in the yeast secretory pathway.

Graham, T. R., Scott, P. A. E., & Emr, S. D. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05727.x · Cited by 105

Brefeldin A, a specific inhibitor of intracellular translocation of vesicular stomatitis virus G protein: Intracellular accumulation of high-mannose type G protein and inhibition of its cell surface expression.

Takatsuki, A., & Tamura, G. (1985) · Agricultural and Biological Chemistry · doi:10.1271/bbb1961.49.899 · Cited by 103

Cloning and expression of a cDNA encoding a bovine brain brefeldin A-sensitive guanine nucleotide-exchange protein for ADP-ribosylation factor

Morinaga, N., Moss, J., & Vaughan, M. M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.24.12926 · Cited by 100

ARNO3, a Sec7-domain guanine nucleotide exchange factor for ADP ribosylation factor 1, is involved in the control of Golgi structure and function

Franco, M., Boretto, J., Robineau, S., Monier, S., Goud, B., Chardin, P., & Chavrier, P. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.17.9926 · Cited by 96

Brefeldin A-inhibited guanine nucleotide-exchange activity of Sec7 domain from yeast Sec7 with yeast and mammalian ADP ribosylation factors

Sata, M., Donaldson, J. G., Moss, J., & Vaughan, M. M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.8.4204 · Cited by 95

Brefeldin A and the endocytic pathway Possible implications for membrane traffic and sorting

Hunziker, W., Whitney, J. A., & Mellman, I. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)80908-y · Cited by 60

Brefeldin A causes a defect in secretion in Saccharomyces cerevisiae.

Vogel, J. P., Lee, J. N., Kirsch, D. R., Rose, M. D., & Sztul, E. S. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53655-3 · Cited by 59

Cytotoxicity of Brefeldin A Correlates with Its Inhibitory Effect on Membrane Binding of COP Coat Proteins

Murakami, K., Torii, S., Banno, T., Watanabe, T., Ikehara, Y., & Nakayama, K. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.19.11574 · Cited by 52

Brefeldin A reversibly inhibits secretion in Saccharomyces cerevisiae.

Shah, N., & Klausner, R. D. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53325-1 · Cited by 48

Effects of brefeldin a on the three‐dimensional structure of the golgi apparatus in a sensitive strain of saccharomyces cerevisiae

Rambourg, A., Clermont, Y., Jackson, C. L., & Képès, F. (1995) · The Anatomical Record · doi:10.1002/ar.1092410102 · Cited by 35

HumanGBF1Is a Ubiquitously Expressed Gene of the Sec7 Domain Family Mapping to 10q24

Mansour, S. J., Herbrick, J.-A., Scherer, S. W., et al. (1998) · Genomics · doi:10.1006/geno.1998.5563 · Cited by 25

K-Ras(G12C) inhibitors allosterically control GTP affinity and effector interactions

Ostrem, J. M., Peters, U., Sos, M. L., Wells, J. A., & Shokat, K. M. (2013) · Nature · doi:10.1038/nature12796 · Cited by 2,557

Small GTP-Binding Proteins

Takai, Y., Sasaki, T., & Matozaki, T. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.1.153 · Cited by 2,511

Vertebrate protein glycosylation: diversity, synthesis and function

Moremen, K. W., Tiemeyer, M., & Nairn, A. V. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3383 · Cited by 1,733

The Arabidopsis GNOM ARF-GEF Mediates Endosomal Recycling, Auxin Transport, and Auxin-Dependent Plant Growth

Geldner, N., Anders, N., Wolters, H., Keicher, J., Kornberger, W., Müller, P., Delbarre, A., Ueda, T., Nakano, A., & Jürgens, G. (2003) · Cell · doi:10.1016/s0092-8674(03)00003-5 · Cited by 1,125

Vacuolar H+-ATPase Activity Is Required for Endocytic and Secretory Trafficking in Arabidopsis

Dettmer, J., Hong‐Hermesdorf, A., Stierhof, Y., et al. (2006) · The Plant Cell · doi:10.1105/tpc.105.037978 · Cited by 853

Identification of a brefeldin A-insensitive guanine nucleotide-exchange protein for ADP-ribosylation factor in bovine brain.

Tsai, S. C., Adamik, R., Moss, J., & Vaughan, M. J. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.8.3063 · Cited by 52

Characterization of the role of Orc6 in the cell cycle of the budding yeast Saccharomyces cerevisiae

Semple, J. W. (2006) · Cited by 1

Effects of brefeldin A and accessory proteins on association of ADP-ribosylation factors 1, 3, and 5 with Golgi

Tsai, S. C., Adamik, R., Haun, R. S., Moss, J., & Vaughan, M. J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82059-2 · Cited by 61

Activation of ADP-ribosylation factor by Golgi membranes. Evidence for a brefeldin A- and protease-sensitive activating factor on Golgi membranes

Randazzo, P. A., Yang, Y. C., Rulka, C., & Kahn, R. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98387-0 · Cited by 136

Tolerance of budding yeastSaccharomyces cerevisiaeto ultra high pressure

Shibata, M., Torigoe, M., Matsumoto, Y., et al. (2014) · Journal of Physics Conference Series · doi:10.1088/1742-6596/500/10/102004 · Cited by 6