Signalling ballet in space and time

The chemical basis of morphogenesis

Turing, A. M. (1952) · Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences · doi:10.1098/rstb.1952.0012 · Cited by 11,733

Lipid rafts and signal transduction

Simons, K., & Toomre, D. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35036052 · Cited by 5,371

Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation

Marshall, C. J. (1995) · Cell · doi:10.1016/0092-8674(95)90401-8 · Cited by 3,906

Regulation and Function of NF-κB Transcription Factors in the Immune System

Vallabhapurapu, S., & Karin, M. (2009) · Annual Review of Immunology · doi:10.1146/annurev.immunol.021908.132641 · Cited by 2,588

Small GTP-Binding Proteins

Takai, Y., Sasaki, T., & Matozaki, T. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.1.153 · Cited by 2,475

De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-κB signalling

Wertz, I. E., O'Rourke, K. M., Zhou, H., Eby, M., Aravind, L., Seshagiri, S., Wu, P., Wiesmann, C., Baker, R., Boone, D. L., et al. (2004) · Nature · doi:10.1038/nature02794 · Cited by 1,856

STIM1, an essential and conserved component of store-operated Ca2 + channel function

Roos, J., DiGregorio, P. J., Yeromin, A. V., Ohlsen, K., Lioudyno, M., Zhang, S., Safrina, O., Kozak, J. A., Wagner, S. L., Cahalan, M. D., et al. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200502019 · Cited by 1,828

Sniffers, buzzers, toggles and blinkers: dynamics of regulatory and signaling pathways in the cell

Tyson, J. J., Chen, K. C., & Novak, B. (2003) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(03)00017-6 · Cited by 1,583

Direct observation of the nanoscale dynamics of membrane lipids in a living cell

Eggeling, C., Ringemann, C., Medda, R., Schwarzmann, G., Sandhoff, K., Polyakova, S., Belov, V. N., Hein, B., von Middendorff, C., Schönle, A., et al. (2009) · Nature · doi:10.1038/nature07596 · Cited by 1,520

β-Arrestins and Cell Signaling

DeWire, S. M., Ahn, S., Lefkowitz, R. J., & Shenoy, S. K. (2007) · Annual Review of Physiology · doi:10.1146/annurev.physiol.69.022405.154749 · Cited by 1,397

Cell-signalling dynamics in time and space

Kholodenko, B. N. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1838 · Cited by 1,347

An ER-Mitochondria Tethering Complex Revealed by a Synthetic Biology Screen

Kornmann, B., Currie, E., Collins, S. R., Schuldiner, M., Nunnari, J., Weissman, J. S., & Walter, P. (2009) · Science · doi:10.1126/science.1175088 · Cited by 1,275

Paradigm Shift of the Plasma Membrane Concept from the Two-Dimensional Continuum Fluid to the Partitioned Fluid: High-Speed Single-Molecule Tracking of Membrane Molecules

Kusumi, A., Nakada, C., Ritchie, K., Murase, K., Suzuki, K., Murakoshi, H., Kasai, R. S., Kondo, J., & Fujiwara, T. (2005) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.34.040204.144637 · Cited by 1,122

The ERK1/2 mitogen-activated protein kinase pathway as a master regulator of the G1- to S-phase transition

Meloche, S., & Pouysségur, J. (2007) · Oncogene · doi:10.1038/sj.onc.1210414 · Cited by 1,091

Coordinating ERK/MAPK signalling through scaffolds and inhibitors

Kolch, W. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1743 · Cited by 1,070

A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane

Hancock, J. F., Paterson, H., & Marshall, C. J. (1990) · Cell · doi:10.1016/0092-8674(90)90294-o · Cited by 1,059

The Biochemical Basis of an All-or-None Cell Fate Switch in Xenopus Oocytes

Ferrell, J. E., & Machleder, E. M. (1998) · Science · doi:10.1126/science.280.5365.895 · Cited by 1,052

STIM1 Clusters and Activates CRAC Channels via Direct Binding of a Cytosolic Domain to Orai1

Park, C. Y., Hoover, P. J., Mullins, F. M., Bachhawat, P., Covington, E. D., Raunser, S., Walz, T., Garcia, K. C., Dolmetsch, R. E., & Lewis, R. S. (2009) · Cell · doi:10.1016/j.cell.2009.02.014 · Cited by 954

Molecular interpretation of ERK signal duration by immediate early gene products

Murphy, L. O., Smith, S., Chen, R.-H., Fingar, D. C., & Blenis, J. (2002) · Nature Cell Biology · doi:10.1038/ncb822 · Cited by 929

Nanoscale Organization of Multiple GPI-Anchored Proteins in Living Cell Membranes

Sharma, P., Varma, R., Sarasij, R. C., Ira, Gousset, K., Krishnamoorthy, G., Rao, M., & Mayor, S. (2004) · Cell · doi:10.1016/s0092-8674(04)00167-9 · Cited by 891

Lipid rafts: contentious only from simplistic standpoints

Hancock, J. F. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1925 · Cited by 788

Dual-specificity phosphatases: critical regulators with diverse cellular targets

Patterson, K. I., Brummer, T., O'brien, P. M., & Daly, R. J. (2009) · Biochemical Journal · doi:10.1042/bj20082234 · Cited by 744

Signaling switches and bistability arising from multisite phosphorylation in protein kinase cascades

Markevich, N. I., Hoek, J. B., & Kholodenko, B. N. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200308060 · Cited by 692

Negative feedback and ultrasensitivity can bring about oscillations in the mitogen‐activated protein kinase cascades

Kholodenko, B. N. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01197.x · Cited by 643

Regulation of Raf-1 by Direct Feedback Phosphorylation

Dougherty, M. K., Müller, J., Ritt, D. A., Zhou, M., Zhou, X. Z., Copeland, T. D., Conrads, T. P., Veenstra, T. D., Lu, K. P., & Morrison, D. K. (2005) · Molecular Cell · doi:10.1016/j.molcel.2004.11.055 · Cited by 633

Integrating signals from RTKs to ERK/MAPK

McKay, M. M., & Morrison, D. K. (2007) · Oncogene · doi:10.1038/sj.onc.1210394 · Cited by 621

Growth factor-induced MAPK network topology shapes Erk response determining PC-12 cell fate

Santos, S. D. M., Verveer, P. J., & Bastiaens, P. I. H. (2007) · Nature Cell Biology · doi:10.1038/ncb1543 · Cited by 609

Ras signalling on the endoplasmic reticulum and the Golgi

Chiu, V. K., Bivona, T., Hach, A., Sajous, J. B., Silletti, J., Wiener, H., Johnson, R. L., Cox, A. D., & Philips, M. R. (2002) · Nature Cell Biology · doi:10.1038/ncb783 · Cited by 594 · cited 1×

Variability and memory of protein levels in human cells

Sigal, A., Milo, R., Cohen, A., Geva-Zatorsky, N., Klein, Y., Liron, Y., Rosenfeld, N., Danon, T., Perzov, N., & Alon, U. (2006) · Nature · doi:10.1038/nature05316 · Cited by 587

Thymic selection threshold defined by compartmentalization of Ras/MAPK signalling

Daniels, M. A., Teixeiro, E., Gill, J., Hausmann, B., Roubaty, D., Holmberg, K., Werlen, G., Holländer, G. A., Gascoigne, N. R. J., & Palmer, E. (2006) · Nature · doi:10.1038/nature05269 · Cited by 577

The Coherent Feedforward Loop Serves as a Sign-sensitive Delay Element in Transcription Networks

Mangan, S., Zaslaver, A., & Alon, U. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.09.049 · Cited by 553

Pulsatile Stimulation Determines Timing and Specificity of NF-κB-Dependent Transcription

Ashall, L., Horton, C. A., Nelson, D. E., Paszek, P., Harper, C. V., Sillitoe, K., Ryan, S., Spiller, D. G., Unitt, J. F., Broomhead, D. S., et al. (2009) · Science · doi:10.1126/science.1164860 · Cited by 543

Visualization of a Ran-GTP Gradient in Interphase and Mitotic Xenopus Egg Extracts

Kalab, P., Weis, K., & Heald, R. (2002) · Science · doi:10.1126/science.1068798 · Cited by 530

Targeting of Cyclic AMP Degradation to β 2 -Adrenergic Receptors by β-Arrestins

Perry, S. J., Baillie, G. S., Kohout, T. A., McPhee, I., Magiera, M. M., Ang, K. L., Miller, W. E., McLean, A. J., Conti, M., Houslay, M. D., et al. (2002) · Science · doi:10.1126/science.1074683 · Cited by 506

A dimerization-dependent mechanism drives RAF catalytic activation

Rajakulendran, T., Sahmi, M., Lefrançois, M., Sicheri, F., & Therrien, M. (2009) · Nature · doi:10.1038/nature08314 · Cited by 489

A module of negative feedback regulators defines growth factor signaling

Amit, I., Citri, A., Shay, T., Lu, Y., Katz, M., Zhang, F., Tarcic, G., Siwak, D., Lahad, J., Jacob-Hirsch, J., et al. (2007) · Nature Genetics · doi:10.1038/ng1987 · Cited by 488

Scaffold proteins may biphasically affect the levels of mitogen-activated protein kinase signaling and reduce its threshold properties

Levchenko, A., Bruck, J., & Sternberg, P. W. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.11.5818 · Cited by 486

Ca2+ transfer from the ER to mitochondria: When, how and why

Rizzuto, R., Marchi, S., Bonora, M., Aguiari, P., Bononi, A., De Stefani, D., Giorgi, C., Leo, S., Rimessi, A., Siviero, R., et al. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.03.015 · Cited by 476

H-ras, K-ras, and inner plasma membrane raft proteins operate in nanoclusters with differential dependence on the actin cytoskeleton

Plowman, S. J., Muncke, C., Parton, R. G., & Hancock, J. F. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504114102 · Cited by 468

Nanoclusters of GPI-Anchored Proteins Are Formed by Cortical Actin-Driven Activity

Goswami, D., Gowrishankar, K., Bilgrami, S., Ghosh, S., Raghupathy, R., Chadda, R., Vishwakarma, R., Rao, M., & Mayor, S. (2008) · Cell · doi:10.1016/j.cell.2008.11.032 · Cited by 450

Untangling the wires: A strategy to trace functional interactions in signaling and gene networks

Kholodenko, B. N., Kiyatkin, A., Bruggeman, F. J., Sontag, E., Westerhoff, H. V., & Hoek, J. B. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.192442699 · Cited by 422

Plasma membrane nanoswitches generate high-fidelity Ras signal transduction

Tian, T., Harding, A., Inder, K., Plowman, S., Parton, R. G., & Hancock, J. F. (2007) · Nature Cell Biology · doi:10.1038/ncb1615 · Cited by 407

Wave-Pinning and Cell Polarity from a Bistable Reaction-Diffusion System

Mori, Y., Jilkine, A., & Edelstein-Keshet, L. (2008) · Biophysical Journal · doi:10.1529/biophysj.107.120824 · Cited by 407

Digital signaling and hysteresis characterize Ras activation in lymphoid cells.

Das, J., Ho, M., Zikherman, J., Govern, C., Yang, M., Weiss, A., Chakraborty, A. K., & Roose, J. P. (2009) · Cell · doi:10.1016/j.cell.2008.11.051 · Cited by 398

Localization of the MP1-MAPK Scaffold Complex to Endosomes Is Mediated by p14 and Required for Signal Transduction

Teis, D., Wunderlich, W., & Huber, L. A. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00364-7 · Cited by 371

Single-molecule imaging analysis of Ras activation in living cells

Murakoshi, H., Iino, R., Kobayashi, T., Fujiwara, T., Ohshima, C., Yoshimura, A., & Kusumi, A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401354101 · Cited by 369

The Dual Specificity Mitogen-activated Protein Kinase Phosphatase-1 and -2 Are Induced by the p42/p44MAPK Cascade

Brondello, J.-M., Brunet, A., Pouysségur, J., & McKenzie, F. R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.2.1368 · Cited by 361

Midzone activation of aurora B in anaphase produces an intracellular phosphorylation gradient

Fuller, B. G., Lampson, M. A., Foley, E. A., Rosasco-Nitcher, S., Le, K. V., Tobelmann, P., Brautigan, D. L., Stukenberg, P. T., & Kapoor, T. M. (2008) · Nature · doi:10.1038/nature06923 · Cited by 354

A spatial gradient coordinates cell size and mitotic entry in fission yeast

Moseley, J. B., Mayeux, A., Paoletti, A., & Nurse, P. (2009) · Nature · doi:10.1038/nature08074 · Cited by 350

A Network of Immediate Early Gene Products Propagates Subtle Differences in Mitogen-Activated Protein Kinase Signal Amplitude and Duration

Murphy, L. O., MacKeigan, J. P., & Blenis, J. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.1.144-153.2004 · Cited by 336

Dynamics of Cdc42 network embodies a Turing‐type mechanism of yeast cell polarity

Goryachev, A. B., & Pokhilko, A. V. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.03.029 · Cited by 327

Molecular recognitions in the MAP kinase cascades

Tanoue, T., & Nishida, E. (2003) · Cellular Signalling · doi:10.1016/s0898-6568(02)00112-2 · Cited by 318

GPI-anchored receptor clusters transiently recruit Lyn and Gα for temporary cluster immobilization and Lyn activation: single-molecule tracking study 1

Suzuki, K. G. N., Fujiwara, T. K., Sanematsu, F., Iino, R., Edidin, M., & Kusumi, A. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200609174 · Cited by 310

Lipid rafts and membrane traffic

Hanzal-Bayer, M. F., & Hancock, J. F. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.03.019 · Cited by 304

Cell fate decisions are specified by the dynamic ERK interactome

von Kriegsheim, A., Baiocchi, D., Birtwistle, M., Sumpton, D., Bienvenut, W., Morrice, N., Yamada, K., Lamond, A., Kalna, G., Orton, R., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1994 · Cited by 286

Cell Shape and Negative Links in Regulatory Motifs Together Control Spatial Information Flow in Signaling Networks

Neves, S. R., Tsokas, P., Sarkar, A., Grace, E. A., Rangamani, P., Taubenfeld, S. M., Alberini, C. M., Schaff, J. C., Blitzer, R. D., Moraru, I. I., et al. (2008) · Cell · doi:10.1016/j.cell.2008.04.025 · Cited by 279

The Ste5 Scaffold Allosterically Modulates Signaling Output of the Yeast Mating Pathway

Bhattacharyya, R. P., Reményi, A., Good, M. C., Bashor, C. J., Falick, A. M., & Lim, W. A. (2006) · Science · doi:10.1126/science.1120941 · Cited by 276

Differential feedback regulation of the MAPK cascade underlies the quantitative differences in EGF and NGF signalling in PC12 cells

Brightman, F. A., & Fell, D. A. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)02037-8 · Cited by 247

Ligand-Specific c-Fos Expression Emerges from the Spatiotemporal Control of ErbB Network Dynamics

Nakakuki, T., Birtwistle, M. R., Saeki, Y., Yumoto, N., Ide, K., Nagashima, T., Brusch, L., Ogunnaike, B. A., Okada-Hatakeyama, M., & Kholodenko, B. N. (2010) · Cell · doi:10.1016/j.cell.2010.03.054 · Cited by 241

Bistability in the JNK cascade

Bagowski, C. P., & Ferrell, J. E. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00330-x · Cited by 237

Rapid and sustained nuclear–cytoplasmic ERK oscillations induced by epidermal growth factor

Shankaran, H., Ippolito, D. L., Chrisler, W. B., Resat, H., Bollinger, N., Opresko, L. K., & Wiley, H. S. (2009) · Molecular Systems Biology · doi:10.1038/msb.2009.90 · Cited by 235

Ligand‐dependent responses of the ErbB signaling network: experimental and modeling analyses

Birtwistle, M. R., Hatakeyama, M., Yumoto, N., Ogunnaike, B. A., Hoek, J. B., & Kholodenko, B. N. (2007) · Molecular Systems Biology · doi:10.1038/msb4100188 · Cited by 234

Potential for Control of Signaling Pathways via Cell Size and Shape

Meyers, J., Craig, J., & Odde, D. J. (2006) · Current Biology · doi:10.1016/j.cub.2006.07.056 · Cited by 232

Ras plasma membrane signalling platforms

HANCOCK, J. F., & PARTON, R. G. (2005) · Biochemical Journal · doi:10.1042/bj20050231 · Cited by 232

Spatial regulation of Fus3 MAP kinase activity through a reaction-diffusion mechanism in yeast pheromone signalling

Maeder, C. I., Hink, M. A., Kinkhabwala, A., Mayr, R., Bastiaens, P. I. H., & Knop, M. (2007) · Nature Cell Biology · doi:10.1038/ncb1652 · Cited by 231

A-kinase anchoring proteins take shape

Beene, D. L., & Scott, J. D. (2007) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2007.02.011 · Cited by 225

Ras membrane orientation and nanodomain localization generate isoform diversity

Abankwa, D., Gorfe, A. A., Inder, K., & Hancock, J. F. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903907107 · Cited by 223

Systems-level interactions between insulin–EGF networks amplify mitogenic signaling

Borisov, N., Aksamitiene, E., Kiyatkin, A., Legewie, S., Berkhout, J., Maiwald, T., Kaimachnikov, N. P., Timmer, J., Hoek, J. B., & Kholodenko, B. N. (2009) · Molecular Systems Biology · doi:10.1038/msb.2009.19 · Cited by 222

Dynamic recruitment of phospholipase Cγ at transiently immobilized GPI-anchored receptor clusters induces IP3–Ca2+ signaling: single-molecule tracking study 2

Suzuki, K. G. N., Fujiwara, T. K., Edidin, M., & Kusumi, A. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200609175 · Cited by 217

Scaffold proteins and immune-cell signalling

Shaw, A. S., & Filbert, E. L. (2009) · Nature Reviews Immunology · doi:10.1038/nri2473 · Cited by 210

Bistability and Oscillations in the Huang-Ferrell Model of MAPK Signaling

Qiao, L., Nachbar, R. B., Kevrekidis, I. G., & Shvartsman, S. Y. (2007) · PLoS Computational Biology · doi:10.1371/journal.pcbi.0030184 · Cited by 210

Sustained Activation of the Mitogen-activated Protein Kinase Pathway

McCawley, L. J., Li, S., Wattenberg, E. V., & Hudson, L. G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.7.4347 · Cited by 203

The Ste5 Scaffold Directs Mating Signaling by Catalytically Unlocking the Fus3 MAP Kinase for Activation

Good, M., Tang, G., Singleton, J., Reményi, A., & Lim, W. A. (2009) · Cell · doi:10.1016/j.cell.2009.01.049 · Cited by 197

Scaffolding Protein Grb2-associated Binder 1 Sustains Epidermal Growth Factor-induced Mitogenic and Survival Signaling by Multiple Positive Feedback Loops

Kiyatkin, A., Aksamitiene, E., Markevich, N. I., Borisov, N. M., Hoek, J. B., & Kholodenko, B. N. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600482200 · Cited by 195

Positive- and negative-feedback regulations coordinate the dynamic behavior of the Ras-Raf-MEK-ERK signal transduction pathway

Shin, S.-Y., Rath, O., Choo, S.-M., Fee, F., McFerran, B., Kolch, W., & Cho, K.-H. (2009) · Journal of Cell Science · doi:10.1242/jcs.036319 · Cited by 192

Identifying Optimal Lipid Raft Characteristics Required To Promote Nanoscale Protein-Protein Interactions on the Plasma Membrane

Nicolau, D. V., Burrage, K., Parton, R. G., & Hancock, J. F. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.1.313-323.2006 · Cited by 188

Spatial gradients of cellular phospho‐proteins

Brown, G. C., & Kholodenko, B. N. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01058-3 · Cited by 183

Quantitative Transcriptional Control of ErbB Receptor Signaling Undergoes Graded to Biphasic Response for Cell Differentiation

Nagashima, T., Shimodaira, H., Ide, K., Nakakuki, T., Tani, Y., Takahashi, K., Yumoto, N., & Hatakeyama, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608653200 · Cited by 177

EGF induced SOS phosphorylation in PC12 cells involves P90 RSK-2

Douville, E., & Downward, J. (1997) · Oncogene · doi:10.1038/sj.onc.1201214 · Cited by 165

A Ras-induced conformational switch in the Ras activator Son of sevenless

Freedman, T. S., Sondermann, H., Friedland, G. D., Kortemme, T., Bar‐Sagi, D., Marqusee, S., & Kuriyan, J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608127103 · Cited by 160

Generation of biological patterns and form: Some physical, mathematical, and logical aspects

Gierer, A. (1981) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(82)90019-0 · Cited by 160

Four-dimensional organization of protein kinase signaling cascades: the roles of diffusion, endocytosis and molecular motors

Kholodenko, B. Ν. (2003) · Journal of Experimental Biology · doi:10.1242/jeb.00298 · Cited by 157

Subcellular Localization Determines MAP Kinase Signal Output

Harding, A. S., Tian, T., Westbury, E., Frische, E. W., & Hancock, J. F. (2005) · Current Biology · doi:10.1016/j.cub.2005.04.020 · Cited by 153

Targeting of Diacylglycerol Degradation to M1 Muscarinic Receptors by ß-Arrestins

Nelson, C. D., Perry, S. J., Regier, D. S., Prescott, S. M., Topham, M. K., & Lefkowitz, R. J. (2007) · Science · doi:10.1126/science.1134562 · Cited by 150

Galectin-1 is a novel structural component and a major regulator of h-ras nanoclusters.

Belanis, L., Plowman, S. J., Rotblat, B., Hancock, J., & Kloog, Y. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-10-1053 · Cited by 147

Live-Cell Imaging of Enzyme-Substrate Interaction Reveals Spatial Regulation of PTP1B

Yudushkin, I. A., Schleifenbaum, A., Kinkhabwala, A., Neel, B. G., Schultz, C., & Bastiaens, P. I. H. (2007) · Science · doi:10.1126/science.1134966 · Cited by 143

K-Ras Nanoclustering Is Subverted by Overexpression of the Scaffold Protein Galectin-3

Shalom‐Feuerstein, R., Plowman, S. J., Rotblat, B., Ariotti, N., Tian, T., Hancock, J. F., & Kloog, Y. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-1117 · Cited by 143

Using plasma membrane nanoclusters to build better signaling circuits

Harding, A. S., & Hancock, J. F. (2008) · Trends in Cell Biology · doi:10.1016/j.tcb.2008.05.006 · Cited by 139

Ras/MAPK signaling from endomembranes

Fehrenbacher, N., Bar-Sagi, D., & Philips, M. (2009) · Molecular Oncology · doi:10.1016/j.molonc.2009.06.004 · Cited by 131

Ras Subcellular Localization Defines Extracellular Signal-Regulated Kinase 1 and 2 Substrate Specificity through Distinct Utilization of Scaffold Proteins

Casar, B., Arozarena, I., Sanz-Moreno, V., Pinto, A., Agudo-Ibáñez, L., Marais, R., Lewis, R. E., Berciano, M., & Crespo, P. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01359-08 · Cited by 126

FGF induces oscillations of Hes1 expression and Ras/ERK activation

Nakayama, K., Satoh, T., Igari, A., Kageyama, R., & Nishida, E. (2008) · Current Biology · doi:10.1016/j.cub.2008.03.013 · Cited by 117

Modular construction of a signaling scaffold: MORG1 interacts with components of the ERK cascade and links ERK signaling to specific agonists

Vomastek, T., Schaeffer, H. J., Tarcsafalvi, A., Smolkin, M. E., Bissonette, E. A., & Weber, M. J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0305894101 · Cited by 114

Composition and Function of G Protein-Coupled Receptor Signalsomes Controlling Mitogen-Activated Protein Kinase Activity

Luttrell, L. M. (2005) · Journal of Molecular Neuroscience · doi:10.1385/jmn:26:2-3:253 · Cited by 113

Recurrent design patterns in the feedback regulation of the mammalian signalling network

Legewie, S., Herzel, H., Westerhoff, H. V., & Blüthgen, N. (2008) · Molecular Systems Biology · doi:10.1038/msb.2008.29 · Cited by 112

Membrane-bound Turing patterns

Levine, H., & Rappel, W. (2005) · Physical Review E · doi:10.1103/physreve.72.061912 · Cited by 112

Membrane Localization of Scaffold Proteins Promotes Graded Signaling in the Yeast MAP Kinase Cascade

Takahashi, S., & Pryciak, P. M. (2008) · Current Biology · doi:10.1016/j.cub.2008.07.050 · Cited by 112

Electrostatic Interactions Positively Regulate K-Ras Nanocluster Formation and Function

Plowman, S. J., Ariotti, N., Goodall, A., Parton, R. G., & Hancock, J. F. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00050-08 · Cited by 108

Retrograde signaling in axonal regeneration

Rishal, I., & Fainzilber, M. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.08.010 · Cited by 105

MAP kinase cascade signaling and endocytic trafficking: a marriage of convenience?

Kholodenko, B. Ν. (2002) · Trends in Cell Biology · doi:10.1016/s0962-8924(02)02251-1 · Cited by 104

Activation of the MAPK module from different spatial locations generates distinct system outputs.

Inder, K. L., Harding, A., Plowman, S. J., Philips, M., Parton, R., & Hancock, J. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-04-0407 · Cited by 92

Bistability, Stochasticity, and Oscillations in the Mitogen-Activated Protein Kinase Cascade

Wang, X., Hao, N., Dohlman, H. G., & Elston, T. C. (2005) · Biophysical Journal · doi:10.1529/biophysj.105.073874 · Cited by 91

Long‐range signaling by phosphoprotein waves arising from bistability in protein kinase cascades

Markevich, N. I., Tsyganov, M. A., Hoek, J. B., & Kholodenko, B. Ν. (2006) · Molecular Systems Biology · doi:10.1038/msb4100108 · Cited by 91

PI3K‐dependent cross‐talk interactions converge with Ras as quantifiable inputs integrated by Erk

Wang, C., Cirit, M., & Haugh, J. M. (2009) · Molecular Systems Biology · doi:10.1038/msb.2009.4 · Cited by 87

Regulation of Microtubule Dynamics by Reaction Cascades Around Chromosomes

Athale, C. A., Dinarina, A., Corral, M. M., Pugieux, C., Nédélec, F., & Karsenti, E. (2008) · Science · doi:10.1126/science.1161820 · Cited by 74

Oscillatory Phosphorylation of Yeast Fus3 MAP Kinase Controls Periodic Gene Expression and Morphogenesis

Hilioti, Z., Sabbagh, W., Paliwal, S., Bergmann, A., Goncalves, M. D., Bardwell, L., & Levchenko, A. (2008) · Current Biology · doi:10.1016/j.cub.2008.09.027 · Cited by 73

Spatially distributed cell signalling

Kholodenko, B. Ν. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.09.045 · Cited by 71

Untangling the signalling wires

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Models of Spatially Restricted Biochemical Reaction Systems

Neves, S. R., & Iyengar, R. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800058200 · Cited by 43

Positional Information Generated by Spatially Distributed Signaling Cascades

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Toggle switches, pulses and oscillations are intrinsic properties of the Src activation/deactivation cycle

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Signaling gradients in cascades of two-state reaction-diffusion systems

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Multiple roles of the NF‐?B signaling pathway regulated by coupled negative feedback circuits

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Revitalizing membrane rafts: new tools and insights

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Encoding and Decoding Cellular Information through Signaling Dynamics

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An atlas of substrate specificities for the human serine/threonine kinome

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