Glycolytic Enzymes Coalesce in G Bodies under Hypoxic Stress

Understanding the Warburg Effect: The Metabolic Requirements of Cell Proliferation

Vander Heiden, M. G., Cantley, L. C., & Thompson, C. B. (2009) · Science · doi:10.1126/science.1160809 · Cited by 16,197 · see citing works

Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae

Longtine, M. S., Mckenzie, A., DeMarini, D. J., Shah, N. G., Wach, A., Brachat, A., Philippsen, P., & Pringle, J. R. (1998) · Yeast · doi:10.1002/(sici)1097-0061(199807)14:10 · Cited by 5,367 · see citing works

Regulation of cancer cell metabolism

Cairns, R. A., Harris, I. S., & Mak, T. W. (2011) · Nature Reviews Cancer · doi:10.1038/nrc2981 · Cited by 4,744 · see citing works

Functional profiling of the Saccharomyces cerevisiae genome

Giaever, G., Chu, A. M., Ni, L., Connelly, C., Riles, L., Véronneau, S., Dow, S., Lucau-Danila, A., Anderson, K., André, B., et al. (2002) · Nature · doi:10.1038/nature00935 · Cited by 4,316 · see citing works

Global analysis of protein localization in budding yeast

Huh, W.-K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., & O'Shea, E. K. (2003) · Nature · doi:10.1038/nature02026 · Cited by 4,248 · cited 2× · see citing works

2016 update of the PRIDE database and its related tools

Vizcaíno, J. A., Csordás, A., del‐Toro, N., Dianes, J. A., Griss, J., Lavidas, I., Mayer, G., Pérez‐Riverol, Y., Reisinger, F., Ternent, T., et al. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv1145 · Cited by 3,466 · see citing works

The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth

Christofk, H. R., Vander Heiden, M. G., Harris, M. H., Ramanathan, A., Gerszten, R. E., Wei, R., Fleming, M. D., Schreiber, S. L., & Cantley, L. C. (2008) · Nature · doi:10.1038/nature06734 · Cited by 2,820 · see citing works

Phase Separation by Low Complexity Domains Promotes Stress Granule Assembly and Drives Pathological Fibrillization

Molliex, A., Temirov, J. P., Lee, J., Coughlin, M., Kanagaraj, A., Kim, H. J., Mittag, T., & Taylor, J. P. (2015) · Cell · doi:10.1016/j.cell.2015.09.015 · Cited by 2,658 · see citing works

Cell-free Formation of RNA Granules: Low Complexity Sequence Domains Form Dynamic Fibers within Hydrogels

Kato, M., Han, T. W., Xie, S., Shi, K., Du, X., Wu, L. C., Mirzaei, H., Goldsmith, E. J., Longgood, J., Pei, J., et al. (2012) · Cell · doi:10.1016/j.cell.2012.04.017 · Cited by 2,012 · see citing works

An Automated Multidimensional Protein Identification Technology for Shotgun Proteomics

Wolters, D. A., Washburn, M. P., & Yates, J. R. (2001) · Analytical Chemistry · doi:10.1021/ac010617e · Cited by 1,821 · see citing works

Coexisting liquid phases underlie nucleolar sub-compartments

Feric, M., Vaidya, N., Harmon, T., Mitrea, D. M., Zhu, L., Richardson, T. M., Kriwacki, R., Pappu, R., & Brangwynne, C. (2016) · Cell · doi:10.1016/j.cell.2016.04.047 · Cited by 1,798 · see citing works

Principles and Properties of Stress Granules

Protter, D. S. W., & Parker, R. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.05.004 · Cited by 1,738 · see citing works

Evaluation of Multidimensional Chromatography Coupled with Tandem Mass Spectrometry (LC/LC−MS/MS) for Large-Scale Protein Analysis: The Yeast Proteome

Peng, J., Elias, J. E., Thoreen, C. C., Licklider, L., & Gygi, S. P. (2002) · Journal of Proteome Research · doi:10.1021/pr025556v · Cited by 1,652 · see citing works

ATPase-Modulated Stress Granules Contain a Diverse Proteome and Substructure

Jain, S., Wheeler, J., Walters, R. W., Agrawal, A., Barsic, A. J., & Parker, R. (2016) · Cell · doi:10.1016/j.cell.2015.12.038 · Cited by 1,597 · see citing works

THE AMP-ACTIVATED/SNF1 PROTEIN KINASE SUBFAMILY: Metabolic Sensors of the Eukaryotic Cell?

Hardie, D. G., Carling, D., & Carlson, M. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.821 · Cited by 1,436 · see citing works

DTASelect and Contrast: Tools for Assembling and Comparing Protein Identifications from Shotgun Proteomics

Tabb, D. L., McDonald, W. H., & Yates, J. R. (2002) · Journal of Proteome Research · doi:10.1021/pr015504q · Cited by 1,369 · see citing works

The disordered P granule protein LAF-1 drives phase separation into droplets with tunable viscosity and dynamics

Elbaum-Garfinkle, S., Kim, Y., Szczepaniak, K., Chen, C. C.-H., Eckmann, C. R., Myong, S., & Brangwynne, C. P. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1504822112 · Cited by 1,278 · see citing works

MetaboAnalyst 2.0--a comprehensive server for metabolomic data analysis

Xia, J., Mandal, R., Sinelnikov, I., Broadhurst, D., & Wishart, D. S. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks374 · Cited by 1,146 · see citing works

The Pairwise Energy Content Estimated from Amino Acid Composition Discriminates between Folded and Intrinsically Unstructured Proteins

Dosztányi, Z., Csizmók, V., Tompa, P., & Simon, I. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.01.071 · Cited by 1,021 · see citing works

A second set of loxP marker cassettes for Cre-mediated multiple gene knockouts in budding yeast

Güldener, U. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.6.e23 · Cited by 982 · see citing works

RNA granules: post-transcriptional and epigenetic modulators of gene expression

Anderson, P., & Kedersha, N. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2694 · Cited by 866 · see citing works

ALS/FTD Mutation-Induced Phase Transition of FUS Liquid Droplets and Reversible Hydrogels into Irreversible Hydrogels Impairs RNP Granule Function

Murakami, T., Qamar, S., Lin, J. Q., Schierle, G. S. K., Rees, E. J., Miyashita, A., Costa, A. R., Dodd, R. B., Chan, F. T. S., Michel, C. H., et al. (2015) · Neuron · doi:10.1016/j.neuron.2015.10.030 · Cited by 848 · see citing works

Reversible compartmentalization of de novo purine biosynthetic complexes in living cells

An, S., Kumar, R., Sheets, E. D., & Benkovic, S. J. (2008) · Science · doi:10.1126/science.1152241 · Cited by 585 · cited 2× · see citing works

Modulation of Intrinsically Disordered Protein Function by Post-translational Modifications

Bah, A., & Forman-Kay, J. D. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.695056 · Cited by 556 · see citing works

A comprehensive strategy enabling high-resolution functional analysis of the yeast genome

Breslow, D. K., Cameron, D. M., Collins, S. R., Schuldiner, M., Stewart-Ornstein, J., Newman, H. W., Braun, S. J., Madhani, H. D., Krogan, N. J., & Weissman, J. S. (2008) · Nature Methods · doi:10.1038/nmeth.1234 · Cited by 517 · see citing works

P bodies promote stress granule assembly in Saccharomyces cerevisiae

Buchan, J. R., Muhlrad, D., & Parker, R. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200807043 · Cited by 517 · see citing works

ProLuCID: An improved SEQUEST-like algorithm with enhanced sensitivity and specificity

Xu, T., Park, S. K., Venable, J. D., Wohlschlegel, J. A., Diedrich, J. K., Cociorva, D., Lu, B., Liao, L., Hewel, J., Han, X., et al. (2015) · Journal of Proteomics · doi:10.1016/j.jprot.2015.07.001 · Cited by 511 · see citing works

Reversible, Specific, Active Aggregates of Endogenous Proteins Assemble upon Heat Stress

Wallace, E. W. J., Kear‐Scott, J. L., Pilipenko, E. V., Schwartz, M. H., Laskowski, P., Rojek, A. E., Katanski, C. D., Riback, J. A., Dion, M. F., Franks, A. M., et al. (2015) · Cell · doi:10.1016/j.cell.2015.08.041 · Cited by 464 · see citing works

AMP-Activated Protein Kinase: A Target for Drugs both Ancient and Modern

Hardie, D. G., Ross, F. A., & Hawley, S. A. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.08.019 · Cited by 373 · see citing works

Widespread reorganization of metabolic enzymes into reversible assemblies upon nutrient starvation

Narayanaswamy, R., Levy, M., Tsechansky, M., Stovall, G. M., O’Connell, J. D., Mirrielees, J. A., Ellington, A. D., & Marcotte, E. M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812771106 · Cited by 368 · see citing works

High expression of inducible 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (iPFK-2; PFKFB3) in human cancers.

Atsumi, T., Chesney, J. A., Metz, C. N., Leng, L., Donnelly, S. C., Makita, Z., Mitchell, R., & Bucala, R. (2002) · PubMed · Cited by 322 · see citing works

Energy metabolism of tumor cells. Requirement for a form of hexokinase with a propensity for mitochondrial binding.

Bustamante, E., Morris, H. P., & Pedersen, P. L. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68900-3 · Cited by 315 · see citing works

Extracting Accurate Precursor Information for Tandem Mass Spectra by RawConverter

He, L., Diedrich, J. K., Chu, Y.-Y., & Yates, J. R. (2015) · Analytical Chemistry · doi:10.1021/acs.analchem.5b02721 · Cited by 295 · see citing works

Glycolytic enzymes localize to synapses under energy stress to support synaptic function

Jang, S., Nelson, J. C., Bend, E. G., Rodríguez-Laureano, L., Tueros, F. G., Cartagenova, L., Underwood, K., Jorgensen, E. M., & Colón-Ramos, D. A. (2016) · Neuron · doi:10.1016/j.neuron.2016.03.011 · Cited by 270 · see citing works

Reducing Time and Increasing Sensitivity in Sample Preparation for Adherent Mammalian Cell Metabolomics

Lorenz, M. A., Burant, C., & Kennedy, R. T. (2011) · Analytical Chemistry · doi:10.1021/ac103313x · Cited by 233 · see citing works

The conserved oligomeric Golgi complex is involved in double-membrane vesicle formation during autophagy

Yen, W.-L., Shintani, T., Nair, U., Cao, Y., Richardson, B. C., Li, Z., Hughson, F. M., Baba, M., & Klionsky, D. J. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200904075 · Cited by 206 · see citing works

Identification of Edc3p as an Enhancer of mRNA Decapping inSaccharomyces cerevisiae

Kshirsagar, M., & Parker, R. (2004) · Genetics · doi:10.1534/genetics.166.2.729 · Cited by 150 · see citing works

A ‘natural’ mutation in Saccharomyces cerevisiae strains derived from S288c affects the complex regulatory gene HAP1 (CYP1)

Gaisne, M., Bécam, A. ‐., Verdière, J., & Herbert, C. J. (1999) · Current Genetics · doi:10.1007/s002940050490 · Cited by 147 · see citing works

Heme Levels Switch the Function of Hap1 of <i>Saccharomyces cerevisiae</i> between Transcriptional Activator and Transcriptional Repressor

Hickman, M. J., & Winston, F. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00887-07 · Cited by 137 · see citing works

Differential effects of Ydj1 and Sis1 on Hsp70-mediated clearance of stress granules in Saccharomyces cerevisiae

Walters, R. W., Muhlrad, D., Garcia, J. F., & Parker, R. (2015) · RNA · doi:10.1261/rna.053116.115 · Cited by 137 · see citing works

Dynamic Reorganization of Metabolic Enzymes into Intracellular Bodies

O’Connell, J. D., Zhao, A. S., Ellington, A. D., & Marcotte, E. M. (2012) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-101011-155841 · Cited by 135 · see citing works

It’s Raining Liquids: RNA Tunes Viscoelasticity and Dynamics of Membraneless Organelles

Guo, L. E., & Shorter, J. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.10.006 · Cited by 131 · see citing works

Targeting Cancer Metabolism - Revisiting the Warburg Effects

Tran, Q., Lee, H., Park, J., Kim, S., & Park, J. (2016) · Toxicological Research · doi:10.5487/tr.2016.32.3.177 · Cited by 109 · see citing works

Reconstruction of the yeast Snf1 kinase regulatory network reveals its role as a global energy regulator

Usaite, R., Jewett, M. C., Oliveira, A. P., Yates, J. R., Lisbeth Olsson, A., & Nielsen, J. (2009) · Molecular Systems Biology · doi:10.1038/msb.2009.67 · Cited by 108 · see citing works

The Structural and Functional Coordination of Glycolytic Enzymes in Muscle: Evidence of a Metabolon?

Menard, L. M., Maughan, D. W., & Vigoreaux, J. O. (2014) · Biology · doi:10.3390/biology3030623 · Cited by 77 · see citing works

Supramolecular organization of glycolytic enzymes

Kurganov, B. I., Np, S., & Ls, M. (1985) · Journal of Theoretical Biology · doi:10.1016/s0022-5193(85)80086-2 · Cited by 71 · see citing works

Spatial Reorganization of Saccharomyces cerevisiae Enolase To Alter Carbon Metabolism under Hypoxia

Miura, N., Shinohara, M., Tatsukami, Y., Sato, Y., Morisaka, H., Kuroda, K., & Ueda, M. (2013) · Eukaryotic Cell · doi:10.1128/ec.00093-13 · Cited by 57 · see citing works

Phosphoproteomic analysis identifies proteins involved in transcription-coupled mRNA decay as targets of Snf1 signaling

Braun, K. A., Vaga, S., Dombek, K. M., Fang, F., Palmisano, S., Aebersold, R. H., & Young, E. T. (2014) · Science Signaling · doi:10.1126/scisignal.2005000 · Cited by 53 · see citing works

Time-Dependent Profiling of Metabolites from Snf1 Mutant and Wild Type Yeast Cells

Humston, E. M., Dombek, K. M., Hoggard, J. C., Young, E. T., & Synovec, R. E. (2008) · Analytical Chemistry · doi:10.1021/ac800998j · Cited by 44 · see citing works

RNA assemblages orchestrate complex cellular processes

Nielsen, F. C., Hansen, H. T., & Christiansen, J. (2016) · BioEssays · doi:10.1002/bies.201500175 · Cited by 22 · see citing works

[Supramolecular organization of glycolytic enzymes].

Kurganov, B. I., Np, S., & Ls, M. (1986) · PubMed · Cited by 11 · see citing works

Protein Phase Separation: A New Phase in Cell Biology

Boeynaems, S., Alberti, S., Fawzi, N. L., Mittag, T., Polymenidou, M., Rousseau, F., Schymkowitz, J. W. H., Shorter, J., Wolozin, B. L., Bosch, L. V. D., et al. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.02.004 · Cited by 1,954 · see citing works

Regulation of glycolysis by the hypoxia-inducible factor (HIF): Implications for cellular physiology

Kierans, S. J., & Taylor, C. T. (2021) · The Journal of Physiology · doi:10.1113/jp280572 · Cited by 1,015 · see citing works

Targeting ROS in cancer: rationale and strategies

Glorieux, C., Liu, S., Trachootham, D., & Huang, P. (2024) · Nature Reviews Drug Discovery · doi:10.1038/s41573-024-00979-4 · Cited by 700 · see citing works

Spontaneous driving forces give rise to protein−RNA condensates with coexisting phases and complex material properties

Boeynaems, S., Holehouse, A. S., Weinhardt, V., Kovács, D., Lindt, J. V., Larabell, C. A., Bosch, L. V. D., Das, R., Tompa, P., Pappu, R. V., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1821038116 · Cited by 482 · see citing works

Biomolecular Condensates and Cancer

Boija, A., Klein, I. A., & Young, R. A. (2021) · Cancer Cell · doi:10.1016/j.ccell.2020.12.003 · Cited by 320 · see citing works

The role of liquid–liquid phase separation in regulating enzyme activity

O’Flynn, B. G., & Mittag, T. (2021) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2020.12.012 · Cited by 210 · see citing works

A brief guideline for studies of phase-separated biomolecular condensates

Gao, Y., Li, X., Li, P., & Lin, Y. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01204-2 · Cited by 197 · see citing works

Glycolysis: A multifaceted metabolic pathway and signaling hub

Kierans, S. J., & Taylor, C. T. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107906 · Cited by 198 · see citing works

Cellular sensing by phase separation: Using the process, not just the products

Yoo, H., Triandafillou, C. G., & Drummond, D. A. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.tm118.001191 · Cited by 182 · see citing works

Influenza A virus ribonucleoproteins form liquid organelles at endoplasmic reticulum exit sites

Alenquer, M., Vale-Costa, S., Etibor, T. A., Ferreira, F., Sousa, A. L., & Amorim, M. J. (2019) · Nature Communications · doi:10.1038/s41467-019-09549-4 · Cited by 182 · see citing works

HIF-1-Independent Mechanisms Regulating Metabolic Adaptation in Hypoxic Cancer Cells

Lee, S.-H., Golinska, M., & Griffiths, J. R. (2021) · Cells · doi:10.3390/cells10092371 · Cited by 169 · see citing works

Defining the RNA interactome by total RNA‐associated protein purification

Shchepachev, V., Bresson, S. M., Spanos, C., Petfalski, E., Fischer, L., Rappsilber, J., & Tollervey, D. W. (2019) · Molecular Systems Biology · doi:10.15252/msb.20188689 · Cited by 139 · see citing works

Exploring Uncharted Territories of Plant Specialized Metabolism in the Postgenomic Era

Jacobowitz, J. R., & Weng, J. (2020) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-081519-035634 · Cited by 135 · see citing works

RNA Droplets

Rhine, K., Vidaurre, V., & Myong, S. (2020) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-052118-115508 · Cited by 130 · see citing works

Structures, functions, and mechanisms of filament forming enzymes: a renaissance of enzyme filamentation

Park, C. K., & Horton, N. C. (2019) · Biophysical Reviews · doi:10.1007/s12551-019-00602-6 · Cited by 128 · see citing works

Biomolecular condensates in neurodegeneration and cancer

Spannl, S., Tereshchenko, M., Mastromarco, G. J., Ihn, S. J., & Lee, H. O. (2019) · Traffic · doi:10.1111/tra.12704 · Cited by 112 · see citing works

RNA promotes phase separation of glycolysis enzymes into yeast G bodies in hypoxia

Fuller, G. G., Han, T., Freeberg, M., Moresco, J. J., Niaki, A. G., Roach, N. P., Yates, J. R., Myong, S., & Kim, J. K. (2020) · eLife · doi:10.7554/elife.48480 · Cited by 115 · see citing works

Regulation of Cellular Metabolism through Phase Separation of Enzymes

Prouteau, M., & Loewith, R. (2018) · Biomolecules · doi:10.3390/biom8040160 · Cited by 111 · see citing works

Norisoboldine, a natural AhR agonist, promotes Treg differentiation and attenuates colitis via targeting glycolysis and subsequent NAD+/SIRT1/SUV39H1/H3K9me3 signaling pathway

Lv, Q., Wang, K., Qiao, S., Yang, L., Xin, Y., Dai, Y., & Wei, Z. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0297-3 · Cited by 110 · see citing works

Reciprocal regulation of cellular mechanics and metabolism

Evers, T. M. J., Holt, L. J., Alberti, S., & Mashaghi, A. (2021) · Nature Metabolism · doi:10.1038/s42255-021-00384-w · Cited by 103 · see citing works

Compartmentalization and metabolic regulation of glycolysis

Fuller, G. G., & Kim, J. K. (2021) · Journal of Cell Science · doi:10.1242/jcs.258469 · Cited by 104 · see citing works

Stress-related biomolecular condensates in plants

Solís-Miranda, J., Chodasiewicz, M., Skirycz, A., Fernie, A. R., Moschou, P. N., Bozhkov, P. V., & Gutiérrez-Beltrán, E. (2023) · The Plant Cell · doi:10.1093/plcell/koad127 · Cited by 98 · see citing works

Targeting Biomolecular Condensation and Protein Aggregation against Cancer

Silva, J. L., Foguel, D., Ferreira, V. F., Vieira, T. C. R. G., Marques, M. A., Ferretti, G. D. S., Outeiro, T. F., Cordeiro, Y., & de Oliveira, G. A. P. (2023) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00131 · Cited by 85 · see citing works

A quantitative screen for metabolic enzyme structures reveals patterns of assembly across the yeast metabolic network

Noree, C., Begovich, K., Samilo, D., Broyer, R. M., Monfort, E. M., & Wilhelm, J. E. (2019) · Molecular Biology of the Cell · doi:10.1091/mbc.e19-04-0224 · Cited by 85 · see citing works

Advances and opportunities for the design of self-sufficient and spatially organized cell-free biocatalytic systems

Schmid-Dannert, C., & López‐Gallego, F. (2018) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2018.11.021 · Cited by 77 · see citing works

Multiple-Omics Techniques Reveal the Role of Glycerophospholipid Metabolic Pathway in the Response of Saccharomyces cerevisiae Against Hypoxic Stress

Xia, Z., Zhou, X., Li, J., Li, L., Ma, Y., Wu, Y., Huang, Z., Li, X., Xu, P., & Xue, M. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.01398 · Cited by 75 · see citing works

Filament formation by metabolic enzymes—A new twist on regulation

Lynch, E. M., Kollman, J. M., & Webb, B. A. (2020) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2020.04.006 · Cited by 78 · see citing works

Liquid-Liquid Phase Separation: Unraveling the Enigma of Biomolecular Condensates in Microbial Cells

Gao, Z., Zhang, W., Chang, R., Zhang, S., Yang, G., & Zhao, G. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.751880 · Cited by 73 · see citing works

New Perspectives on the Biogenesis of Viral Inclusion Bodies in Negative-Sense RNA Virus Infections

Dolnik, O., Gerresheim, G. K., & Biedenkopf, N. (2021) · Cells · doi:10.3390/cells10061460 · Cited by 69 · see citing works

Hypoxia drives the assembly of the multienzyme purinosome complex

Doigneaux, C., Pedley, A. M., Mistry, I. N., Papayova, M., Benkovic, S. J., & Tavassoli, A. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.012175 · Cited by 65 · see citing works

Reversible amyloids of pyruvate kinase couple cell metabolism and stress granule disassembly

Cereghetti, G., Wilson-Zbinden, C., Kissling, V. M., Diether, M., Arm, A., Yoo, H., Piazza, I., Saad, S., Picotti, P., Drummond, D. A., et al. (2021) · Nature Cell Biology · doi:10.1038/s41556-021-00760-4 · Cited by 64 · see citing works

Phosphofructokinase relocalizes into subcellular compartments with liquid-like properties in vivo

Jang, S., Zhao, X., Lagoy, R. C., Jawerth, L. M., Gonzalez, I. J., Singh, M. K., Prashad, S., Kim, H. S., Patel, A., Albrecht, D. R., et al. (2020) · Biophysical Journal · doi:10.1016/j.bpj.2020.08.002 · Cited by 59 · see citing works

Structural basis for allosteric regulation of human phosphofructokinase-1

Lynch, E. M., Hansen, H., Salay, L. E., Cooper, M. P., Timr, Š., Kollman, J. M., & Webb, B. A. (2024) · Nature Communications · doi:10.1038/s41467-024-51808-6 · Cited by 67 · see citing works

Metabolism of Citrate and Other Carboxylic Acids in Erythrocytes As a Function of Oxygen Saturation and Refrigerated Storage

Nemkov, T. G., Sun, K., Reisz, J. A., Yoshida, T., Dunham, A. J., Wen, E. Y., Wen, A. Q., Roach, R. C., Hansen, K. C., Xia, Y., et al. (2017) · Frontiers in Medicine · doi:10.3389/fmed.2017.00175 · Cited by 62 · see citing works

Reversible, functional amyloids: towards an understanding of their regulation in yeast and humans

Cereghetti, G., Saad, S., Dechant, R. C., & Peter, M. (2018) · Cell Cycle · doi:10.1080/15384101.2018.1480220 · Cited by 58 · see citing works

Intracellular energy production and distribution in hypoxia

Flood, D., Lee, E. S., & Taylor, C. T. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105103 · Cited by 59 · see citing works

Hypoxia induces a glycolytic complex in intestinal epithelial cells independent of HIF-1-driven glycolytic gene expression

Kierans, S. J., Fagundes, R. R., Malkov, M. I., Sparkes, R., Dillon, E., Smolenski, A., Faber, K. N., & Taylor, C. T. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2208117120 · Cited by 56 · see citing works

Roles of liquid–liquid phase separation in bacterial RNA metabolism

Nandana, V., & Schrader, J. M. (2021) · Current Opinion in Microbiology · doi:10.1016/j.mib.2021.03.005 · Cited by 54 · see citing works

Localized glucose import, glycolytic processing, and mitochondria generate a focused ATP burst to power basement-membrane invasion

Garde, A., Kenny-Ganzert, I. W., Kelley, L. C., Chi, Q., Mutlu, A. S., Wang, M. C., & Sherwood, D. R. (2022) · Developmental Cell · doi:10.1016/j.devcel.2022.02.019 · Cited by 49 · see citing works

Organization of a functional glycolytic metabolon on mitochondria for metabolic efficiency

Wang, H., Vant, J., Zhang, A., Sánchez, R. G., Wu, Y., Micou, M. L., Luczak, V., Whiddon, Z. D., Carlson, N. M., Yu, S. B., et al. (2024) · Nature Metabolism · doi:10.1038/s42255-024-01121-9 · Cited by 54 · see citing works

Designer Condensates: A Toolkit for the Biomolecular Architect

Hastings, R., & Boeynaems, S. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.166837 · Cited by 51 · see citing works

Hyperosmotic phase separation: Condensates beyond inclusions, granules and organelles

Jalihal, A. P., Schmidt, A., Gao, G., Little, S. R., Pitchiaya, S., & Walter, N. G. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.rev120.010899 · Cited by 52 · see citing works

A plasma membrane-associated glycolytic metabolon is functionally coupled to KATP channels in pancreatic α and β cells from humans and mice

Ho, T., Potapenko, E., Davis, D., & Merrins, M. (2022) · bioRxiv · doi:10.1016/j.celrep.2023.112394 · Cited by 35 · see citing works

Phase separation in Cancer: From the Impacts and Mechanisms to Treatment potentials

Qiu, P., Tan, S., Xia, L., Wu, N., Oyang, L., Tang, Y., Su, M., Luo, X., Wang, Y., Sheng, X., et al. (2022) · International Journal of Biological Sciences · doi:10.7150/ijbs.75410 · Cited by 48 · see citing works

A-kinase-anchoring protein 1 (dAKAP1)-based signaling complexes coordinate local protein synthesis at the mitochondrial surface

Gabrovsek, L., Collins, K. B., Aggarwal, S., Saunders, L. M., Lau, H.-T., Suh, D., Sancak, Y., Trapnell, C., Ong, S., Smith, F. D., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013454 · Cited by 44 · see citing works

Core Fermentation (CoFe) granules focus coordinated glycolytic mRNA localization and translation to fuel glucose fermentation

Morales-Polanco, F., Bates, C., Lui, J., Casson, J., Solari, C. A., Pizzinga, M., Forte, G., Griffin, C., Garner, K. E. L., Burt, H. E., et al. (2021) · iScience · doi:10.1016/j.isci.2021.102069 · Cited by 43 · see citing works

Melatonin: Regulation of Biomolecular Condensates in Neurodegenerative Disorders

Loh, D., & Reiter, R. J. (2021) · Antioxidants · doi:10.3390/antiox10091483 · Cited by 43 · see citing works

Regulation of Biomolecular Condensates by Poly(ADP-ribose)

Rhine, K., Odeh, H. M., Shorter, J., & Myong, S. (2023) · Chemical Reviews · doi:10.1021/acs.chemrev.2c00851 · Cited by 39 · see citing works

Rewired cellular signaling coordinates sugar and hypoxic responses for anaerobic xylose fermentation in yeast

Myers, K. S., Riley, N. M., MacGilvray, M. E., Sato, T. K., McGee, M. A., Heilberger, J., Coon, J. J., & Gasch, A. P. (2019) · PLoS Genetics · doi:10.1371/journal.pgen.1008037 · Cited by 41 · see citing works

RNA Biology in Retinal Development and Disease

Zelinger, L., & Swaroop, A. (2018) · Trends in Genetics · doi:10.1016/j.tig.2018.01.002 · Cited by 42 · see citing works

The expanding world of metabolic enzymes moonlighting as RNA binding proteins

Curtis, N. J., & Jeffery, C. J. (2021) · Biochemical Society Transactions · doi:10.1042/bst20200664 · Cited by 37 · see citing works

It’s Just a Phase: Exploring the Relationship Between mRNA, Biomolecular Condensates, and Translational Control

Parker, D. M., Winkenbach, L. P., & Nishimura, E. O. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.931220 · Cited by 37 · see citing works

The formation and function of plant metabolons

Dahmani, I., Qin, K., Zhang, Y., & Fernie, A. R. (2023) · The Plant Journal · doi:10.1111/tpj.16179 · Cited by 37 · see citing works

Towards sequence-based principles for protein phase separation predictions

Vendruscolo, M., & Fuxreiter, M. (2023) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2023.102317 · Cited by 38 · see citing works

Biomolecular condensates in photosynthesis and metabolism

Wunder, T., & Mueller‐Cajar, O. (2020) · Current Opinion in Plant Biology · doi:10.1016/j.pbi.2020.08.006 · Cited by 35 · see citing works

The mutual interaction of glycolytic enzymes and RNA in post-transcriptional regulation

Wegener, M., & Dietz, K. (2022) · RNA · doi:10.1261/rna.079210.122 · Cited by 34 · see citing works

Self-organizing glycolytic waves tune cellular metabolic states and fuel cancer progression

Zhan, H., Pal, D. S., Borleis, J. A., Deng, Y., Yu, L., Janetopoulos, C., Huang, C., & Devreotes, P. N. (2025) · Nature Communications · doi:10.1038/s41467-025-60596-6 · Cited by 33 · see citing works

Tumor suppressor protein p53 expressed in yeast can remain diffuse, form a prion, or form unstable liquid-like droplets

Park, S.-K., Park, S., Pentek, C., & Liebman, S. W. (2020) · iScience · doi:10.1016/j.isci.2020.102000 · Cited by 32 · see citing works

Phase separation in fungi

Staples, M. I., Frazer, C., Fawzi, N. L., & Bennett, R. J. (2023) · Nature Microbiology · doi:10.1038/s41564-022-01314-6 · Cited by 32 · see citing works

Glucose restriction drives spatial reorganization of mevalonate metabolism

Rogers, S. W., Hariri, H. H., Wood, N. E., Speer, N. O., & Henne, W. M. (2021) · eLife · doi:10.7554/elife.62591 · Cited by 31 · see citing works

Roles of Phase Separation for Cellular Redox Maintenance

Saito, Y., & Kimura, W. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.691946 · Cited by 30 · see citing works

Metabolic Fuel for Epigenetic: Nuclear Production Meets Local Consumption

Boon, R. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.768996 · Cited by 31 · see citing works

Freedom of assembly: metabolic enzymes come together

Simonet, J. C., Burrell, A. L., Kollman, J. M., & Peterson, J. R. (2020) · Molecular Biology of the Cell · doi:10.1091/mbc.e18-10-0675 · Cited by 30 · see citing works

Oncogenic HSP90 Facilitates Metabolic Alterations in Aggressive B-cell Lymphomas

Calvo-Vidal, M. N., Zamponi, N., Krumsiek, J., Stockslager, M. A., Revuelta, M. V., Phillip, J. M., Marullo, R., Tikhonova, E., Kotlov, N., Patel, J., et al. (2021) · Cancer Research · doi:10.1158/0008-5472.can-21-2734 · Cited by 29 · see citing works

Protein folding and quinary interactions: creating cellular organisation through functional disorder

Ribeiro, S. S., Ebbinghaus, S., & Marcos, J. C. (2018) · FEBS Letters · doi:10.1002/1873-3468.13211 · Cited by 25 · see citing works

Fluid Brain Glycolysis: Limits, Speed, Location, Moonlighting, and the Fates of Glycogen and Lactate

Barros, L. F., Martín, A. S., Ruminot, I., Sandoval, P. Y., Baeza‐Lehnert, F., Arce‐Molina, R., Rauseo, D., Contreras‐Baeza, Y., Galaz, A., & Valdivia, S. (2020) · Neurochemical Research · doi:10.1007/s11064-020-03005-2 · Cited by 27 · see citing works

Co‐opted cytosolic proteins form condensate substructures within membranous replication organelles of a positive‐strand RNA virus

Lin, W., & Nagy, P. D. (2024) · New Phytologist · doi:10.1111/nph.19691 · Cited by 27 · see citing works

Insights into the Role of P-Bodies and Stress Granules in Protein Quality Control

Nostramo, R., Xing, S., Zhang, B., & Herman, P. K. (2019) · Genetics · doi:10.1534/genetics.119.302376 · Cited by 24 · see citing works

Melatonin: Regulation of Prion Protein Phase Separation in Cancer Multidrug Resistance

Loh, D., & Reiter, R. J. (2022) · Molecules · doi:10.3390/molecules27030705 · Cited by 25 · see citing works

A Mathematical Model for Enzyme Clustering in Glucose Metabolism

Jeon, M., Kang, H.-W., & An, S. (2018) · Scientific Reports · doi:10.1038/s41598-018-20348-7 · Cited by 22 · see citing works

TPM4 condensates glycolytic enzymes and facilitates actin reorganization under hyperosmotic stress

Yang, W., Wang, Y., Liu, G., Wang, Y., & Wu, C. (2024) · Cell Discovery · doi:10.1038/s41421-024-00744-2 · Cited by 22 · see citing works

Phase separation in cancer at a glance

Xie, Q., Cheng, J., Mei, W., Yang, D., Zhang, P., & Zeng, C. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04082-x · Cited by 22 · see citing works

Misfolding-prone proteins are reversibly sequestered to an Hsp42-associated granule upon chronological aging

Lee, H., Chao, J.-C., Cheng, K.-Y., & Leu, J. (2018) · Journal of Cell Science · doi:10.1242/jcs.220202 · Cited by 21 · see citing works

Liquid–Liquid Phase Separation in Cancer Signaling, Metabolism and Anticancer Therapy

Igelmann, S., Lessard, F., & Ferbeyre, G. (2022) · Cancers · doi:10.3390/cancers14071830 · Cited by 22 · see citing works

Biomolecular Condensation: A New Phase in Cancer Research

Chakravarty, A. K., McGrail, D. J., Lozanoski, T. M., Dunn, B. S., Shih, D. J. H., Cirillo, K. M., Cetinkaya, S. H., Zheng, W. J., Mills, G. B., Yi, S. S., et al. (2022) · Cancer Discovery · doi:10.1158/2159-8290.cd-21-1605 · Cited by 21 · see citing works

Regulation of reaction fluxes via enzyme sequestration and co-clustering

Hinzpeter, F., Tostevin, F., & Gerland, U. (2019) · Journal of The Royal Society Interface · doi:10.1098/rsif.2019.0444 · Cited by 20 · see citing works

Activation of L-lactate oxidase by the formation of enzyme assemblies through liquid–liquid phase separation

Ura, T., Kagawa, A., Sakakibara, N., Yagi, H., Tochio, N., Kigawa, T., Shiraki, K., & Mikawa, T. (2023) · Scientific Reports · doi:10.1038/s41598-023-28040-1 · Cited by 19 · see citing works

Neuroinflammation is responsible for pain in endometriosis - targeting the JAK-STAT pathway and mast cell activation

Golinska, M. A., Wołyniak, M., Kulesza, P., & Fendler, W. M. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1621178 · Cited by 18 · see citing works

Aging RNA granule dynamics in neurodegeneration

Rhine, K., Al-Azzam, N., Yu, T., & Yeo, G. W. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.991641 · Cited by 15 · see citing works

Exploring Mammalian Genome within Phase-Separated Nuclear Bodies: Experimental Methods and Implications for Gene Expression

Lesne, A., Baudement, M.-O., Rebouissou, C., & Forné, T. (2019) · Genes · doi:10.3390/genes10121049 · Cited by 18 · see citing works

Biomolecular Liquid–Liquid Phase Separation for Biotechnology

Shil, S., Tsuruta, M., Kawauchi, K., & Miyoshi, D. (2023) · BioTech · doi:10.3390/biotech12020026 · Cited by 16 · see citing works

A novel viral strategy for host factor recruitment: The co-opted proteasomal Rpn11 protein interaction hub in cooperation with subverted actin filaments are targeted to deliver cytosolic host factors for viral replication

Molho, M., Lin, W., & Nagy, P. D. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009680 · Cited by 16 · see citing works

Interaction network among de novo purine nucleotide biosynthesis enzymes in Escherichia coli

Gedeon, A., Karimova, G., Ayoub, N., Dairou, J., Gianetto, Q. G., Vichier‐Guerre, S., Vidalain, P., Ladant, D., & Munier‐Lehmann, H. (2023) · FEBS Journal · doi:10.1111/febs.16746 · Cited by 16 · see citing works

Hypoxia-inducible factor-driven glycolytic adaptations in host-microbe interactions

DeMichele, E., Buret, A. G., & Taylor, C. T. (2024) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-024-02953-w · Cited by 15 · see citing works

Known types of membrane-less organelles and biomolecular condensates

Darling, A. L., & Uversky, V. N. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-823967-4.00002-6 · Cited by 15 · see citing works

LncRNA and Protein Expression Profiles Reveal Heart Adaptation to High-Altitude Hypoxia in Tibetan Sheep

He, Z., Li, S., Zhao, F., Sun, H., Hu, J., Wang, J., Liu, X., Li, M., Zhao, Z., & Luo, Y. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms25010385 · Cited by 15 · see citing works

Neurons undergo pathogenic metabolic reprogramming in models of familial ALS

Riechers, S., Mojsilovic‐Petrovic, J., Belton, T. B., Chakrabarty, R. P., Garjani, M., Medvedeva, V., Dalton, C., Wong, Y. C., Chandel, N. S., Dienel, G. A., et al. (2022) · Molecular Metabolism · doi:10.1016/j.molmet.2022.101468 · Cited by 16 · see citing works

The kinetic characteristics of human and trypanosomatid phosphofructokinases for the reverse reaction

Fernandes, P. M., Kinkead, J., McNae, I. W., Bringaud, F., Michels, P. A. M., & Walkinshaw, M. D. (2018) · Biochemical Journal · doi:10.1042/bcj20180635 · Cited by 15 · see citing works

The return of metabolism: biochemistry and physiology of glycolysis

Grüning, N., Agostini, F., Caldana, C., Hartl, J., Heinemann, M., Keller, M. A., Krüsemann, J. L., Lamperti, C., Linster, C. L., Lindner, S. N., et al. (2025) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.70104 · Cited by 16 · see citing works

Size-Specific Modulation of a Multienzyme Glucosome Assembly during the Cell Cycle

Jeon, M., Schmitt, D. L., Kyoung, M., & An, S. (2023) · ACS Bio & Med Chem Au · doi:10.1021/acsbiomedchemau.3c00037 · Cited by 14 · see citing works

Liquid–Liquid Phase Separation in Major Hallmarks of Cancer

Xie, C., Wang, T., Liu, X. P., Wang, Y., Dang, Q., Ding, T., Xu, J., Yu, X., Lin, H. L., Xu, X., et al. (2025) · Cell Proliferation · doi:10.1111/cpr.70122 · Cited by 13 · see citing works

Condensate Formation by Metabolic Enzymes in Saccharomyces cerevisiae

Miura, N. (2022) · Microorganisms · doi:10.3390/microorganisms10020232 · Cited by 13 · see citing works

Protein thiol alterations drive aberrant phase separation in agingPreprint

Vignane, T., Hugo, M., Hoffmann, C., Katsouda, A., Petrić, J., Wang, H., Miler, M., Comas, F., Petrovic, D., Chen, S., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.11.07.566021 · Cited by 13 · see citing works

Toward Design Principles for Biomolecular Condensates for Metabolic Pathways

André, A. A. M., Rehnberg, N., Garg, A., & Kjærgaard, M. (2025) · Advanced Biology · doi:10.1002/adbi.202400672 · Cited by 12 · see citing works

Phase separation as a key mechanism in plant development, environmental adaptation, and abiotic stress response

Pougy, K. D. C., Brito, B. A., Melo, G. S., & Pinheiro, A. S. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108548 · Cited by 12 · see citing works

Enzymes and Liquid-Liquid Phase Separation: A New Era for the Regulation of Enzymatic Activity

Dindo, M., Bevilacqua, A., & Laurino, P. (2023) · Seibutsu Butsuri · doi:10.2142/biophys.63.12 · Cited by 12 · see citing works

Mieap forms membrane-less organelles involved in cardiolipin metabolism

Ikari, N., Honjo, K., Sagami, Y., Nakamura, Y., & Arakawa, H. (2024) · iScience · doi:10.1016/j.isci.2024.108916 · Cited by 12 · see citing works

Artificial Compartments Encapsulating Enzymatic Reactions: Towards the Construction of Artificial Organelles

Lin, P., Zhang, S., Komatsubara, F., Konishi, H., Nakata, E., & Morii, T. (2024) · ChemPlusChem · doi:10.1002/cplu.202400483 · Cited by 12 · see citing works

Biomolecular condensates: A new lens on cancer biology

Jiang, L., & Kang, Y. (2024) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2024.189245 · Cited by 13 · see citing works

Relocation of phosphofructokinases within epithelial cells is a novel event preceding breast cancer recurrence that accurately predicts patient outcomes

Cheung, R. A., Kraft, A. M., & Petty, H. R. (2021) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00176.2021 · Cited by 12 · see citing works

Glycolysis enzymes coalesce in G bodies in hypoxia nucleated by RNA

Fuller, G. G., Freeberg, M., Han, T., & Kim, J. (2020) · The FASEB Journal · doi:10.1096/fasebj.2020.34.s1.01753

Metabolic regulation of yeast Saccharomyces cerevisiae by “G body” formation under hypoxia

Miura, N., & Ueda, M. (2018)

Compartmentalization and metabolic regulation of glycolysis

Fuller, G. G., & Kim, J. K. (2021) · Journal of Cell Science · doi:10.1242/jcs.258469 · Cited by 104 · see citing works

Regulation of glycogen phosphorylase in hypoxic cancer cells

Mung, K. L. (2015) · doi:10.5353/th_b5481909

P01.28.B GLYCOLYTIC CONDENSATES AS A METABOLIC ADAPTATION IN HYPOXIC GLIOBLASTOMA CELLS

Lagunar, E. H., Bravo, C. C., & Sztacho, M. (2025) · Neuro-Oncology · doi:10.1093/neuonc/noaf193.108