Cysteine oxidation triggers amyloid fibril formation of the tumor suppressor p16INK4A

Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the 2−ΔΔCT Method

Livak, K. J., & Schmittgen, T. D. (2001) · Methods · doi:10.1006/meth.2001.1262 · Cited by 180,860 · see citing works

NMRPipe: A multidimensional spectral processing system based on UNIX pipes

Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., & Bax, A. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00197809 · Cited by 15,994 · see citing works

MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification

Cox, J., & Mann, M. (2008) · Nature Biotechnology · doi:10.1038/nbt.1511 · Cited by 14,855 · see citing works

Jalview Version 2—a multiple sequence alignment editor and analysis workbench

Waterhouse, A. M., Procter, J. B., Martin, D. M. A., Clamp, M. E., & Barton, G. J. (2009) · Bioinformatics · doi:10.1093/bioinformatics/btp033 · Cited by 10,011 · see citing works

Global quantification of mammalian gene expression control

Schwanhäusser, B., Busse, D., Li, N., Dittmar, G., Schuchhardt, J., Wolf, J., Chen, W., & Selbach, M. (2011) · Nature · doi:10.1038/nature10098 · Cited by 6,566 · see citing works

Protein Misfolding, Functional Amyloid, and Human Disease

Chiti, F., & Dobson, C. M. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.123901 · Cited by 6,435 · see citing works

Cancer Cell Cycles

Sherr, C. J. (1996) · Science · doi:10.1126/science.274.5293.1672 · Cited by 5,379 · see citing works

Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple

Schafer, F. Q., & Buettner, G. R. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00480-4 · Cited by 4,587 · see citing works

Mutation of the mouse klotho gene leads to a syndrome resembling ageing

Kuro-o, M., Matsumura, Y., Aizawa, H., Kawaguchi, H., Suga, T., Utsugi, T., Ohyama, Y., Kurabayashi, M., Kaname, T., Kume, E., et al. (1997) · Nature · doi:10.1038/36285 · Cited by 3,837 · see citing works

Clearance of p16Ink4a-positive senescent cells delays ageing-associated disorders

Baker, D. J., Wijshake, T., Tchkonia, T., LeBrasseur, N. K., Childs, B. G., van de Sluis, B., Kirkland, J. L., & van Deursen, J. M. (2011) · Nature · doi:10.1038/nature10600 · Cited by 3,670 · see citing works

Modulation of oxidative stress as an anticancer strategy

Gorrini, C., Harris, I. S., & Mak, T. W. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4002 · Cited by 3,579 · 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 CCPN data model for NMR spectroscopy: Development of a software pipeline

Vranken, W., Boucher, W., Stevens, T. J., Fogh, R. H., Pajon, A., Llinás, M., Ulrich, E. L., Markley, J. L., Ionides, J., & Laue, E. D. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20449 · Cited by 3,222 · see citing works

Naturally occurring p16Ink4a-positive cells shorten healthy lifespan

Baker, D. J., Childs, B. G., Durik, M., Wijers, M. E., Sieben, C. J., Zhong, J., A. Saltness, R., Jeganathan, K. B., Verzosa, G. C., Pezeshki, A., et al. (2016) · Nature · doi:10.1038/nature16932 · Cited by 2,891 · see citing works

Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade

Chiti, F., & Dobson, C. M. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045115 · Cited by 2,629 · see citing works

Ensembl 2018

Zerbino, D. R., Achuthan, P., Akanni, W., Amode, M. R., Barrell, D., Bhai, J., Billis, K., Cummins, C., Gall, A., Girón, C. G., et al. (2018) · Nucleic Acids Research · doi:10.1093/nar/gkx1098 · Cited by 2,605 · see citing works

Visualizing Spatiotemporal Dynamics of Multicellular Cell-Cycle Progression

Sakaue-Sawano, A., Kurokawa, H., Morimura, T., Hanyu, A., Hama, H., Osawa, H., Kashiwagi, S., Fukami, K., Miyata, T., Miyoshi, H., et al. (2008) · Cell · doi:10.1016/j.cell.2007.12.033 · Cited by 2,123 · see citing works

Cellular mechanisms and physiological consequences of redox-dependent signalling

Holmström, K. M., & Finkel, T. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3801 · Cited by 2,093 · 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

COSMIC: somatic cancer genetics at high-resolution

Forbes, S. A., Beare, D., Boutselakis, H., Bamford, S., Bindal, N., Tate, J., Cole, C. G., Ward, S., Dawson, E., Ponting, L., et al. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkw1121 · Cited by 1,922 · see citing works

Common core structure of amyloid fibrils by synchrotron X-ray diffraction.

Sunde, M., Serpell, L., Bartlam, M., Fraser, P., Pepys, M., & Blake, C. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1348 · Cited by 1,666 · see citing works

Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins

Fernández‐Escamilla, A. M., Rousseau, F., Schymkowitz, J. W. H., & Serrano, L. G. (2004) · Nature Biotechnology · doi:10.1038/nbt1012 · Cited by 1,663 · see citing works

EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers

Ehrnhoefer, D. E., Bieschke, J., Boeddrich, A., Herbst, M., Masino, L., Lurz, R., Engemann, S., Pastore, A., & Wanker, E. (2008) · Nature Structural &Molecular Biology · doi:10.1038/nsmb.1437 · Cited by 1,424 · see citing works

[18] Quantification of β-sheet amyloid fibril structures with thioflavin T

LeVine, H. (1999) · Methods in Enzymology · doi:10.1016/s0076-6879(99)09020-5 · Cited by 1,365 · see citing works

ATSAS 2.8 : a comprehensive data analysis suite for small-angle scattering from macromolecular solutions

Franke, D., Petoukhov, M. V., Konarev, P. V., Panjkovich, A., Tuukkanen, A. T., Mertens, H. D. T., Kikhney, A., Hajizadeh, N. R., Franklin, J. M., Jeffries, C. M., et al. (2017) · Journal of Applied Crystallography · doi:10.1107/s1600576717007786 · Cited by 1,271 · see citing works

The RIP1/RIP3 Necrosome Forms a Functional Amyloid Signaling Complex Required for Programmed Necrosis

Li, J., McQuade, T., Siemer, A. B., Napetschnig, J., Moriwaki, K., Hsiao, Y.-S., Damko, E., Moquin, D., Walz, T., McDermott, A., et al. (2012) · Cell · doi:10.1016/j.cell.2012.06.019 · Cited by 1,222 · see citing works

AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides

Conchillo‐Solé, O., de Groot, N. S., Avilés, F. X., Vendrell, J., Daura, X., & Ventura, S. (2007) · BMC Bioinformatics · doi:10.1186/1471-2105-8-65 · Cited by 1,058 · see citing works

Functional Amyloids As Natural Storage of Peptide Hormones in Pituitary Secretory Granules

Maji, S. K., Perrin, M. H., Sawaya, M. R., Jessberger, S., Vadodaria, K. C., Rissman, R. A., Singru, P. S., Nilsson, K. P. R., Simon, R. A., Schubert, D. A., et al. (2009) · Science · doi:10.1126/science.1173155 · Cited by 1,051 · see citing works

Tau phosphorylation: the therapeutic challenge for neurodegenerative disease

Hanger, D. P., Anderton, B. H., & Noble, W. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2009.01.003 · Cited by 965 · see citing works

Techniques to study amyloid fibril formation in vitro

NILSSON, M. (2004) · Methods · doi:10.1016/j.ymeth.2004.03.012 · Cited by 948 · see citing works

Expression of transcription factor E2F1 induces quiescent cells to enter S phase

Johnson, D. G., Schwarz, J. K., Cress, W. D., & Nevins, J. R. (1993) · Nature · doi:10.1038/365349a0 · Cited by 943 · see citing works

Functional Amyloid Formation within Mammalian Tissue

Fowler, D. M., Koulov, A. V., Alory, C., Marks, M. S., Balch, W. E., & Kelly, J. W. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0040006 · Cited by 824 · see citing works

Structure of FUS Protein Fibrils and Its Relevance to Self-Assembly and Phase Separation of Low-Complexity Domains

Murray, D. T., Kato, M., Lin, Y., Thurber, K. R., Hung, I., McKnight, S. L., & Tycko, R. (2017) · Cell · doi:10.1016/j.cell.2017.08.048 · Cited by 740 · see citing works

FTIR reveals structural differences between native β‐sheet proteins and amyloid fibrils

Zandomeneghi, G., Krebs, M. R. H., McCammon, M. G., & Fändrich, M. (2004) · Protein Science · doi:10.1110/ps.041024904 · Cited by 725 · see citing works

The invasin D protein from Yersinia pseudotuberculosis selectively binds the Fab region of host antibodies and affects colonization of the intestine

Sadana, P., Geyer, R., Pezoldt, J., Helmsing, S., Huehn, J., Hust, M., Dersch, P., & Scrima, A. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.001068 · Cited by 723 · see citing works

Molecular basis for amyloid fibril formation and stability

Makin, O. S., Atkins, E. D. T., Sikorski, P., Johansson, J., & Serpell, L. C. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0406847102 · Cited by 649 · see citing works

Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation.

Klunk, W. E., Pettegrew, J. W., & Abraham, D. J. (1989) · Journal of Histochemistry & Cytochemistry · doi:10.1177/37.8.2666510 · Cited by 625 · see citing works

Quantitative proteomics reveals subset-specific viral recognition in dendritic cells

Luber, C. A., Cox, J., Lauterbach, H., Fancke, B., Selbach, M., Tschopp, J., Akira, S., Wiegand, M., Hochrein, H., O'Keeffe, M., et al. (2010) · Immunity · doi:10.1016/j.immuni.2010.01.013 · Cited by 576 · see citing works

Structural basis for inhibition of the cyclin-dependent kinase Cdk6 by the tumour suppressor p16INK4a

Russo, A. A., Tong, L., Lee, J.-O., Jeffrey, P. D., & Pavletich, N. P. (1998) · Nature · doi:10.1038/26155 · Cited by 524 · see citing works

Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4

Stepanova, L., Leng, X., Parker, S. B., & Harper, J. W. (1996) · Genes & Development · doi:10.1101/gad.10.12.1491 · Cited by 483 · see citing works

PASTA 2.0: an improved server for protein aggregation prediction

Walsh, I., Seno, F., Tosatto, S. C. E., & Trovato, A. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku399 · Cited by 475 · see citing works

ATR-FTIR: A “rejuvenated” tool to investigate amyloid proteins

Sarroukh, R., Goormaghtigh, E., Ruysschaert, J., & Raussens, V. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.04.012 · Cited by 449 · see citing works

Probability‐based protein secondary structure identification using combined NMR chemical‐shift data

Wang, Y., & Jardetzky, O. (2002) · Protein Science · doi:10.1110/ps.3180102 · Cited by 447 · see citing works

Prediction of Aggregation-Prone Regions in Structured Proteins

Tartaglia, G. G., Pawar, A. P., Campioni, S., Dobson, C. M., Chiti, F., & Vendruscolo, M. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.05.013 · Cited by 437 · see citing works

Growth suppression by p16ink4 requires functional retinoblastoma protein

Medema, R. H., Herrera, R. E., Lam, F., & Weinberg, R. A. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.14.6289 · Cited by 433 · see citing works

Metastability of Native Proteins and the Phenomenon of Amyloid Formation

Baldwin, A. J., Knowles, T. P. J., Tartaglia, G. G., Fitzpatrick, A. W. P., Devlin, G. L., Shammas, S. L., Waudby, C. A., Mossuto, M. F., Meehan, S., Gras, S. L., et al. (2011) · Journal of the American Chemical Society · doi:10.1021/ja2017703 · Cited by 428 · see citing works

Monitoring Tumorigenesis and Senescence In Vivo with a p16INK4a-Luciferase Model

Burd, C. E., Sorrentino, J. A., Clark, K. S., Darr, D. B., Krishnamurthy, J., Deal, A. M., Bardeesy, N., Castrillon, D. H., Beach, D. H., & Sharpless, N. E. (2013) · Cell · doi:10.1016/j.cell.2012.12.010 · Cited by 419 · see citing works

Observation of spin exchange by two-dimensional fourier transform 13C cross polarization-magic-angle spinning

Szeverenyi, N. M., Sullivan, M. J., & Maciel, G. E. (1982) · Journal of Magnetic Resonance (1969) · doi:10.1016/0022-2364(82)90213-x · Cited by 411 · see citing works

Cysteine Function Governs Its Conservation and Degeneration and Restricts Its Utilization on Protein Surfaces

Marino, S. M., & Gladyshev, V. N. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.09.027 · Cited by 394 · see citing works

The Structure of the Necrosome RIPK1-RIPK3 Core, a Human Hetero-Amyloid Signaling Complex

Mompeán, M., Li, W., Li, J., Laage, S., Siemer, A. B., Bozkurt, G., Wu, H., & McDermott, A. E. (2018) · Cell · doi:10.1016/j.cell.2018.03.032 · Cited by 337 · see citing works

A redox cycle within the cell cycle: ring in the old with the new

Menon, S. G., & Goswami, P. C. (2006) · Oncogene · doi:10.1038/sj.onc.1209895 · Cited by 294 · see citing works

Tumor suppressor genes and ROS: complex networks of interactions

Vurusaner, B., Poli, G., & Başağa, H. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.09.035 · Cited by 292 · see citing works

Proteome-wide analysis of cysteine oxidation reveals metabolic sensitivity to redox stress

van der Reest, J., Lilla, S., Zheng, L., Zanivan, S. R., & Gottlieb, E. (2018) · Nature Communications · doi:10.1038/s41467-018-04003-3 · Cited by 267 · see citing works

Initiation and elongation in fibrillation of ALS-linked superoxide dismutase

Chattopadhyay, M., Durazo, A., Sohn, S. H., Strong, C. D., Gralla, E. B., Whitelegge, J. P., & Valentine, J. S. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807058105 · Cited by 228 · see citing works

Cross‐seeding effects of amyloid β‐protein and α‐synuclein

Ono, K., Takahashi, R., Ikeda, T., & Yamada, M. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2012.07847.x · Cited by 213 · see citing works

A role for 2-Cys peroxiredoxins in facilitating cytosolic protein thiol oxidation

Stöcker, S., Maurer, M. J., Ruppert, T., & Dick, T. P. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2536 · Cited by 209 · see citing works

Complete Loss of Post-translational Modifications Triggers Fibrillar Aggregation of SOD1 in the Familial Form of Amyotrophic Lateral Sclerosis

Furukawa, Y., Kaneko, K., Yamanaka, K., O’Halloran, T. V., & Nukina, N. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802083200 · Cited by 207 · see citing works

The Expanding Landscape of the Thiol Redox Proteome

Yang, J. H., Carroll, K. S., & Liebler, D. C. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o115.056051 · Cited by 205 · see citing works

Necroptosis in neurodegenerative diseases: a potential therapeutic target

Zhang, S., Tang, M., Luo, H., Shi, C.-H., & Xu, Y.-M. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.286 · Cited by 198 · see citing works

Redox State Controls Phase Separation of the Yeast Ataxin-2 Protein via Reversible Oxidation of Its Methionine-Rich Low-Complexity Domain

Kato, M., Yang, Y.-S., Sutter, B. M., Wang, Y., McKnight, S. L., & Tu, B. P. (2019) · Cell · doi:10.1016/j.cell.2019.02.044 · Cited by 169 · see citing works

Redox-Dependent Control of FOXO/DAF-16 by Transportin-1

Putker, M., Madl, T., Vos, H. R., de Ruiter, H., Visscher, M., van den Berg, M. C. W., Kaplan, M., Korswagen, H. C., Boelens, R., Vermeulen, M., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.12.014 · Cited by 163 · see citing works

A complex of Kif18b and MCAK promotes microtubule depolymerization and is negatively regulated by Aurora kinases

Tanenbaum, M. E., Macurek, L., van der Vaart, B., Galli, M., Akhmanova, A., & Medema, R. H. (2011) · Current Biology · doi:10.1016/j.cub.2011.07.017 · Cited by 148 · see citing works

The Role of Disulfide Bridge in the Folding and Stability of the Recombinant Human Prion Protein

Maiti, N. R., & Surewicz, W. K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007862200 · Cited by 112 · see citing works

TDP-43 Inclusion Bodies Formed in Bacteria Are Structurally Amorphous, Non-Amyloid and Inherently Toxic to Neuroblastoma Cells

Capitini, C., Conti, S., Perni, M., Guidi, F., Cascella, R., Poli, A. D., Penco, A., Relini, A., Cecchi, C., & Chiti, F. (2014) · PLoS ONE · doi:10.1371/journal.pone.0086720 · Cited by 88 · see citing works

Statistics for proteomics: Experimental design and 2-DE differential analysis

Chich, J., David, O., Villers, F., Schaeffer, B., Lutomski, D., & Huet, S. (2006) · Journal of Chromatography B · doi:10.1016/j.jchromb.2006.09.033 · Cited by 86 · see citing works

Reversible Amyloid Formation by the p53 Tetramerization Domain and a Cancer-associated Mutant

Lee, A. S., Galea, C. A., DiGiammarino, E. L., Jun, B., Murti, G., Ribeiro, R. C., Zambetti, G. P., Schultz, C. P., & Kriwacki, R. W. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00175-x · Cited by 81 · see citing works

Disulfide bonds in amyloidogenesis diseases related proteins

Li, Y., Yan, J., Zhang, X., & Huang, K. (2013) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24338 · Cited by 65 · see citing works

Disulfide Bonds Reduce the Toxicity of the Amyloid Fibrils Formed by an Extracellular Protein

Mossuto, M. F., Bolognesi, B., Guixer, B., Dhulesia, A., Agostini, F., Kumita, J. R., Tartaglia, G. G., Dumoulin, M., Dobson, C. M., & Salvatella, X. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201100986 · Cited by 64 · see citing works

Amyloid by Design: Intrinsic Regulation of Microbial Amyloid Assembly

Deshmukh, M. G., Evans, M. L., & Chapman, M. R. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.07.007 · Cited by 51 · see citing works

Dissecting the role of disulfide bonds on the amyloid formation of insulin

Li, Y., Gong, H., Sun, Y., Yan, J., Cheng, B., Zhang, X., Huang, J., Yu, M., Guo, Y., Zheng, L., et al. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.05.133 · Cited by 50 · see citing works

Autophagy regulates the localization and degradation of p16 INK4a

Coryell, P., Goraya, S. K., Griffin, K. A., Redick, M. A., Sisk, S. R., & Purvis, J. E. (2020) · Aging Cell · doi:10.1111/acel.13171 · Cited by 46 · see citing works

Role of the Disulfide Bond in Prion Protein Amyloid Formation: A Thermodynamic and Kinetic Analysis

Honda, R. P. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2017.12.031 · Cited by 30 · see citing works

Reversible disulfide bond formation of intracellular proteins probed by NMR spectroscopy

Piotukh, K., Kosslick, D., Zimmermann, J., Krause, E., & Freund, C. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.06.010 · Cited by 24 · see citing works

Analysis of the putative tumor suppressor gene cdkn2ab in pigment cells and melanoma of Xiphophorus and medaka

Regneri, J., Klotz, B. J., Wilde, B., Kottler, V. A., Hausmann, M., Kneitz, S., Regensburger, M., Maurus, K., Götz, R., Lü, Y., et al. (2018) · Pigment Cell & Melanoma Research · doi:10.1111/pcmr.12729 · Cited by 22 · see citing works

Cancer metabolism and tumor microenvironment: fostering each other?

Yuan, Y., Li, H., Wang, P., Chen, L., Guo, D. S., Jiang, H., He, B., Qin, S., Wang, K., Li, N., et al. (2021) · Science China Life Sciences · doi:10.1007/s11427-021-1999-2 · Cited by 138 · see citing works

Cross-talk between redox signalling and protein aggregation

van Dam, L., & Dansen, T. B. (2020) · Biochemical Society Transactions · doi:10.1042/bst20190054 · Cited by 53 · see citing works

Endogenous SO2-dependent Smad3 redox modification controls vascular remodeling

Huang, Y., Li, Z., Zhang, L., Tang, H., Zhang, H., Wang, C., Chen, S. Y., Bu, D., Zhang, Z., Zhu, Z., et al. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101898 · Cited by 50 · see citing works

Functional Amyloids: Where Supramolecular Amyloid Assembly Controls Biological Activity or Generates New Functionality

Buchanan, J. A., Varghese, N. R., Johnston, C. L., & Sunde, M. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167919 · Cited by 39 · see citing works

The Cys Sense: Thiol Redox Switches Mediate Life Cycles of Cellular Proteins

Radzinski, M., Oppenheim, T., Metanis, N., & Reichmann, D. (2021) · Biomolecules · doi:10.3390/biom11030469 · Cited by 40 · see citing works

Herpes simplex virus encoded ICP6 protein forms functional amyloid assemblies with necroptosis-associated host proteins.

Shanmugam, N., Baker, M., Sanz-Hernández, M., Sierecki, E., Gambin, Y., Steain, M., Pham, C. L. L., & Sunde, M. (2020) · Biophysical Chemistry · doi:10.1016/j.bpc.2020.106524 · Cited by 29 · see citing works

Regulation of Functional Protein Aggregation by Multiple Factors: Implications for the Amyloidogenic Behavior of the CAP Superfamily Proteins

Sheng, J., Olrichs, N. K., Gadella, B. M., Kaloyanova, D. V., & Helms, J. B. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186530 · Cited by 25 · see citing works

Cyclin D-CDK4 Disulfide Bond Attenuates Pulmonary Vascular Cell Proliferation

Knight, H., Abis, G., Kaur, M., Green, H. L. H., Krasemann, S., Hartmann, K., Lynham, S., Clark, J., Zhao, L., Ruppert, C., et al. (2023) · Circulation Research · doi:10.1161/circresaha.122.321836 · Cited by 25 · see citing works

Native disulphide-linked dimers facilitate amyloid fibril formation by bovine milk αS2-casein

Thorn, D. C., Bahraminejad, E., Grosas, A. B., Koudelka, T., Hoffmann, P., Mata, J. P., Devlin, G. L., Sunde, M., Ecroyd, H. W., Holt, C., et al. (2020) · Biophysical Chemistry · doi:10.1016/j.bpc.2020.106530 · Cited by 18 · see citing works

How is the Amyloid Fold Built? Polymorphism and the Microscopic Mechanisms of Fibril Assembly

Aubrey, L. D., & Radford, S. E. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169008 · Cited by 17 · see citing works

Dihydroartemisinin induces cell apoptosis through repression of UHRF1 in prostate cancer cells

Xia, T., Liu, S., Xu, G., Zhou, S., & Luo, Z. (2021) · Anti-Cancer Drugs · doi:10.1097/cad.0000000000001156 · Cited by 16 · see citing works

Amyloid formation of fish β-parvalbumin involves primary nucleation triggered by disulfide-bridged protein dimers

Werner, T., Bernson, D., Esbjörner, E. K., Rocha, S., & Wittung-Stafshede, P. E. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2015503117 · Cited by 15 · see citing works

Oxidation Promotes Distinct Huntingtin Aggregates in the Presence and Absence of Membranes

Adegbuyiro, A., Stonebraker, A. R., Sedighi, F., Fan, C. K., Hodges, B. L., Li, P., Valentine, S. J., & Legleiter, J. A. (2022) · Biochemistry · doi:10.1021/acs.biochem.2c00212 · Cited by 15 · see citing works

Bioinformatic identification of previously unrecognized amyloidogenic proteins

Rosenberg, G. M., Murray, K., Salwínski, L., Hughes, M., Abskharon, R., & Eisenberg, D. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101920 · Cited by 11 · see citing works

Amyloid formation and depolymerization of tumor suppressor p16INK4a are regulated by a thiol-dependent redox mechanism

Heath, S. G., Gray, S. G., Hamzah, E. M., O'Connor, K. M., Bozonet, S. M., Botha, A. D., de Cordovez, P., Magon, N. J., Naughton, J. D., Goldsmith, D. L. W., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-49581-7 · Cited by 11 · see citing works

Conserved cysteine-switches for redox sensing operate in the cyclin-dependent kinase inhibitor p21(CIP/KIP) protein family

Montero, L., Okraine, Y. V., Orlowski, J., Matzkin, S., Scarponi, I., Miranda, M. V., Nusblat, A. D., Gottifredi, V., & Alonso, L. G. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.09.013 · Cited by 11 · see citing works

Mitochondria inter-organelle relationships in cancer protein aggregation

Genovese, I., Fornetti, E., & Ruocco, G. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.1062993 · Cited by 11 · see citing works

Reaction of N-Acetylcysteine with Cu2+: Appearance of Intermediates with High Free Radical Scavenging Activity: Implications for Anti-/Pro-Oxidant Properties of Thiols

Valent, I., Bednářová, L., Schreiber, I., Bujdák, J., Valachová, K., & Šoltés, L. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23116199 · Cited by 6 · see citing works

Oxidation-sensitive cysteines drive IL-38 amyloid formation

Díaz-Barreiro, A., Cereghetti, G., Ortega, F. G., Tonacini, J., Talabot‐Ayer, D., Kieffer‐Jaquinod, S., Kissling, V. M., Huard, A., Swale, C., Knowles, T. P. J., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114940 · Cited by 5 · see citing works

Cysteine Redox State Governs the Condensation Pathway of Hendra Virus W Protein and Differentially Impacts Type I IFN and NF‐κB Signaling

Gondelaud, F., Lalande, A., Pesce, G., Bouchet, A., Meunier, C., Bignon, C., Ptchelkine, D., Gu, Y., Ogire, E., Lozach, P., et al. (2026) · Advanced Science · doi:10.1002/advs.202523465 · Cited by 4 · see citing works

Characterizing the amyloid core region of the tumor suppressor protein p16INK4a using a limited proteolysis and peptide-based approach

Heath, S. G., Naughton, J. D., Magon, N. J., Gray, S. G., Smith, B. R., Morris, V. K., & Göbl, C. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107590 · Cited by 3 · see citing works

ROS and the cell cycle: Cycling in and out of the comfort zone of redox control

Hsiu, O. O. N., & Poon, R. Y. C. (2026) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2026.102613 · Cited by 2 · see citing works

1H, 13C, 15N backbone chemical shift assignment of P18ink4c from Danio rerio (zebrafish) using solution-state NMR spectroscopy

Sethi, A., de Cordovez, P., Mohanty, B., Morris, V. K., & Göbl, C. (2025) · Biomolecular NMR Assignments · doi:10.1007/s12104-025-10245-2 · Cited by 1 · see citing works

Redox proteomics of PANC-1 cells reveals the significance of HIF-1 signaling protein oxidation in pancreatic ductal adenocarcinoma pathogenesis

Tan, C., Chen, L.-C., Guan, X., Huang, W., Feng, Y., Li, Z., Wu, L., Huang, X., Ouyang, Q., Liu, S., et al. (2024) · Journal of Translational Medicine · doi:10.1186/s12967-024-05068-z · Cited by 1 · see citing works

Huntingtin aggregation at interfaces associated with membranes and organelles

Adegbuyiro, A. (2021) · doi:10.33915/etd.8315 · Cited by 1 · see citing works

The amyloidogenic properties of the CAP superfamily proteins

Sheng, J. (2020) · doi:10.33540/530

Cellular response to compartmentalized redox alterations

Revazian, A. (2022) · doi:10.53846/goediss-9408

Additional file 2 of Redox proteomics of PANC-1 cells reveals the significance of HIF-1 signaling protein oxidation in pancreatic ductal adenocarcinoma pathogenesis

Tan, C., Chen, L., Guan, X., Huang, W., Feng, Y., Li, Z., Wu, L., Huang, X., Ouyang, Q., Liu, S., et al. (2024) · Figshare · doi:10.6084/m9.figshare.25424817

Additional file 1 of Redox proteomics of PANC-1 cells reveals the significance of HIF-1 signaling protein oxidation in pancreatic ductal adenocarcinoma pathogenesis

Tan, C., Chen, L., Guan, X., Huang, W., Feng, Y., Li, Z., Wu, L., Huang, X., Ouyang, Q., Liu, S., et al. (2024) · Figshare · doi:10.6084/m9.figshare.25424780

Additional file 3 of Redox proteomics of PANC-1 cells reveals the significance of HIF-1 signaling protein oxidation in pancreatic ductal adenocarcinoma pathogenesis

Tan, C., Chen, L., Guan, X., Huang, W., Feng, Y., Li, Z., Wu, L., Huang, X., Ouyang, Q., Liu, S., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26694414

The impact of physiological oxidants on triggering amyloid formation of the cell cycle regulator protein p16 INK4A

Smith, B. R., Magon, N. J., Sethi, A., Gray, S. G., Heath, S. G., Morris, V. K., & Göbl, C. (2026) · Protein Science · doi:10.1002/pro.70723

Amyloid formation and depolymerization of tumor suppressor p16INK4a are regulated by a thiol-dependent redox mechanism

Heath, S. G., Gray, S. G., Hamzah, E. M., O'Connor, K. M., Bozonet, S. M., Botha, A. D., de Cordovez, P., Magon, N. J., Naughton, J. D., Goldsmith, D. L. W., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-49581-7 · Cited by 11 · see citing works

The impact of physiological oxidants on triggering amyloid formation of the cell cycle regulator protein p16 INK4A

Smith, B. R., Magon, N. J., Sethi, A., Gray, S. G., Heath, S. G., Morris, V. K., & Göbl, C. (2026) · Protein Science · doi:10.1002/pro.70723

Oxidation of the tumour suppressor p15INK4b triggers aggregation into an amyloid-like state

Ramana, J. (2025) · Otago University Research Archive (University of Otago)

Understanding the mechanism of amyloid fibril formation of human tumour suppressor p16INK4a through cancer associated and hyper-stable variants,

Gray, S. G. (2023) · University of Canterbury Research Repository (University of Canterbury) · doi:10.26021/14743

Exploring the response of p16ᴵᴺᴷ⁴ᵃ to oxidation in human cells

Botha, A. (2024) · Otago University Research Archive (University of Otago)