C-Phycocyanin from Spirulina Inhibits α-Synuclein and Amyloid-β Fibril Formation but Not Amorphous Aggregation

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

Molecular chaperones in protein folding and proteostasis

Hartl, F. U., Bracher, A., & Hayer-Hartl, M. K. (2011) · Nature · doi:10.1038/nature10317 · Cited by 3,525 · 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

Accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson disease

Conway, K. A., Harper, J. D., & Lansbury, P. T. (1998) · Nature Medicine · doi:10.1038/3311 · Cited by 1,501 · see citing works

Chaperone machines for protein folding, unfolding and disaggregation

Saibil, H. R. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3658 · Cited by 1,174 · see citing works

Evidence for a Partially Folded Intermediate in α-Synuclein Fibril Formation

Uversky, V. N., Li, J., & Fink, A. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010907200 · Cited by 1,096 · see citing works

Ion mobility–mass spectrometry analysis of large protein complexes

Ruotolo, B. T., Benesch, J. L. P., Sandercock, A. M., Hyung, S., & Robinson, C. V. (2008) · Nature Protocols · doi:10.1038/nprot.2008.78 · Cited by 1,095 · see citing works

Conformational properties of α-synuclein in its free and lipid-associated states 1 1Edited by P. E. Wright

Eliezer, D., Kutluay, E., Bussell, R., & Browne, G. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4538 · Cited by 1,077 · see citing works

EGCG remodels mature α-synuclein and amyloid-β fibrils and reduces cellular toxicity

Bieschke, J., Russ, J., Friedrich, R., Ehrnhoefer, D. E., Wobst, H. J., Neugebauer, K., & Wanker, E. (2010) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0910723107 · Cited by 986 · 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

Native mass spectrometry: a bridge between interactomics and structural biology

Heck, A. J. R. (2008) · Nature Methods · doi:10.1038/nmeth.1265 · Cited by 766 · see citing works

C-Phycocyanin: A Biliprotein with Antioxidant, Anti-Inflammatory and Neuroprotective Effects

Romay, C., Gonzalez, R., Ledón, N., Remírez, D., & Rimbau, V. (2003) · Current Protein and Peptide Science · doi:10.2174/1389203033487216 · Cited by 718 · see citing works

Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry

Hernández, H., & Robinson, C. V. (2007) · Nature Protocols · doi:10.1038/nprot.2007.73 · Cited by 655 · see citing works

Quantitative determination of noncovalent binding interactions using soft ionization mass spectrometry

Daniel, J. M., Friess, S. D., Sudha, R., Wendt, S., & Zenobi, R. (2002) · International Journal of Mass Spectrometry · doi:10.1016/s1387-3806(02)00585-7 · Cited by 473 · see citing works

Protein misfolding and aggregation in cataract disease and prospects for prevention

Moreau, K. L., & King, J. A. (2012) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2012.03.005 · Cited by 461 · see citing works

Gymnastics of Molecular Chaperones

Mayer, M. P. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.07.012 · Cited by 364 · see citing works

Relationships between the Sequence of α-Synuclein and its Membrane Affinity, Fibrillization Propensity, and Yeast Toxicity

Volles, M. J., & Lansbury, P. T. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.12.044 · Cited by 247 · see citing works

Structure and Mechanism of Protein Stability Sensors: Chaperone Activity of Small Heat Shock Proteins

Mchaourab, H. S., Godar, J. A., & Stewart, P. L. (2009) · Biochemistry · doi:10.1021/bi900212j · Cited by 240 · see citing works

Small molecule inhibitors of amyloid β peptide aggregation as a potential therapeutic strategy for Alzheimer's disease

Nie, Q., Du, X., & Geng, M. (2011) · Acta Pharmacologica Sinica · doi:10.1038/aps.2011.14 · Cited by 239 · see citing works

Structure of beta-crystallite assemblies formed by Alzheimer beta-amyloid protein analogues: analysis by x-ray diffraction.

Inouye, H., Fraser, P., & Kirschner, D. (1993) · Biophysical Journal · doi:10.1016/s0006-3495(93)81393-6 · Cited by 239 · see citing works

Heat Shock Protein 70 Inhibits α-Synuclein Fibril Formation via Preferential Binding to Prefibrillar Species

Dedmon, M. M., Christodoulou, J. C., Wilson, M. R., & Dobson, C. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413024200 · Cited by 235 · see citing works

Interaction of the Molecular Chaperone αB-Crystallin with α-Synuclein: Effects on Amyloid Fibril Formation and Chaperone Activity

Rekas, A., Adda, C. G., Aquilina, J. A., Barnham, K. J., Sunde, M., Galatis, D., Williamson, N. A., Masters, C. L., Anders, R. F., Robinson, C. V., et al. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.05.054 · Cited by 223 · see citing works

Hepatoprotective Effect of C-Phycocyanin: Protection for Carbon Tetrachloride andR-(+)-Pulegone-Mediated Hepatotoxicty in Rats

Bhat, V. B., Gaikwad, N. W., & Madyastha, K. M. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.9149 · Cited by 215 · see citing works

Chaperonins: two rings for folding

Yébenes, H., Mesa, P., Muñoz, I. G., Montoya, G., & Valpuesta, J. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.05.003 · Cited by 162 · see citing works

In Vitro Antioxidant and Antiproliferative Activities of Selenium-Containing Phycocyanin from Selenium-Enriched<i>Spirulina platensis</i>

Chen, T., & Wong, Y.-S. (2008) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf073399k · Cited by 157 · see citing works

α-Synuclein: Stable compact and extended monomeric structures and pH dependence of dimer formation

Bernstein, S. L., Liu, D., Wyttenbach, T., Bowers, M. T., Lee, J. C., Gray, H. B., & Winkler, J. R. (2004) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2004.08.003 · Cited by 154 · see citing works

The Interaction of αB-Crystallin with Mature α-Synuclein Amyloid Fibrils Inhibits Their Elongation

Waudby, C. A., Knowles, T. P. J., Devlin, G. L., Skepper, J. N., Ecroyd, H. W., Carver, J. A., Welland, M. E., Christodoulou, J. C., Dobson, C. M., & Meehan, S. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2009.10.056 · Cited by 154 · see citing works

The Chaperone Activity and Substrate Spectrum of Human Small Heat Shock Proteins

Mymrikov, E. V., Daake, M., Richter, B., Haslbeck, M., & Büchner, J. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.760413 · Cited by 152 · see citing works

The chaperone αB-crystallin uses different interfaces to capture an amorphous and an amyloid client

Mainz, A., Peschek, J., Stavropoulou, M., Back, K. C., Bardiaux, B., Asami, S., Prade, E., Peters, C., Weinkauf, S., Büchner, J., et al. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3108 · Cited by 149 · see citing works

Phosphomimics Destabilize Hsp27 Oligomeric Assemblies and Enhance Chaperone Activity

Jovcevski‬, B., Kelly, M. A., Rote, A. P., Berg, T., Gastall, H. Y., Benesch, J. L. P., Aquilina, J. A., & Ecroyd, H. W. (2015) · Chemistry & Biology · doi:10.1016/j.chembiol.2015.01.001 · Cited by 126 · see citing works

Small Heat-shock Proteins Prevent α-Synuclein Aggregation via Transient Interactions and Their Efficacy Is Affected by the Rate of Aggregation

Cox, D., Selig, E. E., Griffin, M. D. W., Carver, J. A., & Ecroyd, H. W. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.739250 · Cited by 116 · see citing works

Role of quality control pathways in human diseases involving protein misfolding

Welch, W. J. (2004) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2003.12.011 · Cited by 109 · see citing works

Mass spectrometry of protein-ligand complexes: Enhanced gas-phase stability of ribonuclease-nucleotide complexes

Yin, S., Xie, Y., & Loo, J. (2008) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2008.05.012 · Cited by 101 · see citing works

Curcumin and kaempferol prevent lysozyme fibril formation by modulating aggregation kinetic parameters

Borana, M. S., Mishra, P., Pissurlenkar, R. R. S., Hosur, R. V., & Ahmad, B. (2014) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2014.01.009 · Cited by 100 · see citing works

Small molecule probes of protein aggregation

Young, L. M., Ashcroft, A. E., & Radford, S. E. (2017) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2017.06.008 · Cited by 93 · see citing works

Modulating Self‐Assembly of Amyloidogenic Proteins as a Therapeutic Approach for Neurodegenerative Diseases: Strategies and Mechanisms

Liu, T., & Bitan, G. (2012) · ChemMedChem · doi:10.1002/cmdc.201100585 · Cited by 75 · see citing works

The effect of small molecules in modulating the chaperone activity of αB‐crystallin against ordered and disordered protein aggregation

Ecroyd, H. W., & Carver, J. A. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06257.x · Cited by 60 · see citing works

Mechanistic Insight into the Relationship between N-Terminal Acetylation of α-Synuclein and Fibril Formation Rates by NMR and Fluorescence

Kang, L., Janowska, M. K., Moriarty, G. M., & Baum, J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0075018 · Cited by 58 · see citing works

The characterization of C-phycocyanin from an extremely halo-tolerant blue–green alga, Coccochloris elabens

Kao, O. H. W., Berns, D. S., & Town, W. R. (1973) · Biochemical Journal · doi:10.1042/bj1310039 · Cited by 54 · see citing works

The small heat-shock protein αB-crystallin uses different mechanisms of chaperone action to prevent the amorphous versus fibrillar aggregation of α-lactalbumin

Kulig, M., & Ecroyd, H. W. (2012) · Biochemical Journal · doi:10.1042/bj20121187 · Cited by 51 · see citing works

Inhibition of islet amyloid polypeptide fibril formation by selenium-containing phycocyanin and prevention of beta cell apoptosis.

Li, X.-L., Ma, L.-J., Zheng, W.-J., & Chen, T. (2014) · Biomaterials · doi:10.1016/j.biomaterials.2014.06.056 · Cited by 49 · see citing works

Interaction of Amyloid Inhibitor Proteins with Amyloid Beta Peptides: Insight from Molecular Dynamics Simulations

Das, P., Kang, S.-G., Temple, S., & Belfort, G. (2014) · PLoS ONE · doi:10.1371/journal.pone.0113041 · Cited by 46 · see citing works

Physical-chemical properties of C-phycocyanin isolated from an acido-thermophilic eukaryote, Cyanidium caldarium

Kao, O. H. W., Edwards, M. R., & Berns, D. S. (1975) · Biochemical Journal · doi:10.1042/bj1470063 · Cited by 45 · see citing works

SerpinB2 (PAI-2) Modulates Proteostasis via Binding Misfolded Proteins and Promotion of Cytoprotective Inclusion Formation

Lee, J., Yerbury, J. J., Farrawell, N. E., Shearer, R. F., Constantinescu, P., Hatters, D. M., Schroder, W. A., Suhrbier, A., Wilson, M. R., Saunders, D. N., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0130136 · Cited by 40 · see citing works

Ion Mobility Mass Spectrometry Studies of the Inhibition of Alpha Synuclein Amyloid Fibril Formation by (–)-Epigallocatechin-3-Gallate

Liu, Y., Ho, L. H., Carver, J. A., & Pukala, T. L. (2011) · Australian Journal of Chemistry · doi:10.1071/ch10334 · Cited by 21 · see citing works

Phycobiliproteins from cyanobacteria: Chemistry and biotechnological applications

Pagels, F., Guedes, A. C., Amaro, H. M., Kijjoa, A., & Vasconcelos, V. (2019) · Biotechnology Advances · doi:10.1016/j.biotechadv.2019.02.010 · Cited by 426 · see citing works

Exploring the Benefits of Phycocyanin: From Spirulina Cultivation to Its Widespread Applications

Fernandes, R., Campos, J., Serra, M., Fidalgo, J., Almeida, H., Casas, A., Toubarro, D., & Barros, A. (2023) · Pharmaceuticals · doi:10.3390/ph16040592 · Cited by 255 · see citing works

Phycobiliproteins: Structural aspects, functional characteristics, and biotechnological perspectives

Dagnino-Leone, J., Figueroa, C. P., Castañeda, M. L., Youlton, A. D., Vallejos-Almirall, A., Agurto-Muñoz, A., Pavón Pérez, J., & Agurto-Muñoz, C. (2022) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2022.02.016 · Cited by 234 · see citing works

Phycocyanin: Anti-inflammatory effect and mechanism

Liu, R., Qin, S., & Li, W. (2022) · Biomedicine &amp; Pharmacotherapy · doi:10.1016/j.biopha.2022.113362 · Cited by 157 · see citing works

Beneficial Effects of Spirulina Consumption on Brain Health

Trotta, T., Porro, C., Cianciulli, A., & Panaro, M. A. (2022) · Nutrients · doi:10.3390/nu14030676 · Cited by 98 · see citing works

Sorption of ionized dyes on high-salinity microalgal residue derived biochar: Electron acceptor-donor and metal-organic bridging mechanisms

Tan, X., Zhu, S., Show, P. L., Qi, H., & Ho, S. (2020) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2020.122435 · Cited by 87 · see citing works

Rationally designed peptide-based inhibitor of Aβ42 fibril formation and toxicity: a potential therapeutic strategy for Alzheimer's disease

Horsley, J. R., Jovcevski‬, B., Wegener, K. L., Yu, J., Pukala, T. L., & Abell, A. D. (2020) · Biochemical Journal · doi:10.1042/bcj20200290 · Cited by 73 · see citing works

C-Phycocyanin-derived Phycocyanobilin as a Potential Nutraceutical Approach for Major Neurodegenerative Disorders and COVID-19-induced Damage to the Nervous System

Pentón-Rol, G., Marín-Prida, J., & McCarty, M. F. (2021) · Current Neuropharmacology · doi:10.2174/1570159x19666210408123807 · Cited by 73 · see citing works

Using mass spectrometry‐based methods to understand amyloid formation and inhibition of alpha‐synuclein and amyloid beta

Wagner, W. J., & Gross, M. L. (2022) · Mass Spectrometry Reviews · doi:10.1002/mas.21814 · Cited by 35 · see citing works

Nutraceutical and therapeutic potential of Phycocyanobilin for treating Alzheimer’s disease

Piniella‐Matamoros, B., Marín‐Prida, J., & Pentón‐Rol, G. (2021) · Journal of Biosciences · doi:10.1007/s12038-021-00161-7 · Cited by 34 · see citing works

Sustainable Microalgae and Cyanobacteria Biotechnology

López-Hernández, J.-F., Kean-Meng, T., Asencio-Alcudia, G.-G., Asyraf-Kassim, M., Alvarez-González, C.-A., & Márquez-Rocha, F.-J. (2022) · Applied Sciences · doi:10.3390/app12146887 · Cited by 30 · see citing works

Phycobiliproteins in Microalgae: Occurrence, Distribution, and Biosynthesis

Kannaujiya, V. K., Singh, P. R., Kumar, D., & Sinha, R. P. (2020) · Pigments from Microalgae Handbook · doi:10.1007/978-3-030-50971-2_3 · Cited by 28 · see citing works

The powerful phycobiliproteins-phycocyanin and phycoerythrin: Pleiotropic applications and biofunctional uses

Ashaolu, T. J. (2024) · Algal Research · doi:10.1016/j.algal.2024.103636 · Cited by 26 · see citing works

Bridging Cyanobacteria to Neurodegenerative Diseases: A New Potential Source of Bioactive Compounds against Alzheimer’s Disease

Castañeda, A., Ferraz, R., Vieira, M., Cardoso, I., Vasconcelos, V. M., & Martins, R. F. (2021) · Marine Drugs · doi:10.3390/md19060343 · Cited by 24 · see citing works

Phycobilins Versatile Pigments with Wide-Ranging Applications: Exploring Their Uses, Biological Activities, Extraction Methods and Future Perspectives

García‐Gómez, C., Aguirre-Cavazos, D. E., Chávez-Montes, A., Ballesteros-Torres, J. M., Orozco-Flores, A. A., Reyna-Martínez, G. R., Torres-Hernández, Á. D., González-Meza, G. M., Castillo, S., Garza, M. A. G., et al. (2025) · Marine Drugs · doi:10.3390/md23050201 · Cited by 24 · see citing works

The molecular chaperone β-casein prevents amorphous and fibrillar aggregation of α-lactalbumin by stabilisation of dynamic disorder

Sanders, H. M., Jovcevski‬, B., Carver, J. A., & Pukala, T. L. (2020) · Biochemical Journal · doi:10.1042/bcj20190638 · Cited by 23 · see citing works

Mass spectrometric insights into protein aggregation

Pukala, T. L. (2023) · Essays in Biochemistry · doi:10.1042/ebc20220103 · Cited by 19 · see citing works

Biosynthesis, acquisition, regulation, and upcycling of heme: recent advances

Yu, F., Wang, Z., Zhang, Z., Zhou, J., Li, J., Chen, J., Du, G., & Zhao, X. (2024) · Critical Reviews in Biotechnology · doi:10.1080/07388551.2023.2291339 · Cited by 19 · see citing works

Polyphenol Honokiol and Flavone 2′,3′,4′-Trihydroxyflavone Differentially Interact with α-Synuclein at Distinct Phases of Aggregation

Jovcevski‬, B., Das, S., Smid, S. D., & Pukala, T. L. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00654 · Cited by 18 · see citing works

Insight to biotechnological utility of phycochemicals from cyanobacterium Anabaena sp.: An overview

Mandhata, C. P., Bishoyi, A. K., Sahoo, C. R., Maharana, S., & Padhy, R. N. (2023) · Fitoterapia · doi:10.1016/j.fitote.2023.105594 · Cited by 13 · see citing works

Designer D-peptides targeting the N-terminal region of α-synuclein to prevent parkinsonian-associated fibrilization and cytotoxicity

Horsley, J. R., Jovcevski‬, B., Pukala, T. L., & Abell, A. D. (2022) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2022.140826 · Cited by 14 · see citing works

Stalling the Course of Neurodegenerative Diseases: Could Cyanobacteria Constitute a New Approach toward Therapy?

Ramos, V., Reis, M. A., Ferreira, L., Silva, A. M., Ferraz, R., Vieira, M., Vasconcelos, V. M., & Martins, R. F. (2023) · Biomolecules · doi:10.3390/biom13101444 · Cited by 12 · see citing works

Extraction, Purification, Bioactivity and Pharmacological Effects of Phycobiliproteins (PBPs): A Review

Madji, S., Antih, J., Tabib, M., Silvestre, C., Ghennai, A., Warnery, A., Vaillant, F. E., Bichon, F., Echalier, A., & Poucheret, P. (2025) · Analytica—A Journal of Analytical Chemistry and Chemical Analysis · doi:10.3390/analytica6040044 · Cited by 12 · see citing works

Molecular Interaction of Protein-Pigment C-Phycocyanin with Bovine Serum Albumin in a Gomphosis Structure Inhibiting Amyloid Formation

Luo, Y.-C., & Jing, P. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218207 · Cited by 9 · see citing works

Phycocyanin: A potential bioresource for functional food product development

Chhirang, P., Gahlawat, V. K., & Singh, B. P. (2024) · South African Journal of Botany · doi:10.1016/j.sajb.2024.08.047 · Cited by 8 · see citing works

Novel Molecular Targets and Mechanisms for Neuroprotective Modulation in Neurodegenerative Disorders

Irannejad, H., Azari, A., Goodarzi, A., Jafarkhani, B., Eghbali, M., Karimi, Z., & Balef, S. S. H. (2022) · Central Nervous System Agents in Medicinal Chemistry · doi:10.2174/1871524922666220616092132 · Cited by 8 · see citing works

Polyphenol characterisation and diverse bioactivities of native Australian lilly pilly ( Syzygium paniculatum ) extract

Pachulicz, R. J., Yu, L., Jovcevski‬, B., Bulone, V., & Pukala, T. L. (2022) · Food & Function · doi:10.1039/d2fo01305c · Cited by 8 · see citing works

Investigation of the Potential of Selected Food-Derived Antioxidants to Bind and Stabilise the Bioactive Blue Protein C-Phycocyanin from Cyanobacteria Spirulina

Gligorijević, N., Jovanović, Z., Cvijetić, I., Šunderić, M., Veličković, L., Katrlı́k, J., Holazová, A., Nikolic, M. R., & Minic, S. L. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms25010229 · Cited by 7 · see citing works

Phycocyanin, The Microalgae Bio-Treasure

Campos, J., Fernandes, R., & Barros, A. (2024) · Food science and nutrition · doi:10.5772/intechopen.115108 · Cited by 6 · see citing works

Rational Design of Key Enzymes to Efficiently Synthesize Phycocyanobilin in Escherichia coli

Wang, Z., Zhou, J., Li, J., Du, G., Chen, J., & Zhao, X. (2024) · Biomolecules · doi:10.3390/biom14030301 · Cited by 6 · see citing works

IM-MS and ECD-MS/MS Provide Insight into Modulation of Amyloid Proteins Self-Assembly by Peptides and Small Molecules

Taha, H. B., Chawla, E., & Bitan, G. (2023) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.3c00065 · Cited by 4 · see citing works

Bioactive Compounds of the Genus Spirulina Can Prevent the Progression of Neurological Diseases

Elkader, H. A. E. A., Essawy, A. E., & Al‐Shami, A. S. (2024) · Neurochemical Journal · doi:10.1134/s1819712424010057 · Cited by 4 · see citing works

Nutraceutical prospects of genetically engineered cyanobacteria- technological updates and significance

Tiwari, D., Kumar, N., Bongirwar, R., & Shukla, P. (2024) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-024-04064-1 · Cited by 3 · see citing works

Phycocyanin from Sp. platensis: taxonomy, structure and properties, medical application (review)

Shabanov, K. A., Panov, A. V., Суслов, В. В., & Кедик, С. А. (2025) · Гербариум. · doi:10.33380/3034-3925-2025-2-1-13 · Cited by 1 · see citing works

Phycobiliproteins-algae-derived pigments: Advances in research on the therapeutic potential

Jaiswal, M., Lal, R., Pandey, S., Amin, N., Pandey, A., & Kannaujiya, V. K. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-24017-1.00008-7

Therapeutic Potential of Macroalgae- and Microalgae-Derived Bioactive Compounds in Parkinson’s Disease

Lee, J. Y., Lim, L. W. C., Wong, C.-Y., Koh, R. Y., Lim, C. L., Kok, Y.-Y., & Chye, S. M. (2026) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/0118715273403412251202093934

AChE inhibitors from marine resources

Kim, C. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-45844-6.00018-4

Amphiphilic modification of human lysozyme enhances its ability to inhibit Aβ42 aggregation

Waku, T., Tokazu, R., Hori, T., Okuda, M., Sugimoto, H., Matsuo, K., & Kobori, A. (2026) · Chemistry Letters · doi:10.1093/chemle/upag146

Cyanobacterial biorefinery: sustainable wastewater management for generation of biofuels and high-value products aligning with a circular economy approach

Kikani, B. A., Andhare, P., Sonavane, B., Dube, S., Desai, C., & Madamwar, D. (2026) · Systems Microbiology and Biomanufacturing · doi:10.1007/s43393-026-00535-8

Molecular Interaction of Protein-Pigment C-Phycocyanin with Bovine Serum Albumin in a Gomphosis Structure Inhibiting Amyloid Formation

Luo, Y.-C., & Jing, P. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218207 · Cited by 9 · see citing works

Toward the Discovery of Effective Polycyclic Inhibitors of α-Synuclein Amyloid Assembly

Lamberto, G. R., Monserrat, V. T., Bertoncini, C. W., Salvatella, X., Zweckstetter, M., Griesinger, C., & Fernández, C. O. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.242958 · Cited by 44 · see citing works

Phthalocyanines as Molecular Scaffolds to Block Disease-Associated Protein Aggregation

Valiente‐Gabioud, A. A., Miotto, M., Chesta, M. E., Lombardo, V. A., Binolfi, A., & Fernández, C. O. (2016) · Accounts of Chemical Research · doi:10.1021/acs.accounts.5b00507 · Cited by 47 · see citing works

Polyphenols-Based Nanosheets of Propolis Modulate Cytotoxic Amyloid Fibril Assembly of α-Synuclein

Rafiei, Y., Salmani, B., Mirzaei-Behbahani, B., Taleb, M., Meratan, A. A., Ramezani, M., Nikfarjam, N., Becker, S., & Rezaei‐Ghaleh, N. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00465 · Cited by 9 · see citing works

Tryptophan‐cardanol fluorescent nanoparticles inhibit α‐synuclein aggregation and disrupt amyloid fibrils

Sunny, L. P., Srikanth, P., Sunitha, A. K., Tembulkar, N., & Abraham, J. N. (2021) · Journal of Peptide Science · doi:10.1002/psc.3374 · Cited by 5 · see citing works