Small heat-shock proteins: important players in regulating cellular proteostasis von Treweek, Teresa M, Meehan, Sarah, Ecroyd, Heath, Carver, John A

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The multifaceted nature of αB-crystallin von Hayashi, Junna, Carver, John A.

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Quantitative multivalent binding model of the structure, size distribution and composition of the casein micelles of cow milk von Holt, Carl, Carver, John. A.

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Preventing α-synuclein aggregation: The role of the small heat-shock molecular chaperone proteins von Cox, Dezerae, Carver, John A., Ecroyd, Heath

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thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compounds von Hudson, Sean A, Ecroyd, Heath, Kee, Tak W, Carver, John A

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β-Synuclein: An Enigmatic Protein with Diverse Functionality von Hayashi, Junna, Carver, John A

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Monitoring Early-Stage Protein Aggregation by an Aggregation-Induced Emission Fluorogen von Kumar, Manjeet, Hong, Yuning, Thorn, David C, Ecroyd, Heath, Carver, John A

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A Spectroscopic Marker for Structural Transitions Associated with Amyloid‑β Aggregation von Das, Anirban, Gupta, Ankur, Hong, Yuning, Carver, John A, Maiti, Sudipta

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Are casein micelles extracellular condensates formed by liquid‐liquid phase separation? von Horvath, Attila, Fuxreiter, Monika, Vendruscolo, Michele, Holt, Carl, Carver, John A.

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Crystallin proteins and amyloid fibrils von Ecroyd, H, Carver, John A

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Small Heat-shock Proteins Prevent α-Synuclein Aggregation via Transient Interactions and Their Efficacy Is Affected by the Rate of Aggregation von Cox, Dezerae, Selig, Emily, Griffin, Michael D.W., Carver, John A., Ecroyd, Heath

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Binding of the Molecular Chaperone αB-Crystallin to Aβ Amyloid Fibrils Inhibits Fibril Elongation von Shammas, Sarah L., Waudby, Christopher A., Wang, Shuyu, Buell, Alexander K., Knowles, Tuomas P.J., Ecroyd, Heath, Welland, Mark E., Carver, John A., Dobson, Christopher M., Meehan, Sarah

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Application of the Double-Mutant Cycle Strategy to Protein Aggregation Reveals Transient Interactions in Amyloid‑β Oligomers von Das, Anirban, Korn, Alexander, Carroll, Adam, Carver, John A, Maiti, Sudipta

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The structured core domain of αB-crystallin can prevent amyloid fibrillation and associated toxicity von Hochberg, Georg K. A., Ecroyd, Heath, Liu, Cong, Cox, Dezerae, Cascio, Duilio, Sawaya, Michael R., Collier, Miranda P., Stroud, James, Carver, John A., Baldwin, Andrew J., Robinson, Carol V., Eisenberg, David S., Benesch, Justin L. P., Laganowsky, Arthur

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Gallic acid interacts with α-synuclein to prevent the structural collapse necessary for its aggregation von Liu, Yanqin, Carver, John A., Calabrese, Antonio N., Pukala, Tara L.

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Sequence characteristics responsible for protein‐protein interactions in the intrinsically disordered regions of caseins, amelogenins, and small heat‐shock proteins von Holt, Carl, Raynes, Jared K., Carver, John A.

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The molecular chaperone β-casein prevents amorphous and fibrillar aggregation of α-lactalbumin by stabilisation of dynamic disorder von Sanders, Henry M, Jovcevski, Blagojce, Carver, John A, Pukala, Tara L

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Amyloid fibril formation by αS1- and β-casein implies that fibril formation is a general property of casein proteins von Bahraminejad, Elmira, Paliwal, Devashi, Sunde, Margaret, Holt, Carl, Carver, John A., Thorn, David C.

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The functional roles of the unstructured N- and C-terminal regions in αB-crystallin and other mammalian small heat-shock proteins von Carver, John A., Grosas, Aidan B., Ecroyd, Heath, Quinlan, Roy A.

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A multi-pathway perspective on protein aggregation: Implications for control of the rate and extent of amyloid formation von Hall, Damien, Kardos, József, Edskes, Herman, Carver, John A., Goto, Yuji

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