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December 2022
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Cover Image
Cover Image
α-Synuclein (α-Syn) forms different higher order assemblies during the process of aggregation into amyloid fibrils, which has pathological implications in Parkinson's disease. Recently liquid-liquid phase separation (LLPS) of α-Syn has emerged as a prominent early stage event in the aggregation pathway. With time, α-Syn LLPS undergoes liquid-to-solid transition and subsequently forms amyloid fibrils. The phase-separated droplets eventually fuse/grow into a larger manifestation of a hydrogel containing amyloid fibrils. In this illustration, the hourglass represents time dependent LLPS and subsequent liquid-to-solid transition followed by amyloid fibril formation. For further information see the review in this issue by Poudyal and colleagues (pages 987-1000). Image credit Pradeep Kadu and Dr. Soumik Ray.
ISSN 0071-1365
EISSN 1744-1358
In this Issue
Shapeshifting Proteins
Editorial
Shapeshifting proteins: the role of structural disorder and conformational plasticity in physiology and disease
Essays Biochem (2022) 66 (7): 817–819.
Review Articles
Biological soft matter: intrinsically disordered proteins in liquid–liquid phase separation and biomolecular condensates
Alexander V. Fonin; Iuliia A. Antifeeva; Irina M. Kuznetsova; Konstantin K. Turoverov; Boris Y. Zaslavsky; Prakash Kulkarni; Vladimir N. Uversky
Essays Biochem (2022) 66 (7): 831–847.
NMR insights into dynamic, multivalent interactions of intrinsically disordered regions: from discrete complexes to condensates
Essays Biochem (2022) 66 (7): 863–873.
The biophysics of disordered proteins from the point of view of single-molecule fluorescence spectroscopy
Essays Biochem (2022) 66 (7): 875–890.
Unravelling the microscopic characteristics of intrinsically disordered proteins upon liquid–liquid phase separation
Essays Biochem (2022) 66 (7): 891–900.
How phosphorylation impacts intrinsically disordered proteins and their function
Essays Biochem (2022) 66 (7): 901–913.
Functional benefit of structural disorder for the replication of measles, Nipah and Hendra viruses
Frank Gondelaud; Giulia Pesce; Juliet F. Nilsson; Christophe Bignon; Denis Ptchelkine; Denis Gerlier; Cyrille Mathieu; Sonia Longhi
Essays Biochem (2022) 66 (7): 915–934.
How viral proteins bind short linear motifs and intrinsically disordered domains
Essays Biochem (2022) 66 (7): 935–944.
Evolution of SLiM-mediated hijack functions in intrinsically disordered viral proteins
Essays Biochem (2022) 66 (7): 945–958.
Controlling amyloid formation of intrinsically disordered proteins and peptides: slowing down or speeding up?
Essays Biochem (2022) 66 (7): 959–975.
Phase separation and other forms of α-Synuclein self-assemblies
Essays Biochem (2022) 66 (7): 987–1000.
Shapeshifting tau: from intrinsically disordered to paired-helical filaments
Kurtis Mengham; Youssra Al-Hilaly; Sebastian Oakley; Kamillia Kasbi; Mahmoud B. Maina; Louise C. Serpell
Essays Biochem (2022) 66 (7): 1001–1011.
The chameleonic behavior of p53 in health and disease: the transition from a client to an aberrant condensate scaffold in cancer
Essays Biochem (2022) 66 (7): 1023–1033.