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Biochem Soc Trans (2021) 49 (2): 977–985.
Published: 30 April 2021
... amyloid fibrils that are β-sheet rich, while the native state of SAA shows an all-alpha fold ( Figure 1 ). The ramification of this finding is that a more or less full unfolding event is required to convert the native precursor into the pathogenic aggregate. The fibril morphologies, which can be...
Biochem Soc Trans (2014) 42 (4): 1246–1250.
Published: 11 August 2014
.... The aggregation-prone LSCRs (low-sequence-complexity regions), and in particular, the polyQ/N-rich regions, have been extensively studied under pathological conditions due to their role in neurodegenerative diseases. In the present review, we discuss recent in vitro , in vivo and computational data...
Biochem Soc Trans (2013) 41 (6): 1536–1540.
Published: 20 November 2013
... brain inclusions in ALS (amyotrophic lateral sclerosis) and FTLD (frontotemporal lobar degeneration) patients. Functionally, this aberrant aggregation and mislocalization implies that, in the affected neurons, transcripts regulated by TDP-43 may be altered. Since then, a considerable amount of data has...
Biochem Soc Trans (2012) 40 (4): 644–652.
Published: 20 July 2012
...Yipeng Wang; Eckhard Mandelkow Tau aggregates are present in several neurodegenerative diseases and correlate with the severity of memory deficit in AD (Alzheimer's disease). However, the triggers of tau aggregation and tau-induced neurodegeneration are still elusive. The impairment of protein...
Luc Buée, Laëtitia Troquier, Sylvie Burnouf, Karim Belarbi, Anneke Van der Jeugd, Tariq Ahmed, Francisco Fernandez-Gomez, Raphaelle Caillierez, Marie-Eve Grosjean, Séverine Begard, Bérangère Barbot, Dominique Demeyer, Hélène Obriot, Ingrid Brion, Valérie Buée-Scherrer, Claude-Alain Maurage, Detlef Balschun, Rudi D'Hooge, Malika Hamdane, David Blum, Nicolas Sergeant
Biochem Soc Trans (2010) 38 (4): 967–972.
Published: 26 July 2010
... Balschun; Rudi D'Hooge; Malika Hamdane; David Blum; Nicolas Sergeant Tau pathology is characterized by intracellular aggregates of abnormally and hyperphosphorylated tau proteins. It is encountered in many neurodegenerative disorders, but also in aging. These neurodegenerative disorders are referred to as...
Biochem Soc Trans (2010) 38 (4): 955–961.
Published: 26 July 2010
...Yipeng Wang; Sarika Garg; Eva-Maria Mandelkow; Eckhard Mandelkow Tau aggregation is a hallmark of several neurodegenerative diseases, including AD (Alzheimer's disease), although the mechanism underlying tau aggregation remains unclear. Recent studies show that the proteolysis of tau plays an...
Biochem Soc Trans (2009) 37 (4): 682–686.
Published: 22 July 2009
...Mark R.H. Krebs; Kristin R. Domike; Athene M. Donald The aggregation of misfolded proteins into amyloid fibrils, and the importance of this step for various diseases, is well known. However, it is becoming apparent that the fibril is not the only structure that aggregating proteins of widely...
Biochem Soc Trans (2009) 37 (1): 36–41.
Published: 20 January 2009
... To whom correspondence should be addressed (email firstname.lastname@example.org ). 28 10 2008 © The Authors Journal compilation © 2009 Biochemical Society 2009 aggregation archaeon DNA repair hyperthermophile Sulfolobus UV damage All living organisms, from bacteria...
Biochem Soc Trans (2005) 33 (5): 1113–1115.
Published: 26 October 2005
... conditions in order to obtain reliable conditions for producing fibrils for further structural investigations. The results indicate that the rate of aggregation and the morphology of the fibrils formed are sensitive to pH and temperature. 1 To whom correspondence should be addressed (email...
Biochem Soc Trans (2005) 33 (4): 543–547.
Published: 01 August 2005
... or delayed clearance of protein aggregates. Hence, inhibition of pathologic protein–protein interactions is a very attractive mechanism for drug development. This review focuses on a novel therapeutic strategy to inhibit the de novo formation of protein aggregates. Inspired by strategies used in...
Biochem Soc Trans (2004) 32 (6): 1127–1129.
Published: 26 October 2004
...J. Madine; A.J. Doig; D.A. Middleton α-Synuclein is a 140 amino acid protein, which is associated with presynaptic membranes in the brain, and is the major component of protein aggregates produced during the progression of many neurodegenerative diseases. It has been shown that a central...
Biochem Soc Trans (2002) 30 (4): 548–551.
Published: 01 August 2002
... aggregation. Detailed understanding of these phenomena is therefore crucial in order to rationalize different phases of the diseases. In the past decade, a few studies have focused on the structural properties of polyglutamine and on the molecular bases of the aggregation process. Most of these studies have...
Biochem Soc Trans (2001) 29 (2): 222–227.
Published: 01 May 2001
..., which has a well-recognized function in gene regulation, provides a unique opportunity to investigate the functional significance of poly(amino acid) repeats in normal and disease states. 1 e-mail: email@example.com 21 12 2000 © 2001 Biochemical Society 2001 aggregation...