scholarly journals Signalling: the remarkable dynasties

2006 ◽  
Vol 28 (1) ◽  
pp. 33-36
Author(s):  
Robin Irvine
Keyword(s):  
Biochemical Journal ◽  
Metabolism Enzymes ◽  
Journal Papers

The list of Biochemical Journal papers selected by the Editorial Board1–12 for the ‘classic’ status in signalling (plus a couple of directly relevant classics from the metabolism/enzymes section that I have included) consists almost entirely of papers with inositol or inositide in the title. This reflects a truly remarkable relationship between inositides, UK scientists and the Biochemical Journal.

scholarly journals Classic papers on the quantification of respiratory proton ejection

2015 ◽  
Vol 37 (5) ◽  
pp. 47-50
Author(s):  
Ian C. West
Keyword(s):  
Mitochondrial Respiration ◽  
Chemiosmotic Theory ◽  
Chemiosmotic Hypothesis ◽  
Biochemical Journal ◽  
Definitive Statement ◽  
Classic Papers ◽  
Journal Papers

This article looks at two Biochemical Journal papers that are frequently cited as the definitive statement of the quantitative support for Mitchell's chemiosmotic hypothesis in relation to mitochondrial respiration. Both are rich in methodological detail; both contain elaborations of chemiosmotic and biophysical theory. With these two papers, chemiosmotic theory entered the mainstream of bioenergetic thought.

Reading the phosphorylation code: binding of the 14-3-3 protein to multivalent client phosphoproteins

2020 ◽  
Vol 477 (7) ◽  
pp. 1219-1225 ◽  
Author(s):  
Nikolai N. Sluchanko
Keyword(s):  
Protein Function ◽  
Intrinsically Disordered Protein ◽  
Structural Basis ◽  
Major Protein ◽  
Post Translational Modifications ◽  
Protein Protein Interaction ◽  
Intrinsically Disordered ◽  
Biochemical Journal ◽  
Multiple Binding ◽  
And Control

Many major protein–protein interaction networks are maintained by ‘hub’ proteins with multiple binding partners, where interactions are often facilitated by intrinsically disordered protein regions that undergo post-translational modifications, such as phosphorylation. Phosphorylation can directly affect protein function and control recognition by proteins that ‘read’ the phosphorylation code, re-wiring the interactome. The eukaryotic 14-3-3 proteins recognizing multiple phosphoproteins nicely exemplify these concepts. Although recent studies established the biochemical and structural basis for the interaction of the 14-3-3 dimers with several phosphorylated clients, understanding their assembly with partners phosphorylated at multiple sites represents a challenge. Suboptimal sequence context around the phosphorylated residue may reduce binding affinity, resulting in quantitative differences for distinct phosphorylation sites, making hierarchy and priority in their binding rather uncertain. Recently, Stevers et al. [Biochemical Journal (2017) 474: 1273–1287] undertook a remarkable attempt to untangle the mechanism of 14-3-3 dimer binding to leucine-rich repeat kinase 2 (LRRK2) that contains multiple candidate 14-3-3-binding sites and is mutated in Parkinson's disease. By using the protein-peptide binding approach, the authors systematically analyzed affinities for a set of LRRK2 phosphopeptides, alone or in combination, to a 14-3-3 protein and determined crystal structures for 14-3-3 complexes with selected phosphopeptides. This study addresses a long-standing question in the 14-3-3 biology, unearthing a range of important details that are relevant for understanding binding mechanisms of other polyvalent proteins.

Expression of Arachidonate Metabolism Enzymes and Receptors in Nasal Polyps of Aspirin-Hypersensitive Asthmatics

2011 ◽  
Vol 157 (4) ◽  
pp. 354-362 ◽  
Author(s):  
Anna M. Adamusiak ◽  
Olga Stasikowska-Kanicka ◽  
Anna Lewandowska-Polak ◽  
Marian Danilewicz ◽  
Malgorzata Wagrowska-Danilewicz ◽  
...  
Keyword(s):  
Nasal Polyps ◽  
Arachidonate Metabolism ◽  
Metabolism Enzymes

scholarly journals Metabolic and histochemical characteristics of fat and muscle tissues in homozygous or heterozygous pigs for the body composition QTL located on chromosome 7

2007 ◽  
Vol 30 (3) ◽  
pp. 232-241 ◽  
Author(s):  
Julie Demars ◽  
Juliette Riquet ◽  
Marie-Pierre Sanchez ◽  
Yvon Billon ◽  
Jean-François Hocquette ◽  
...  
Keyword(s):  
Body Composition ◽  
Carcass Composition ◽  
The Body ◽  
Chromosome 7 ◽  
Isolated Cells ◽  
Large White ◽  
Muscle Tissues ◽  
Metabolism Enzymes ◽  
Tissue Characteristics ◽  
Qtl Effects

Quantitative trait loci (QTL) influencing many traits including backfat thickness and carcass composition have been detected on porcine chromosome 7 (SSC7) in an F2 cross between Large White (LW) and Meishan (MS) pigs. However, the genes and controlled pathways underlying the QTL effects on body phenotype remain unknown. This study aimed at investigating the tissue characteristics at metabolic and cellular levels in pigs that were either homozygous or heterozygous for a body composition SSC7 QTL. A backcross pig (BC3) was first progeny tested to confirm its heterozygoty for the SSC7 QTL; results on all offspring ( n = 80) confirmed the QTL effects on body fatness. This boar was then mated with three sows known to be heterozygous for this QTL. In the subset of pigs per genotype, we found that heterozygous LWQTL7/MSQTL7 pigs had smaller adipocytes in backfat, together with a lower basal rate of glucose incorporation into lipids and lower activities of selected lipogenic enzymes in backfat isolated cells, compared with homozygous LWQTL7/LWQTL7 pigs. A higher number of adipocytes was also estimated in backfat of LWQTL7/MSQTL7 animals compared with LWQTL7/LWQTL7 pigs. The SSC7 QTL did not influence oxidative and glycolytic metabolisms of longissimus and trapezius muscles, as estimated by the activities of specific energy metabolism enzymes, or the myofiber type properties. Altogether, this study provides new evidence for an altered adipocyte cellularity in backfat of pigs carrying at least one MS allele for the SSC7 QTL. Some candidate genes known for their functions on adipocyte growth and differentiation are suggested.

Evidence for novel aspects of Nox4 oxidase regulation of mitochondrial function and peroxide generation in an endothelial cell model of senescence

2013 ◽  
Vol 452 (2) ◽  
pp. e1-e2 ◽  
Author(s):  
Michael S. Wolin
Keyword(s):  
Endothelial Cell ◽  
Mitochondrial Function ◽  
Cell Model ◽  
Mitochondrial Fission ◽  
Cellular Aging ◽  
Cell Aging ◽  
Regulatory Processes ◽  
Napdh Oxidase ◽  
Transport Chain ◽  
Biochemical Journal

Observations by Kozieł et al. reported in this issue of the Biochemical Journal suggest the existence of novel regulatory processes associated with new evidence for increased Nox4 (NAPDH oxidase 4) regulation of mitochondrial function in a cultured endothelial cell aging-induced senescence model. Cellular aging appears to promote a Nox4 interaction with mitochondria that disrupts complex I in the electron transport chain and increases the detection of mitochondrial H2O2. Nox4 appears to maintain a highly interconnected mitochondrial network, which may influence mitochondrial fission and/or fusion mechanisms in a manner that could be a contributing factor in the loss of replicative lifespan seen in senescence.

Sign in / Sign up

Export Citation Format

Share Document