X-ray structures of ferritins and related proteins

Crichton, Robert R.; Declercq, Jean‐Paul

doi:10.1016/j.bbagen.2010.03.019

Cited by 157 publications

(158 citation statements)

References 56 publications

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“…Transferrin [38] and ferritin [39] are crucial iron-transporting proteins and crucial elements of iron metabolism [40]. Increased levels of transferrin and ferritin in dystrophic muscle agree with recent findings from the proteomic analysis of the aged mdx diaphragm [26] and the aged mdx heart [41].…”

Section: Discussionsupporting

confidence: 77%

Comparative proteomic analysis of the contractile-protein-depleted fraction from normal versus dystrophic skeletal muscle

Carberry

Zweyer

Swandulla

et al. 2014

Analytical Biochemistry

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a b s t r a c tIn basic and applied myology, gel-based proteomics is routinely used for studying global changes in the protein constellation of contractile fibers during myogenesis, physiological adaptations, neuromuscular degeneration, and the natural aging process. Since the main proteins of the actomyosin apparatus and its auxiliary sarcomeric components often negate weak signals from minor muscle proteins during proteomic investigations, we have here evaluated whether a simple prefractionation step can be employed to eliminate certain aspects of this analytical obstacle. To remove a large portion of highly abundant contractile proteins from skeletal muscle homogenates without the usage of major manipulative steps, differential centrifugation was used to decisively reduce the sample complexity of crude muscle tissue extracts. The resulting protein fraction was separated by two-dimensional gel electrophoresis, and 2D-landmark proteins were identified by mass spectrometry. To evaluate the suitability of the contractileprotein-depleted fraction for comparative proteomics, normal versus dystrophic muscle preparations were examined. The mass spectrometric analysis of differentially expressed proteins, as determined by fluorescence difference in-gel electrophoresis, identified 10 protein species in dystrophic mdx hindlimb muscles. Interesting new biomarker candidates included Hsp70, transferrin, and ferritin, whereby their altered concentration levels in dystrophin-deficient muscle were confirmed by immunoblotting.Ó 2013 Elsevier Inc. All rights reserved.In high-throughput biochemistry, mass spectrometry is the method of choice for the fast and reliable identification of proteins in large-scale surveys of physiological or pathological processes [1][2][3]. This makes protein mass spectrometry an integral part of biological network analysis [4] and the discovery of novel disease biomarker signatures [5]. Disorder-specific protein markers play a central diagnostic, prognostic, and therapeutic role in skeletal muscle pathology and the systematic application of proteomics has greatly expanded the range of biomarkers for neuromuscular disorders [6]. Proteome-wide studies combine protein separation methods, such as high-resolution two-dimensional gel electrophoresis [7-9] and liquid chromatography [10], with sophisticated mass spectrometric techniques to determine potential changes in protein concentration, isoform expression patterns, protein-protein interactions and posttranslational modifications [11][12][13].However, proteomic findings from comparative studies focusing on total protein extracts from highly complex and dynamic types of tissues, such as skeletal muscle fibers, are often limited to mostly soluble and relatively abundant proteins [14][15][16], missing especially the classes of very low abundance proteins and hydrophobic proteins. Thus, to cover all of the assessable constituents in a heterogeneous assembly of proteins with a greatly differing abundance and physicochemical properties, as are found in contr...

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Section: Discussionsupporting

confidence: 77%

Comparative proteomic analysis of the contractile-protein-depleted fraction from normal versus dystrophic skeletal muscle

Carberry

Zweyer

Swandulla

et al. 2014

Analytical Biochemistry

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“…The protein shell is in the shape of a hollow rhombic dodecahedron with 4-3-2 symmetry that forms intersubunit channels along the three-and four-fold axes to accommodate iron [21]. The faces of the dodecahedron are formed by two subunits related by a two-fold symmetry axis at the centre [18]. Each axis is connected to subunits by electrostatic interactions and hydrogen bonding.…”

Section: Apoferritin Structurementioning

confidence: 99%

“…The ferritin shell is able to store 4500 iron atoms in its structure in the form of ferric oxide phosphate, which is structurally similar to ferrihydrite [21], although it generally contains less than 2000 iron atoms in the inner core [35]. The iron stored in the ferritin cavity is usually in the form of ferric hydroxyphosphate micelles [18] and it is readily available to cellular demand [36]. The major pathway of iron release in cells is via the degradation of the ferritin cage [37].…”

Section: Functions Of Ferritin In Organismsmentioning

confidence: 99%

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Apoferritin: protein nanocarrier for targeted delivery

Dostálová¹,

Heger²,

Kudr³

et al. 2015

Nano Based Drug Delivery

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“…3b). [85][86][87] Each of the four-helix-bundle subunits of BFR contains a dinuclear metal binding site. The site binds two Fe II atoms with histidine (H54 and H130) and glutamate (E51, E18, E127 and E94) residues as capping ligands.…”

Section: Modified Bacterioferritin As a Photoactive Reaction Centrementioning

confidence: 99%

Perspectives for Photobiology in Molecular Solar Fuels

Hingorani

Hillier

2012

Aust. J. Chem.

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This paper presents an overview of the prospects for bio-solar energy conversion. The Global Artificial Photosynthesis meeting at Lord Howe Island (14–18 August 2011) underscored the dependence that the world has placed on non-renewable energy supplies, particularly for transport fuels, and highlighted the potential of solar energy. Biology has used solar energy for free energy gain to drive chemical reactions for billions of years. The principal conduits for energy conversion on earth are photosynthetic reaction centres – but can they be harnessed, copied and emulated? In this communication, we initially discuss algal-based biofuels before investigating bio-inspired solar energy conversion in artificial and engineered systems. We show that the basic design and engineering principles for assembling photocatalytic proteins can be used to assemble nanocatalysts for solar fuel production.

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X-ray structures of ferritins and related proteins

Cited by 157 publications

References 56 publications

Comparative proteomic analysis of the contractile-protein-depleted fraction from normal versus dystrophic skeletal muscle

Comparative proteomic analysis of the contractile-protein-depleted fraction from normal versus dystrophic skeletal muscle

Apoferritin: protein nanocarrier for targeted delivery

Perspectives for Photobiology in Molecular Solar Fuels

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