Results 1 to 10 of about 11,873 (185)
A phylogenomic profile of globins [PDF]
BACKGROUND: Globins occur in all three kingdoms of life: they can be classified into single-domain globins and chimeric globins. The latter comprise the flavohemoglobins with a C-terminal FAD-binding domain and the gene-regulating globin coupled sensors,
Arredondo-Peter, Raúl+7 more
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Globin-based redox signaling [PDF]
In recent years, moderate levels of reactive oxygen species (ROS) have become recognized as signaling cues that participate at all levels of cellular organization. Globins, with their redox-active heme iron and ubiquitous presence, seem ideally suited to
Braeckman, Bart, De Henau, Sasha
core +7 more sources
A Globin in the Nucleus! [PDF]
Cytoglobin and neuroglobin are recently discovered members of the globin family. In situ hybridization localized neuroglobin mainly in brain and retina, while cytoglobin was expressed ubiquitously in all analyzed tissues. In the present study, polyclonal antibodies were raised against both proteins and the distribution of them was studied by ...
Geuens, Eva+5 more
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Regulation of the Globin Genes [PDF]
The a- and b-globin gene clusters are subject to several levels of regulation. They are expressed exclusively in the erythroid cells, only during defined periods of development and in a perfectly tuned way, assuring, at any stage of ontogeny, a correct balance in the availability of a- and b-globin chains for hemoglobin assembling. Such a tight control
Cao A, MOI, PAOLO
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TMEM8 – a non-globin gene entrapped in the globin web [PDF]
For more than 30 years it was believed that globin gene domains included only genes encoding globin chains. Here we show that in chickens, the domain of alpha-globin genes also harbor the non-globin gene TMEM8. It was relocated to the vicinity of the alpha-globin cluster due to inversion of an approximately 170-kb genomic fragment.
Elena S. Philonenko+5 more
openaire +3 more sources
The folding pathway for globins [PDF]
Previous investigations have successfully predicted the three-dimensional structures of trypsin inhibitor [ 1,2] , myoglobin [3,4] , TMV protein [ 51 and rubredoxin [2]. Using mechanisms of protein chain folding which one of us [5 $1 suggested,.we can find a common folding pathway for the globins which are included in the ‘Atlas of Protein Sequence and
V.I. Lim, Alexander V. Efimov
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Visible Volume: a Robust Measure for Protein Structure Characterization [PDF]
We propose a new characterization of protein structure based on the natural tetrahedral geometry of the β carbon and a new geometric measure of structural similarity, called visible volume.
Bashford+31 more
core +2 more sources
Proximal and distal control for ligand binding in neuroglobin: role of the CD loop and evidence for His64 gating [PDF]
Neuroglobin (Ngb) is predominantly expressed in neurons of the central and peripheral nervous systems and it clearly seems to be involved in neuroprotection.
Anselmi, Massimiliano+10 more
core +4 more sources
Nitrosative stress defences of the enterohepatic pathogenic bacterium Helicobacter pullorum [PDF]
Helicobacter pullorum is an avian bacterium that causes gastroenteritis, intestinal bowel and hepatobiliary diseases in humans. Although H. pullorum has been shown to activate the mammalian innate immunity with release of nitric oxide (NO), the proteins ...
Boneca, Ivo G.+6 more
core +3 more sources
An automatic method for assessing structural importance of amino acid positions [PDF]
Background: A great deal is known about the qualitative aspects of the sequence-structure relationship, for example that buried residues are usually more conserved between structurally similar homologues, but no attempts have been made to quantitate the ...
Jones, D.T., Sadowski, M.I.
core +3 more sources