Results 11 to 20 of about 9,982 (140)

A Globin in the Nucleus! [PDF]

open access: yesJournal of Biological Chemistry, 2003
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
openaire   +4 more sources

A phylogenomic profile of globins [PDF]

open access: yesBMC Evolutionary Biology, 2006
AbstractBackgroundGlobins 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, with variable C-terminal domains.
Vinogradov, S. N.   +7 more
openaire   +8 more sources

Regulation of the Globin Genes [PDF]

open access: yesPediatric Research, 2002
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
openaire   +3 more sources

TMEM8 – a non-globin gene entrapped in the globin web [PDF]

open access: yesNucleic Acids Research, 2009
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]

open access: yesFEBS Letters, 1977
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
openaire   +3 more sources

Nerve Globins in Invertebrates

open access: yesIUBMB Life, 2004
AbstractThe expression of nerve hemoglobins in invertebrates is a well‐established fact, but this occurrence is uncommon. In the species where nerve globins occur, they probably function as an oxygen store for sustaining activity of the nerves during anoxic conditions.
GEUENS E.   +9 more
openaire   +6 more sources

Cotranslational Folding of Globin [PDF]

open access: yesJournal of Biological Chemistry, 1997
Globin synthesis in a wheat germ cell-free translation system was performed in the presence of [3H]hemin and [35S]methionine to determine the minimal length of the nascent ribosome-bound globin chain capable of heme binding. Nascent polypeptides of predetermined size were synthesized on ribosomes by translation of truncated mRNA molecules.
Anton A. Komar   +3 more
openaire   +3 more sources

Red blood cell endothelial nitric oxide synthase: A major player in regulating cardiovascular health

open access: yesBritish Journal of Pharmacology, EarlyView., 2023
Abstract Red blood cells (RBCs) have traditionally been seen as simple carriers of gases and nutrients in the body. One important non‐canonical function of RBCs in the cardiovascular system is the regulation of nitric oxide (NO) metabolism. It has been shown that RBCs can scavenge NO, transport NO metabolites and produce NO in hypoxic conditions ...
Anthea LoBue   +7 more
wiley   +1 more source

Globins in Caenorhabditis elegans

open access: yesIUBMB Life, 2011
AbstractExtensive in silico search of the genome of Caenorhabditis elegans revealed the presence of 33 genes coding for globins that are all transcribed. These globins are very diverse in gene and protein structure and are localized in a variety of cells, mostly neurons. The large number of C.
Tilleman, L   +8 more
openaire   +6 more sources

Differences in cattle globins [PDF]

open access: yesBiochemical Journal, 1965
1. Comparisons have been made between electrophoretic mobilities of the cattle haemoglobins, HbA, HbB, HbC, HbD and HbF, at pH8.9. The fastest was HbB, then came in decreasing order HbF, HbC, HbA and HbD. 2. Globins were prepared from the main fractions of the five haemoglobins by CM-cellulose chromatography and investigated by starch-gel ...
M Braend, G Efremov
openaire   +3 more sources

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