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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Heme binding protein 2

SOUL, pp23, heme-binding protein 2, C6ORF34
Top mentioned proteins: bcl-2, STAM2, CAN, ACID, OUT
Papers on SOUL
Proteomic analysis of human bladder epithelial cells by 2D blue native SDS-PAGE reveals TCDD-induced alterations of calcium and iron homeostasis possibly mediated by nitric oxide.
Schmitz-Spanke et al., München, Germany. In J Proteome Res, Feb 2015
Major differences between the proteome of control and exposed cells involved the alteration of many calcium-regulated proteins (calmodulin, protein S100-A2, annexin A5, annexin A10, gelsolin isoform b) and iron-regulated proteins (ferritin, heme-binding protein 2, transferrin).
Proteome analysis of cytoplasmatic and plastidic β-carotene lipid droplets in Dunaliella bardawil.
Pick et al., Israel. In Plant Physiol, 2015
The βC-plastoglobuli proteome resembles the C. reinhardtii eyespot and Arabidopsis (Arabidopsis thaliana) plastoglobule proteomes and contains carotene-globule-associated protein, plastid-lipid-associated protein-fibrillins, SOUL heme-binding proteins, phytyl ester synthases, β-carotene biosynthesis enzymes, and proteins involved in membrane remodeling/lipid droplet biogenesis: VESICLE-INDUCING PLASTID PROTEIN1, synaptotagmin, and the eyespot assembly proteins EYE3 and SOUL3.
Identification of key genes in the response to Salmonella enterica Enteritidis, Salmonella enterica Pullorum, and poly(I:C) in chicken spleen and caecum.
Chen et al., Yangzhou, China. In Biomed Res Int, 2013
Four DEGs were identified in spleen of all three challenge groups (RBM16, FAH, SOX5, and RBM9) and different four genes in caecum (SOUL, FCN2, ANLN, and ACSL1).
Disrupting the bimolecular binding of the haem-binding protein 5 (AtHBP5) to haem oxygenase 1 (HY1) leads to oxidative stress in Arabidopsis.
Buckhout et al., Berlin, Germany. In J Exp Bot, 2012
The Arabidopsis thaliana L. SOUL/haem-binding proteins, AtHBPs belong to a family of five members.
Possible predictors of histopathological response to neoadjuvant chemoradiotherapy for rectal cancer.
Bellyei et al., Pécs, Hungary. In J Cancer Res Clin Oncol, 2012
Our aim was to correlate the response to CRT with the pre-treatment expression of heat shock protein 90 (Hsp90), small heat shock protein 16.2 (sHsp 16.2), phospho-Akt (p-Akt), growth hormone-releasing hormone receptor (GHRH-R) and heme-binding protein 2 (SOUL) in order to try to identify one or more as a predictive marker.
Structural changes in the BH3 domain of SOUL protein upon interaction with the anti-apoptotic protein Bcl-xL.
Monaco et al., Verona, Italy. In Biochem J, 2011
There are important structural differences in the BH3 domain in the intact SOUL molecule and the same sequence bound to Bcl-xL.
Identification and expression of soul/p22HBP genes in zebrafish.
Sordino et al., Napoli, Italy. In Gene Expr Patterns, 2011
The SOUL/p22HBP family is an evolutionarily ancient group of heme binding proteins with a main function as cytosolic buffer against tetrapyrrole accumulation.
Correlation between tumor-associated proteins and response to neoadjuvant treatment in patients with advanced squamous-cell esophageal cancer.
Papp et al., Pécs, Hungary. In Anticancer Res, 2011
heme-binding protein 2 (SOUL), BCL2-associated X protein (Bax), B-cell-associated leukemia protein 2 (Bcl-2) and heat shock protein 90 (Hsp90) antibodies.
Facilitation of mitochondrial outer and inner membrane permeabilization and cell death in oxidative stress by a novel Bcl-2 homology 3 domain protein.
Gallyas et al., Pécs, Hungary. In J Biol Chem, 2010
SOUL can be a novel member of the BH3 domain-only proteins that cannot induce cell death alone but can facilitate both outer and inner mitochondrial membrane permeabilization and predominantly necrotic cell death in oxidative stress.
Preliminary structural characterization of human SOUL, a haem-binding protein.
Carvalho et al., Caparica, Portugal. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2009
preliminary X ray structure
Characterization of cytosolic tetrapyrrole-binding proteins in Arabidopsis thaliana.
Masuda et al., Tokyo, Japan. In Photochem Photobiol Sci, 2008
In animal cells, experimental evidence suggests that the p22HBP/SOUL family are cytosolic heme carrier proteins functioning in heme trafficking.
The phosphoproteome of a Chlamydomonas reinhardtii eyespot fraction includes key proteins of the light signaling pathway.
Kreimer et al., Jena, Germany. In Plant Physiol, 2008
Among the identified phosphoproteins are enzymes of carotenoid and fatty acid metabolism, putative signaling components, such as a SOUL heme-binding protein, a Ca(2+)-binding protein, and an unusual protein kinase, but also several proteins with unknown function.
Induction of necrotic cell death and mitochondrial permeabilization by heme binding protein 2/SOUL.
Gallyas et al., Pécs, Hungary. In Febs Lett, 2006
SOUL promotes necrotic cell death by inducing mitochondrial permeability transition
The first structure from the SOUL/HBP family of heme-binding proteins, murine P22HBP.
Goodfellow et al., Caparica, Portugal. In J Biol Chem, 2006
Murine p22HBP, a 22-kDa monomer originally identified as a cytosolic heme-binding protein ubiquitously expressed in various tissues, has 27% sequence identity to murine SOUL, a heme-binding hexamer specifically expressed in the retina.
SOUL in mouse eyes is a new hexameric heme-binding protein with characteristic optical absorption, resonance Raman spectral, and heme-binding properties.
Shimizu et al., Sendai, Japan. In Biochemistry, 2004
The heme-binding properties and coordination structure of SOUL protein are distinct from those of mouse liver p22HBP, despite high sequence homology.
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