gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Erythrocyte membrane protein band 4.1

protein 4.1R
Top mentioned proteins: Actin, CAN, Glycophorin, CaM, HSP60
Papers on protein 4.1R
Anatomy of the red cell membrane skeleton: unanswered questions.
Lux, Boston, United States. In Blood, Feb 2016
The red cell membrane skeleton is a pseudohexagonal meshwork of spectrin, actin, protein 4.1R, ankyrin, and actin-associated proteins that laminates the inner membrane surface and attaches to the overlying lipid bilayer via band 3-containing multiprotein complexes at the ankyrin- and actin-binding ends of spectrin.
Interactions between Plasmodium falciparum skeleton-binding protein 1 and the membrane skeleton of malaria-infected red blood cells.
Cooke et al., Australia. In Biochim Biophys Acta, Jul 2015
Using a combination of approaches, we have defined the region of SBP1 that binds specifically to defined sub-domains of two major components of the RBC membrane skeleton, protein 4.1R and spectrin.
[Effects of membrane skeleton protein 4.1R on the efficiency of photodynamic therapy].
Ji et al., Zhengzhou, China. In Zhonghua Yi Xue Za Zhi, 2015
OBJECTIVE: To explore the effects of membrane skeleton protein 4.1R on the efficiency of photodynamic therapy (PDT).
HnRNP A1 tethers KSRP to an exon splicing silencer that inhibits an erythroid-specific splicing event in PU.1-induced erythroleukemia.
Baklouti et al., Villeurbanne, France. In Am J Cancer Res, 2014
Exon 16 inclusion is a critical splicing event that triggers the production of a functional protein 4.1R in mature normal erythroblasts, and is obviated in PU.1-induced erythroleukemia cells.
Protein 4.1R attenuates autoreactivity in experimental autoimmune encephalomyelitis by suppressing CD4(+) T cell activation.
Kang et al., Zhengzhou, China. In Cell Immunol, 2014
Protein 4.1R, a red cell membrane cytoskeletal protein, recently was identified as an important component of immunological synapse (IS) and acted as the negative regulator of CD4(+) T cell activation.
FERM family proteins and their importance in cellular movements and wound healing (review).
Jiang et al., Cardiff, United Kingdom. In Int J Mol Med, 2014
The protein 4.1R, ezrin, radixin, moesin (FERM) superfamily consists of over 40 proteins all containing a three lobed N-terminal FERM domain which binds a variety of cell-membrane associated proteins and lipids.
Unique structural changes in calcium-bound calmodulin upon interaction with protein 4.1R FERM domain: novel insights into the calcium-dependent regulation of 4.1R FERM domain binding to membrane proteins by calmodulin.
Takakuwa et al., Akita, Japan. In Cell Biochem Biophys, 2014
Calmodulin (CaM) binds to the FERM domain of 80 kDa erythrocyte protein 4.1R (R30) independently of Ca(2+) but, paradoxically, regulates R30 binding to transmembrane proteins in a Ca(2+)-dependent manner.
Phosphatidylinositol-4,5 bisphosphate (PIP(2)) inhibits apo-calmodulin binding to protein 4.1.
Takakuwa et al., Akita, Japan. In Biochem Biophys Res Commun, 2014
Membrane skeletal protein 4.1R(80) plays a key role in regulation of erythrocyte plasticity.
Protein 4.1R binds to CLASP2 and regulates dynamics, organization and attachment of microtubules to the cell cortex.
Correas et al., Madrid, Spain. In J Cell Sci, 2013
Protein 4.1R also controls binding of CLASP2 to MTs at the cell edge by locally altering GSK3 activity.
Novel mechanism of regulation of protein 4.1G binding properties through Ca2+/calmodulin-mediated structural changes.
Takakuwa et al., Akita, Japan. In Cell Biochem Biophys, 2013
Based upon sequence homologies with the Ca(2+)/CaM-binding motif in protein 4.1R headpiece region, we establish that the 4.1G S(71)RGISRFIPPWLKKQKS peptide (pepG) mediates Ca(2+)/CaM binding.
Hereditary red cell membrane disorders and laboratory diagnostic testing.
Zanella et al., Bristol, United Kingdom. In Int J Lab Hematol, 2013
The diagnosis of HE/HPP is based on abnormal red cell morphology and the detection of protein 4.1R deficiency or spectrin variants using gel electrophoresis.
Impaired intestinal calcium absorption in protein 4.1R-deficient mice due to altered expression of plasma membrane calcium ATPase 1b (PMCA1b).
An et al., New York City, United States. In J Biol Chem, 2013
Protein 4.1R was first identified in the erythrocyte membrane skeleton.
Two different unique cardiac isoforms of protein 4.1R in zebrafish, Danio rerio, and insights into their cardiac functions as related to their unique structures.
Cherr et al., Davis, United States. In Dev Growth Differ, 2010
The results indicate that the gene product of ZF4.1R is essential for normal morphological shape of the developing heart and to support the repetitive cycles of its muscle contraction and relaxation.
The Gerbich blood group system: a review.
Reid et al., In Immunohematology, 2009
GPC and GPD interact with protein 4.1R, contributing stability to RBC membrane.
Characterization of protein 4.1R in erythrocytes of zebrafish (Danio rerio): unique binding properties with transmembrane proteins and calmodulin.
Murata et al., Tokyo, Japan. In Comp Biochem Physiol B Biochem Mol Biol, 2007
This study defines unique structural and functional properties for ZF4.1R.
Molecular pathogenesis of meningiomas.
Reifenberger et al., Saint Louis, United States. In J Neurooncol, 2004
Current data indicate that meningioma initiation is closely linked to the inactivation of one or more members of the highly conserved protein 4.1 superfamily, including the neurofibromatosis type 2 gene product merlin/schwannomin, protein 4.IB (DAL-1) and protein 4.1R.
Cell-specific mitotic defect and dyserythropoiesis associated with erythroid band 3 deficiency.
Zon et al., Boston, United States. In Nat Genet, 2003
Rescue experiments in ret zebrafish embryos expressing transgenic slc4a1 with a variety of mutations show that the requirement for band 3 in normal erythroid mitosis is mediated through its protein 4.1R-binding domains.
share on facebooktweetadd +1mail to friends