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

LanC lantibiotic synthetase component C-like 1

erythrocyte membrane protein 1, LANCL1
This gene encodes a loosely associated peripheral membrane protein related to the LanC family of bacterial membrane-associated proteins involved in the biosynthesis of antimicrobial peptides. This protein may play a role as a peptide-modifying enzyme component in eukaryotic cells. Previously considered a member of the G-protein-coupled receptor superfamily, this protein is now in the LanC family. Multiple alternatively spliced variants, encoding the same protein, have been identified. [provided by RefSeq, Nov 2008] (from NCBI)
Top mentioned proteins: CAN, CsA, CD36, HAD, V1a
Papers on erythrocyte membrane protein 1
The role of PfEMP1 as targets of naturally acquired immunity to childhood malaria: prospects for a vaccine.
Abdi et al., Cambridge, United Kingdom. In Parasitology, Feb 2016
UNASSIGNED: The Plasmodium falciparum erythrocyte membrane protein 1 antigens that are inserted onto the surface of P. falciparum infected erythrocytes play a key role both in the pathology of severe malaria and as targets of naturally acquired immunity.
Maintenance of phenotypic diversity within a set of virulence encoding genes of the malaria parasite Plasmodium falciparum.
Recker et al., Exeter, United Kingdom. In J R Soc Interface, Jan 2016
The var gene-encoded surface proteins Plasmodium falciparum erythrocyte membrane protein 1 mediate variant-specific binding of infected red blood cells to a diverse set of host receptors that has been linked to specific disease manifestations, including cerebral and pregnancy-associated malaria.
Functional analysis of monoclonal antibodies against the Plasmodium falciparum PfEMP1-VarO adhesin.
Mercereau-Puijalon et al., Paris, France. In Malar J, Dec 2015
Rosetting results from specific interactions between a subset of variant P. falciparum erythrocyte membrane protein 1 (PfEMP1) adhesins encoded by var genes, serum components and RBC receptors.
PfEMP1 - A Parasite Protein Family of Key Importance in Plasmodium falciparum Malaria Immunity and Pathogenesis.
Jensen et al., Copenhagen, Denmark. In Adv Parasitol, Apr 2015
Among several proteins and protein families implicated in this process, the P. falciparum erythrocyte membrane protein 1 (PfEMP1) family of high-molecular weight and highly variable antigens appears to be the most prominent.
Alternative functions of the brain transsulfuration pathway represent an underappreciated aspect of brain redox biochemistry with significant potential for therapeutic engagement.
Denton et al., Toledo, United States. In Free Radic Biol Med, 2015
The known biological origins of lanthionine and its ketimine metabolite will be described in detail and placed in context with recent discoveries of a GSH- and LK-binding brain protein called LanCL1 that is proving essential for neuronal antioxidant defense; and a related LanCL2 homolog now implicated in immune sensing and cell fate determinations.
Beninese children with cerebral malaria do not develop humoral immunity against the IT4-VAR19-DC8 PfEMP1 variant linked to EPCR and brain endothelial binding.
Gamain et al., Paris, France. In Malar J, 2014
Cytoadhesion of IEs is mediated by members of the highly diverse Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1).
Haplotypes of the endothelial protein C receptor (EPCR) gene are not associated with severe malaria in Tanzania.
Lavstsen et al., Copenhagen, Denmark. In Malar J, 2014
BACKGROUND: Endothelial protein C receptor (EPCR) was recently identified as a key receptor for Plasmodium falciparum erythrocyte membrane protein 1 mediating sequestration of P. falciparum-infected erythrocytes in patients suffering from severe malaria.
Developing vaccines to prevent malaria in pregnant women.
Deloron et al., Paris, France. In Expert Opin Biol Ther, 2014
EXPERT OPINION: The approach taken to develop a P. falciparum erythrocyte membrane protein 1-based vaccine to protect pregnant women is very promising in view of the current difficulties of achieving a sterilizing vaccine against malaria parasite.
The role of PfEMP1 adhesion domain classification in Plasmodium falciparum pathogenesis research.
Smith, Seattle, United States. In Mol Biochem Parasitol, 2014
The Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) family has a key role in parasite survival, transmission, and virulence.
Pathogenesis of cerebral malaria--inflammation and cytoadherence.
Craig et al., Liverpool, United Kingdom. In Front Cell Infect Microbiol, 2013
Recent data have suggested that a combination of parasite variant types, mainly defined by the variant surface antigen, P. falciparum erythrocyte membrane protein 1 (PfEMP1), its receptors, coagulation and host endothelial cell activation (or inflammation) are equally important.
PfSETvs methylation of histone H3K36 represses virulence genes in Plasmodium falciparum.
Miller et al., Shanghai, China. In Nature, 2013
The variant antigen Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1), which is expressed on the surface of P. falciparum-infected red blood cells, is a critical virulence factor for malaria.
Severe malaria is associated with parasite binding to endothelial protein C receptor.
Theander et al., Copenhagen, Denmark. In Nature, 2013
Sequestration is mediated by specific interactions between members of the P. falciparum erythrocyte membrane protein 1 (PfEMP1) family and receptors on the endothelial lining.
Structure of human lanthionine synthetase C-like protein 1 and its interaction with Eps8 and glutathione.
Zhang et al., Beijing, China. In Genes Dev, 2009
the crystal structures of human LanCL1, both free of and complexed with glutathione, revealing glutathione binding to a zinc ion at the putative active site formed by conserved GxxG motifs
A var gene promoter controls allelic exclusion of virulence genes in Plasmodium falciparum malaria.
Cowman et al., Australia. In Nature, 2006
In the apicomplexan parasite Plasmodium falciparum, responsible for the severe form of malaria in humans, this is exemplified by antigenic variation of the highly polymorphic P. falciparum erythrocyte membrane protein 1 (PfEMP1).
Structural basis for Duffy recognition by the malaria parasite Duffy-binding-like domain.
Sharma et al., New Delhi, India. In Nature, 2006
DBLs of parasite erythrocyte-binding proteins mediate invasion, and those from the antigenically variant P. falciparum erythrocyte membrane protein 1 (PfEMP1) have been implicated in cytoadherence.
Role of nonimmune IgG bound to PfEMP1 in placental malaria.
Wahlgren et al., Stockholm, Sweden. In Science, 2001
Normal, nonimmune IgG that is bound to a duffy binding-like domain beta of the P. falciparum erythrocyte membrane protein 1 (PfEMP1) might at the IE surface act as a bridge to neonatal Fc receptors of the placenta.
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