Results 31 to 40 of about 157,972 (251)
The PIP2 binding mode of the C2 domains of rabphilin‐3A [PDF]
Protein Science, 2008 AbstractPhosphatidylinositol‐4,5‐bisphosphate (PIP2) is a key player in the neurotransmitter release process. Rabphilin‐3A is a neuronal C2 domain tandem containing protein that is involved in this process. Both its C2 domains (C2A and C2B) are able to bind PIP2.
Montaville, P. +5 more
openaire +3 more sources
Neoplasia: An International Journal for Oncology Research, 2013 Organotypic models may provide mechanistic insight into colorectal cancer (CRC) morphology. Three-dimensional (3D) colorectal gland formation is regulated by phosphatase and tensin homologue deleted on chromosome 10 (PTEN) coupling of cell division cycle
Ishaan C. Jagan +8 more
doaj +1 more source
The role of phosphatidylserine on the membrane in immunity and blood coagulation
Biomarker Research, 2022 The negatively charged aminophospholipid, phosphatidylserine (PtdSer), is located in the inner leaflet of the plasma membrane in normal cells, and may be exposed to the outer leaflet under some immune and blood coagulation processes.
Jiao Wang +10 more
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Journal of Microbiology, Immunology and Infection, 2023 Background: Invasion of red blood cells by Plasmodium falciparum merozoites is governed by multiple receptor–ligand interactions which are critical for bridging the two cells together.
Akshay Munjal +2 more
doaj +1 more source
DUF581 is plant specific FCS-like zinc finger involved in protein-protein interaction. [PDF]
PLoS ONE, 2014 Zinc fingers are a ubiquitous class of protein domain with considerable variation in structure and function. Zf-FCS is a highly diverged group of C2-C2 zinc finger which is present in animals, prokaryotes and viruses, but not in plants.
Muhammed Jamsheer K, Ashverya Laxmi
doaj +1 more source
BMC Cell Biology, 2009 Background Ubiquitination serves multiple cellular functions, including proteasomal degradation and the control of stability, function, and intracellular localization of a wide variety of proteins.
Lalouel Jean-Marc +4 more
doaj +1 more source
Membrane-binding properties of the Factor VIII C2 domain [PDF]
Biochemical Journal, 2011 Factor VIII functions as a cofactor for Factor IXa in a membrane-bound enzyme complex. Membrane binding accelerates the activity of the Factor VIIIa–Factor IXa complex approx. 100000-fold, and the major phospholipid-binding motif of Factor VIII is thought to be on the C2 domain.
Valerie A, Novakovic +5 more
openaire +2 more sources
C2‐domain containing calcium sensors in neuroendocrine secretion [PDF]
Journal of Neurochemistry, 2016 The molecular mechanisms for calcium‐triggered membrane fusion have long been sought for, and detailed models now exist that account for at least some of the functions of the many proteins involved in the process. Key players in the fusion reaction are a group of proteins that, upon binding to calcium, trigger the merger of cargo‐filled vesicles with ...
Pinheiro, Paulo S +2 more
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FEBS Letters, EarlyView.In this study, we found that human cervical‐derived adipocytes maintain intracellular iron level by regulating the expression of iron transport‐related proteins during adrenergic stimulation. Melanotransferrin is predicted to interact with transferrin receptor 1 based on in silico analysis.
Rahaf Alrifai +9 more
wiley +1 more source
Haematologica, 2017 Factor VIII C-domains are believed to have specific functions in cofactor activity and in interactions with von Willebrand factor. We have previously shown that factor VIII is co-targeted with von Willebrand factor to the Weibel-Palade bodies in blood ...
Eduard H.T.M. Ebberink +7 more
doaj +1 more source