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Beaded filament structural protein 2, phakinin

CP47, CP49, BFSP2
More than 99% of the vertebrate ocular lens is comprised of terminally differentiated lens fiber cells. Two lens-specific intermediate filament-like proteins, the protein product of this gene (phakinin), and filensin, are expressed only after fiber cell differentiation has begun. Both proteins are found in a structurally unique cytoskeletal element that is referred to as the beaded filament (BF). Mutations in this gene have been associated with juvenile-onset, progressive cataracts and Dowling-Meara epidermolysis bullosa simplex. [provided by RefSeq, Jun 2009] (from NCBI)
Top mentioned proteins: CAN, ACID, HAD, Chl, fibrillin-1
Papers on CP47
Structure-Based Modeling of Fluorescence Kinetics of Photosystem II: Relation between Its Dimeric Form and Photoregulation.
Shibata et al., In J Phys Chem B, Jan 2016
PSII-cc consists of two core antenna (CP43 and CP47) and the reaction center (RC) complex.
Photosystem II Assembly Steps Take Place in the Thylakoid Membrane of the Cyanobacterium Synechocystis sp. PCC6803.
Norling et al., Singapore, Singapore. In Plant Cell Physiol, Dec 2015
PCC6803 cyanobacterium strain lacking the CP47 antenna.
Multi-residue determination of 10 selected new psychoactive substances in wastewater samples by liquid chromatography-tandem mass spectrometry.
Thomaidis et al., Athens, Greece. In Talanta, Dec 2015
To the authors' knowledge, it is the first time that eight out of these substances (4'-methylpyrrolidinobutyrophenone (MPPP), a-pyrrolidinopentiophenone (a-PVP), 2-[(1S,3R)-3-hydroxycyclohexyl]-5-(2-methyl-2-octanyl) phenol (CP47,497), (1-naphthyl(1-pentyl-1H-indol-3-yl) methanone (JWH-018), (1-butyl-1H-indol-3-yl)(1-naphthyl) methanone (JWH-073), (4-ethyl-1-naphthyl)(1-pentyl-1H-indol-3-yl) methanone (JWH-210), (4-methyl-1-naphthyl) (1-pentyl-1H-indol-3-yl) methanone (JWH-122) and 2-(2-methoxyphenyl)-1-(1-pentyl-1H-indol-3-yl) ethanone (JWH-250)) are investigated in wastewater.
Interaction of the PsbH subunit with a chlorophyll bound to histidine 114 of CP47 is responsible for the red 77K fluorescence of Photosystem II.
Komenda et al., Amsterdam, Netherlands. In Biochim Biophys Acta, Oct 2015
The origin of this emission has been attributed to a monomeric 'red' chlorophyll molecule located in the CP47 subunit.
The Use of Contact Mode Atomic Force Microscopy in Aqueous Medium for Structural Analysis of Spinach Photosynthetic Complexes.
Grossman et al., Argentina. In Plant Physiol, Oct 2015
This study represents, to our knowledge, the first use of atomic force microscopy to distinguish the putative large extrinsic loop of Photosystem II CP47 reaction center protein (CP47) from the putative oxygen-evolving enhancer proteins 1, 2, and 3 (PsbO, PsbP, and PsbQ) and large extrinsic loop of Photosystem II CP43 reaction center protein (CP43) in the PSII-OEC extrinsic domains of grana membranes under conditions resulting in the disordered arrangement of PSII-OEC particles.
Phenotypes of Recessive Pediatric Cataract in a Cohort of Children with Identified Homozygous Gene Mutations (An American Ophthalmological Society Thesis).
Alkuraya et al., Riyadh, Saudi Arabia. In Trans Am Ophthalmol Soc, Sep 2015
The remaining 12 families each had mutations in 12 different genes (CRYAA, CRYBA1, AKR1E2, AGK, BFSP2, CYP27A1, CYP51A1, EPHA2, GCNT2, LONP1, RNLS, WDR87) with unique phenotypes noted for CYP27A1 (bilateral juvenile fleck with anterior and/or posterior capsular cataract and later cerebrotendinous xanthomatosis), EPHA2 (bilateral anterior persistent fetal vasculature), and BFSP2 (bilateral flecklike with cloudy cortex).
Impact of a synthetic cannabinoid (CP-47,497-C8) on protein expression in human cells: evidence for induction of inflammation and DNA damage.
Knasm├╝ller et al., Vienna, Austria. In Arch Toxicol, Aug 2015
In order to predict potential health effects in consumers and to elucidate the underlying mechanisms of action, we investigated the impact of a representative of the cyclohexylphenols, CP47,497-C8, which binds to both cannabinoid receptors, on protein expression patterns, genomic stability and on induction of inflammatory cytokines in human lymphocytes.
The role of putrescine in the regulation of proteins and fatty acids of thylakoid membranes under salt stress.
Guo et al., Nanjing, China. In Sci Rep, 2014
BN-PAGE revealed Put up-regulated the expression of ATP synthase, CP47, D1, Qb, and psbA proteins and down-regulated CP24, D2, and LHCII type III in NaCl-stressed thylakoid membranes.
Light harvesting in photosystem II.
Croce et al., Wageningen, Netherlands. In Photosynth Res, 2013
The RC is located in the PSII core that also contains the inner light-harvesting complexes CP43 and CP47, harboring 13 and 16 chlorophyll pigments, respectively.
Complex RNA metabolism in the chloroplast: an update on the psbB operon.
Meurer et al., Martinsried, Germany. In Planta, 2013
It encodes the subunits CP47 (psbB), T (psbT), and H (psbH) of photosystem II as well as cytochrome b (6) (petB) and subunit IV (petD) of the cytochrome b (6) f complex.
Novel recessive BFSP2 and PITX3 mutations: insights into mutational mechanisms from consanguineous populations.
Alkuraya et al., Riyadh, Saudi Arabia. In Genet Med, 2011
Data show that BFSP2 and PITX3, hitherto known to cause eye defects only in a dominant fashion, can also present recessively.
Optical properties, excitation energy and primary charge transfer in photosystem II: theory meets experiment.
Schlodder et al., Austria. In J Photochem Photobiol B, 2011
We also discuss the stationary and time-dependent optical properties of the CP43 and CP47 subunits and the excitation energy transfer and trapping-by-charge-transfer kinetics in the core complex.
Light-harvesting and structural organization of Photosystem II: from individual complexes to thylakoid membrane.
van Amerongen et al., Groningen, Netherlands. In J Photochem Photobiol B, 2011
The RC is located in the PSII core which also contains light-harvesting complexes CP43 and CP47.
Primary photophysical processes in photosystem II: bridging the gap between crystal structure and optical spectra.
Schlodder et al., Linz, Austria. In Chemphyschem, 2010
Evidence that exciton transfer between the core antenna complexes CP43 and CP47 and the RC is the bottleneck for the overall photochemical trapping of excitation energy in PS-II is discussed.
Removal of Hsf4 leads to cataract development in mice through down-regulation of gamma S-crystallin and Bfsp expression.
Hu et al., Shanghai, China. In Bmc Mol Biol, 2008
disruption of the Hsf4 gene leads to cataracts via at least three pathways: down-regulation of gamma-crystallin, particularly gamma S-crystallin; decreased lens beaded filament expression; and loss of post-translational modification of alpha A-crystallin
A new mutation in BFSP2 (G1091A) causes autosomal dominant congenital lamellar cataracts.
Zhu et al., Beijing, China. In Mol Vis, 2007
This is the first reported case of a congenital lamellar cataract phenotype associated with the mutation of Arg339His (P.R339H) in BFSP2.
The E233del mutation in BFSP2 causes a progressive autosomal dominant congenital cataract in a Chinese family.
Fu et al., Harbin, China. In Mol Vis, 2006
Progressive phenotype has provided more evidence for the heterogeneity of congenital cataract caused by BFSP2 mutations and for the important role BFSP2 plays in cataract formation.
Progressive sutural cataract associated with a BFSP2 mutation in a Chinese family.
Liu et al., Harbin, China. In Mol Vis, 2005
Progressive isolated sutural cataract associated with deletion mutation of BFSP2 gene in Chinese pedigree. Physiological importance of beaded filament protein. Role of BFSP2 in human cataract formation.
Crystal structure of photosystem II from Synechococcus elongatus at 3.8 A resolution.
Orth et al., Berlin, Germany. In Nature, 2001
To date, structural information on the architecture of the complex has been provided by electron microscopy of intact, active photosystem II at 15-30 A resolution, and by electron crystallography on two-dimensional crystals of D1-D2-CP47 photosystem II fragments without water oxidizing activity at 8 A resolution.
Three-dimensional structure of the plant photosystem II reaction centre at 8 A resolution.
K├╝hlbrandt et al., Frankfurt am Main, Germany. In Nature, 1998
Here we report the three-dimensional structure of a photosystem II subcomplex, containing the proteins D1, D2, CP47 and cytochrome b-559, determined by electron crystallography.
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