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Potassium voltage-gated channel, subfamily G, member 1

KH2, Kv6.1
Voltage-gated potassium (Kv) channels represent the most complex class of voltage-gated ion channels from both functional and structural standpoints. Their diverse functions include regulating neurotransmitter release, heart rate, insulin secretion, neuronal excitability, epithelial electrolyte transport, smooth muscle contraction, and cell volume. This gene encodes a member of the potassium channel, voltage-gated, subfamily G. This gene is abundantly expressed in skeletal muscle. Multiple alternatively spliced transcript variants have been found in normal and cancerous tissues. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: KH1, ACID, CAN, FMR1, HAD
Papers on KH2
Optimizing the production of the biosurfactant lichenysin and its application in biofilm control.
Manresa et al., Barcelona, Spain. In J Appl Microbiol, Jan 2016
A production of 3·2 g l(-1) of lichenysin was achieved with an optimum medium containing 107·82 g l(-1) of molasses, 6·47 g l(-1) of NaNO3 and 9·7 g l(-1) of K2 HPO4 /KH2 PO4 , in which molasses and phosphate salts had a significant effect on biosurfactant production.
Proteomic analyses provide new insights into the responses of Pinus massoniana seedlings to phosphorus deficiency.
Wen et al., Guiyang, China. In Proteomics, Dec 2015
The selected seedlings were treated with 0.5 mM KH2 PO4 (control), 0.01 mM KH2 PO4 (P1) or 0.06 mM KH2 PO4 (P2) for 48 days.
Simultaneous determination of water-soluble whitening ingredients and adenosine in different cosmetic formulations by high-performance liquid chromatography coupled with photodiode array detection.
Abd El-Aty et al., Suwŏn, South Korea. In Int J Cosmet Sci, Dec 2015
METHODS: Separation by HPLC-DAD was conducted using a C18 column with a gradient elution of 5 mM KH2 PO4 buffer (containing 0.1% phosphoric acid) and methanol (containing 0.1% phosphoric acid).
A new validated HPLC method for the determination of sulforaphane: application to study pharmacokinetics of sulforaphane in rats.
Elbarbry et al., Hillsboro, United States. In Biomed Chromatogr, Dec 2015
The chromatographic analysis was achieved on a Shimadzu LC 20A HPLC system equipped with a Zorbax Eclipse XDB C18 column and an isocratic mobile phase consisted of 10 mM KH2 PO4 (pH 4.5) and acetonitrile HPLC grade (40:60, v/v) run at a flow rate of 1 ml/min for 10 minutes.
A Series of Aluminoborates Templated or Supported by Zinc-Amine Complexes.
Yang et al., Jinhua, China. In Chemistry, Nov 2015
The second harmonic generation (SHG) measurement shows that the SHG responses of 1-3 are about 2.5, 1.6, and 0.5 times that of KH2 PO4 .
(1)H, (15)N and (13)C backbone resonance assignments of the N-terminal, tandem KH domains of human hnRNP E1.
Hennig et al., Charleston, United States. In Biomol Nmr Assign, Oct 2015
Our NMR assignments lay the foundation for a detailed investigation of the dynamic cooperation of the tandem KH1 and KH2 domains to bind nucleic acids.
Pharmacogenomic Testing and Warfarin Management.
Maluso, Cerveteri, Italy. In Oncol Nurs Forum, Sep 2015
Its mode of action is to prevent vitamin K from converting to vitamin KH2, thereby inhibiting clotting factors (Johnson & Cavallari, 2015).
Clinical effect of four different ointment bases on healthy cat eyes.
Nell et al., Vienna, Austria. In Vet Ophthalmol, Jun 2015
Hundred grams of OB contained the following: OB-A: 35.17 g liquid paraffin (lp), 64.83 g white petrolatum (wp); OB-B: 10.03 g lp, 84.95 g wp 5.02 g lanolin; OB-C: 18.34 g lp, 51.40 g wp, 25.00 mg KH2 PO4 , 57.00 mg K2 HPO4 , 18.90 g eucerinum anhydricum, 11.28 g water for injections; and OB-D: 70 g unguentum lanalcoli, 20 g lp, 10 g aqua conservans.
Biophysical and biochemical analysis of hnRNP K: arginine methylation, reversible aggregation and combinatorial binding to nucleic acids.
Ostareck et al., In Biol Chem, 2014
Quantitative evaluation indicated that all hnRNP K homology domains of hnRNP K contribute differentially to RNA binding, with KH1-KH2 acting as a tandem domain and KH3 as an individual binding domain.
Fragile X family members have important and non-overlapping functions.
Ceman et al., In Biomol Concepts, 2011
They share significant homology in the protein functional domains, including the Tudor domains, the nuclear localization sequence, a protein-protein interaction domain, the KH1 and KH2 domains and the nuclear export sequence.
Structure and function of KH domains.
Regan et al., New Haven, United States. In Febs J, 2008
The interest derives from the observation that an individual with this Ile mutated to Asn, in the KH2 domain of fragile X mental retardation protein, exhibits a particularly severe form of the syndrome.
The vitamin K cycle.
Watzka et al., Bonn, Germany. In Vitam Horm, 2007
Vitamin K shuttles reducing equivalents as electrons between two enzymes: VKORC1, which is itself reduced by an unknown ER lumenal reductant in order to reduce vitamin K epoxide (K>O) to the quinone form (KH2); and gamma-glutamyl carboxylase, which catalyzes posttranslational gamma-carboxylation and oxidizes KH2 to K>O.
Molecular mechanisms mediating vascular calcification: role of matrix Gla protein.
Shanahan et al., Cambridge, United Kingdom. In Nephrology (carlton), 2006
Its expression is regulated by several factors including retinoic acid, vitamin D and extracellular calcium ions, and a reduced form of vitamin K (KH2) is important in maintaining MGP in an active form.
FMRP RNA targets: identification and validation.
Darnell et al., New York City, United States. In Genes Brain Behav, 2005
In addition, we present evidence that point mutations in the K-homology (KH)1 or KH2 domains of FMRP abrogate its polyribosome association in transfected neuroblastoma cells but that the deletion of the RGG box does not.
Vitamin K and energy transduction: a base strength amplification mechanism.
Naganathan et al., Pittsburgh, United States. In Science, 1995
In the base strength amplification sequence, the free energy of oxygenation of vitamin K hydroquinone (vitamin KH2) is used to transform a weak base to a strong base in order to effect proton removal from selected glutamate (Glu) residues in the blood-clotting proteins.
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