- direct the flow of; "channel information towards a broad audience" (同)canalize, canalise
- a television station and its programs; "a satellite TV channel"; "surfing through the channels"; "they offer more than one hundred channels" (同)television channel, TV channel
- a passage for water (or other fluids) to flow through; "the fields were crossed with irrigation channels"; "gutters carried off the rainwater into a series of channels under the street"
- (often plural) a means of communication or access; "it must go through official channels"; "lines of communication were set up between the two firms" (同)communication channel, line
- a path over which electrical signals can pass; "a channel is typically what you rent from a telephone company" (同)transmission channel
- a deep and relatively narrow body of water (as in a river or a harbor or a strait linking two larger bodies) that allows the best passage for vessels; "the ship went aground in the channel"
- any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"
- official routes of communication; "you have to go through channels"
- 〈C〉『水路』(川・湾・運河の船の通行ができる深い部分) / 〈U〉河床・川底 / 〈C〉『海峡』 / 〈C〉みぞ(groove),(道路の)水渠(すいきょ) / 《複数形で》(運搬・伝達の)正式の経路(手続き);(一般に)経路 / 〈C〉(テレビ・ラジオの)チャンネル / …‘に'水路を開く / …‘に'みぞを堀る / …'を'伝える,流す
全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.
- Solid phase extraction using magnetic core mesoporous shell microspheres with C18-modified interior pore-walls for residue analysis of cephalosporins in milk by LC-MS/MS.
- Liu X1, Yu Y1, Zhao M1, Zhang H2, Li Y3, Duan G1.Author information 1Department of Pharmaceutical Analysis, School of Pharmacy, Fudan University, No. 826 Zhangheng Road, Shanghai 201203, PR China.2Department of Biology, Dezhou University, Shangdong 253023, PR China.3Department of Pharmaceutical Analysis, School of Pharmacy, Fudan University, No. 826 Zhangheng Road, Shanghai 201203, PR China. Electronic address: email@example.com.AbstractA fast and effective extraction method has been developed for measuring the residue of cephalosporins (cefalexin, cefazolin, cefoperazone) in milk by using magnetic core-mesoporous shell microspheres with C18-functionalized interior pore-walls (C18-Fe3O4@mSiO2) as adsorbent. With no need for any protein precipitation procedure, the cephalosporins were directly adsorbed onto the C18-Fe3O4@mSiO2 microspheres through hydrophobic interaction with C18-groups (Octadecyl functional groups) functionalized in the interior walls of mesopore channels while the abundant proteins in milk sample were excluded out of the channel due to the size exclusion effect. Thereafter, the cephalosporins-absorbed C18-Fe3O4@mSiO2 microspheres were rapidly isolated by placing a magnet, and followed by liquid chromatography-tandem mass spectrometry analysis after eluted by methanol. Various parameters which could affect the extraction performance were optimised. The newly developed extraction method was successfully applied in determination of cephalosporin residues in milk samples, offering a valuable alternative to simplify and speed up the sample preparation step.
- Food chemistry.Food Chem.2014 May 1;150:206-12. doi: 10.1016/j.foodchem.2013.10.145. Epub 2013 Nov 4.
- A fast and effective extraction method has been developed for measuring the residue of cephalosporins (cefalexin, cefazolin, cefoperazone) in milk by using magnetic core-mesoporous shell microspheres with C18-functionalized interior pore-walls (C18-Fe3O4@mSiO2) as adsorbent. With no need for any pro
- PMID 24360441
- Transcription Factor Sp1 Regulates T-Type Ca(2+) Channel CaV 3.1 Gene Expression.
- González-Ramírez R, Martínez-Hernández E, Sandoval A, Felix R.Author information Department of Molecular Biology and Histocompatibility, "Dr. Manuel Gea González" General Hospital, Mexico City, Mexico.AbstractVoltage-gated T-type Ca(2+) (CaV 3) channels mediate a number of physiological events in developing and mature cells, and are implicated in neurological and cardiovascular diseases. In mammals, there are three distinct T-channel genes (CACNA1G, CACNA1H, and CACNA1I) encoding proteins (CaV 3.1-CaV 3.3) that differ in their localization as well as in molecular, biophysical, and pharmacological properties. The CACNA1G is a large gene that contains 38 exons and is localized in chromosome 17q22. Only basic characteristics of the CACNA1G gene promoter region have been investigated classifying it as a TATA-less sequence containing several potential transcription factor-binding motifs. Here, we cloned and characterized a proximal promoter region and initiated the analysis of transcription factors that control CaV 3.1 channel expression using the murine Cacna1g gene as a model. We isolated a ∼1.5 kb 5'-upstream region of Cacna1g and verified its transcriptional activity in the mouse neuroblastoma N1E-115 cell line. In silico analysis revealed that this region possesses a TATA-less minimal promoter that includes two potential transcription start sites and four binding sites for the transcription factor Sp1. The ability of one of these sites to interact with the transcription factor was confirmed by electrophoretic mobility shift assays. Consistent with this, Sp1 over-expression enhanced promoter activity while siRNA-mediated Sp1 silencing significantly decreased the level of CaV 3.1 protein and reduced the amplitude of whole-cell T-type Ca(2+) currents expressed in the N1E-115 cells. These results provide new insights into the molecular mechanisms that control CaV 3.1 channel expression. J. Cell. Physiol. 229: 551-560, 2014. © 2013 Wiley Periodicals, Inc.
- Journal of cellular physiology.J Cell Physiol.2014 May;229(5):551-60. doi: 10.1002/jcp.24432.
- Voltage-gated T-type Ca(2+) (CaV 3) channels mediate a number of physiological events in developing and mature cells, and are implicated in neurological and cardiovascular diseases. In mammals, there are three distinct T-channel genes (CACNA1G, CACNA1H, and CACNA1I) encoding proteins (CaV 3.1-CaV 3.
- PMID 23868804
- Protein expression pattern in cerebellum of Cav2.1 mutant, tottering-6j mice
- channel protein [′chan·el ‚prō‚tēn] (cell and molecular biology) Protein forming an aqueous pore spanning the lipid bilayer of the cell membrane which ... The precise control of this movement relies on the direct physical interaction ...
- channel [chan´el] a passage, cut, or groove through which something can pass or flow across a solid structure. calcium channel (calcium-sodium channel) a slow ... Recently his group has applied single molecule techniques to study protein channel ...
- channel protein
- aquaporin、water channel
- ion channel、ionic channel