Database : MEDLINE
Search on : D02.455.426.559.389.097.150 [DeCS Category]
References found : 614 [refine]
Displaying: 1 .. 10   in format [Large]

page 1 of 62 go to page                         

  1 / 614 MEDLINE  
              next record last record
select
to print
Photocopy
Full text
PMID:25432972
Author:Wang TD; Zhang HF; Wu ZC; Li JG; Huang XM; Wang HC
Address:Physiological Laboratory for South China Fruits, College of Horticulture, South China Agricultural University, Guangzhou, 510642, PR China These authors contributed equally to this work.
Title:Sugar uptake in the Aril of litchi fruit depends on the apoplasmic post-phloem transport and the activity of proton pumps and the putative transporter LcSUT4.
Source:Plant Cell Physiol; 56(2):377-87, 2015 Feb.
ISSN:1471-9053
Country of publication:Japan
Language:eng
Abstract:The post-phloem unloading pathway and the mechanism of sugar accumulation remain unclear in litchi fruit. A combination of electron microscopy, transport of phloem-mobile symplasmic tracer (carboxyfluorescein, CF) and biochemical and molecular assays was used to explore the post-phloem transport pathway and the mechanism of aril sugar accumulation in litchi. In the funicle, where the aril originates, abundant plasmodesmata were observed, and CF introduced from the peduncle diffused to the parenchyma cells. In addition, abundant starch and pentasaccharide were detected and the sugar concentration was positively correlated with activities of sucrose hydrolysis enzymes. These results clearly showed that the phloem unloading and post-phloem transport in the funicle were symplastic. On the other hand, imaging of CF showed that it remained confined to the parenchyma cells in funicle tissues connecting the aril. Infiltration of both an ATPase inhibitor [eosin B (EB)] and a sucrose transporter inhibitor [p-chloromercuribenzene sulfonate (PCMBS)] inhibited sugar accumulation in the aril. These results indicated an apoplasmic post-phloem sugar transport from the funicle to the aril. Although facilitated diffusion might help sucrose uptake from the cytosol to the vacuole in cultivars with high soluble invertase, membrane ATPases in the aril, especially tonoplast ATPase, are crucial for aril sugar accumulation. The expression of a putative aril vacuolar membrane sucrose transporter gene (LcSUT4) was highly correlated with the sugar accumulation in the aril of litchi. These data suggest that apoplasmic transport is critical for sugar accumulation in litchi aril and that LcSUT4 is involved in this step.
Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Name of substance:0 (Fluoresceins); 0 (Membrane Transport Proteins); 0 (Plant Proteins); 0 (Proton Pumps); 3301-79-9 (6-carboxyfluorescein); 5YIN07W42H (4-Chloromercuribenzenesulfonate); EC 3.6.1.- (Vacuolar Proton-Translocating ATPases); OMS4XQD1T0 (Eosine I Bluish)


  2 / 614 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text
PMID:24292275
Author:Dédaldéchamp F; Saeedi S; Fleurat-Lessard P; Roblin G
Address:Université de Poitiers, EBI UMR CNRS 7267, Equipe Physiologie Moléculaire du Transport des Sucres, 3 rue Jacques Fort, 86022 Poitiers cedex, France. Electronic address: fabienne.dedaldechamp@univ-poitiers.fr.
Title:Uptake and metabolic effects of salicylic acid on the pulvinar motor cells of Mimosa pudica L.
Source:Plant Physiol Biochem; 74:125-32, 2014 Jan.
ISSN:1873-2690
Country of publication:France
Language:eng
Abstract:In this paper, the salicylic acid (o-hydroxy benzoic acid) (SA) uptake by the pulvinar tissues of Mimosa pudica L. pulvini was shown to be strongly pH-dependent, increasing with acidity of the assay medium. This uptake was performed according to a unique affinity system (K(m) = 5.9 mM, V(m) = 526 pmol mgDW(-1)) in the concentration range of 0.1-5 mM. The uptake rate increased with increasing temperature (5-35 °C) and was inhibited following treatment with sodium azide (NaN3) and carbonyl cyanide m-chlorophenylhydrazone (CCCP), suggesting the involvement of an active component. Treatment with p-chloromercuribenzenesulfonic acid (PCMBS) did not modify the uptake, indicating that external thiol groups were not necessary. KCl, which induced membrane depolarization had no significant effect, and fusicoccin (FC), which hyperpolarized cell membrane, stimulated the uptake, suggesting that the pH component of the proton motive force was likely a driving force. These data suggest that the SA uptake by the pulvinar tissues may be driven by two components: an ion-trap mechanism playing a pivotal role and a putative carrier-mediated mechanism. Unlike other benzoic acid derivatives acting as classical respiration inhibitors (NaN3 and KCN), SA modified the pulvinar cell metabolism by increasing the respiration rate similar to CCCP and 2,4-dinitrophenol (DNP). Furthermore, SA inhibited the osmoregulated seismonastic reaction in a pH dependent manner and induced characteristic damage to the ultrastructural features of the pulvinar motor cells, particularly at the mitochondrial level.
Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Name of substance:555-60-2 (Carbonyl Cyanide m-Chlorophenyl Hydrazone); 5YIN07W42H (4-Chloromercuribenzenesulfonate); 968JJ8C9DV (Sodium Azide); O414PZ4LPZ (Salicylic Acid)


  3 / 614 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
PubMed Central Full text
Full text
PMID:24376811
Author:Lindinger MI; Leung MJ; Hawke TJ
Address:Department of Human Health and Nutritional Sciences, University of Guelph, Guelph, Ontario, Canada.
Title:Inward flux of lactate⁻ through monocarboxylate transporters contributes to regulatory volume increase in mouse muscle fibres.
Source:PLoS One; 8(12):e84451, 2013.
ISSN:1932-6203
Country of publication:United States
Language:eng
Abstract:Mouse and rat skeletal muscles are capable of a regulatory volume increase (RVI) after they shrink (volume loss resultant from exposure to solutions of increased osmolarity) and that this RVI occurs mainly by a Na-K-Cl-Cotransporter (NKCC)-dependent mechanism. With high-intensity exercise, increased extracellular osmolarity is accompanied by large increases in extracellular [lactate⁻]. We hypothesized that large increases in [lactate⁻] and osmolarity augment the NKCC-dependent RVI response observed with a NaCl (or sucrose)-induced increase in osmolarity alone; a response that is dependent on lactate⁻ influx through monocarboxylate transporters (MCTs). Single mouse muscle fibres were isolated and visualized under light microscopy under varying osmolar conditions. When solution osmolarity was increased by adding NaLac by 30 or 60 mM, fibres lost significantly less volume and regained volume sooner compared to when NaCl was used. Phloretin (MCT1 inhibitor) accentuated the volume loss compared to both NaLac controls, supporting a role for MCT1 in the RVI response in the presence of elevated [lactate⁻]. Inhibition of MCT4 (with pCMBS) resulted in a volume loss, intermediate to that seen with phloretin and NaLac controls. Bumetanide (NKCC inhibitor), in combination with pCMBS, reduced the magnitude of volume loss, but volume recovery was complete. While combined phloretin-bumetanide also reduced the magnitude of the volume loss, it also largely abolished the cell volume recovery. In conclusion, RVI in skeletal muscle exposed to raised tonicity and [lactate⁻] is facilitated by inward flux of solute by NKCC- and MCT1-dependent mechanisms. This work demonstrates evidence of a RVI response in skeletal muscle that is facilitated by inward flux of solute by MCT-dependent mechanisms. These findings further expand our understanding of the capacities for skeletal muscle to volume regulate, particularly in instances of raised tonicity and lactate⁻ concentrations, as occurs with high intensity exercise.
Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Name of substance:0 (Monocarboxylic Acid Transporters); 0 (Muscle Proteins); 0 (Slc16a4 protein, mouse); 0Y2S3XUQ5H (Bumetanide); 33X04XA5AT (Lactic Acid); 5YIN07W42H (4-Chloromercuribenzenesulfonate); S5J5OE47MK (Phloretin)


  4 / 614 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
PubMed Central Full text
Full text
PMID:24009076
Author:Stewart DS; Hotta M; Li GD; Desai R; Chiara DC; Olsen RW; Forman SA
Address:From the Department of Anesthesia Critical Care and Pain Medicine, Massachusetts General Hospital, Boston, Massachusetts 02114.
Title:Cysteine substitutions define etomidate binding and gating linkages in the α-M1 domain of γ-aminobutyric acid type A (GABAA) receptors.
Source:J Biol Chem; 288(42):30373-86, 2013 Oct 18.
ISSN:1083-351X
Country of publication:United States
Language:eng
Abstract:Etomidate is a potent general anesthetic that acts as an allosteric co-agonist at GABAA receptors. Photoreactive etomidate derivatives labeled αMet-236 in transmembrane domain M1, which structural models locate in the ß+/α- subunit interface. Other nearby residues may also contribute to etomidate binding and/or transduction through rearrangement of the site. In human α1ß2γ2L GABAA receptors, we applied the substituted cysteine accessibility method to α1-M1 domain residues extending from α1Gln-229 to α1Gln-242. We used electrophysiology to characterize each mutant's sensitivity to GABA and etomidate. We also measured rates of sulfhydryl modification by p-chloromercuribenzenesulfonate (pCMBS) with and without GABA and tested if etomidate blocks modification of pCMBS-accessible cysteines. Cys substitutions in the outer α1-M1 domain impaired GABA activation and variably affected etomidate sensitivity. In seven of eight residues where pCMBS modification was evident, rates of modification were accelerated by GABA co-application, indicating that channel activation increases water and/or pCMBS access. Etomidate reduced the rate of modification for cysteine substitutions at α1Met-236, α1Leu-232 and α1Thr-237. We infer that these residues, predicted to face ß2-M3 or M2 domains, contribute to etomidate binding. Thus, etomidate interacts with a short segment of the outer α1-M1 helix within a subdomain that undergoes significant structural rearrangement during channel gating. Our results are consistent with in silico docking calculations in a homology model that orient the long axis of etomidate approximately orthogonal to the transmembrane axis.
Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
Name of substance:0 (Anesthetics, Intravenous); 0 (Enzyme Inhibitors); 0 (Receptors, GABA-A); 5YIN07W42H (4-Chloromercuribenzenesulfonate); Z22628B598 (Etomidate)


  5 / 614 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
PubMed Central Full text
Full text
PMID:23552862
Author:Geyer RR; Musa-Aziz R; Enkavi G; Mahinthichaichan P; Tajkhorshid E; Boron WF
Address:Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, OH 44106, USA. rrg8@cwru.edu
Title:Movement of NH3 through the human urea transporter B: a new gas channel.
Source:Am J Physiol Renal Physiol; 304(12):F1447-57, 2013 Jun 15.
ISSN:1522-1466
Country of publication:United States
Language:eng
Abstract:Aquaporins and Rh proteins can function as gas (CO2 and NH3) channels. The present study explores the urea, H2O, CO2, and NH3 permeability of the human urea transporter B (UT-B) (SLC14A1), expressed in Xenopus oocytes. We monitored urea uptake using [¹4C]urea and measured osmotic water permeability (Pf) using video microscopy. To obtain a semiquantitative measure of gas permeability, we used microelectrodes to record the maximum transient change in surface pH (ΔpHS) caused by exposing oocytes to 5% CO2/33 mM HCO3⁻ (pHS increase) or 0.5 mM NH3/NH4⁺ (pHS decrease). UT-B expression increased oocyte permeability to urea by >20-fold, and Pf by 8-fold vs. H2O-injected control oocytes. UT-B expression had no effect on the CO2-induced ΔpHS but doubled the NH3-induced ΔpHS. Phloretin reduced UT-B-dependent urea uptake (Jurea*) by 45%, Pf* by 50%, and (- ΔpHS*)NH3 by 70%. p-Chloromercuribenzene sulfonate reduced Jurea* by 25%, Pf* by 30%, and (ΔpHS*)NH3 by 100%. Molecular dynamics (MD) simulations of membrane-embedded models of UT-B identified the monomeric UT-B pores as the main conduction pathway for both H2O and NH3 and characterized the energetics associated with permeation of these species through the channel. Mutating each of two conserved threonines lining the monomeric urea pores reduced H2O and NH3 permeability. Our data confirm that UT-B has significant H2O permeability and for the first time demonstrate significant NH3 permeability. Thus the UTs become the third family of gas channels. Inhibitor and mutagenesis studies and results of MD simulations suggest that NH3 and H2O pass through the three monomeric urea channels in UT-B.
Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
Name of substance:0 (Gases); 0 (Membrane Transport Proteins); 0 (urea transporter); 059QF0KO0R (Water); 142M471B3J (Carbon Dioxide); 5YIN07W42H (4-Chloromercuribenzenesulfonate); 7664-41-7 (Ammonia); 8W8T17847W (Urea); S5J5OE47MK (Phloretin)


  6 / 614 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text
PMID:23546606
Author:Lima de Souza EC; Groeneweg S; Visser WE; Peeters RP; Visser TJ
Address:PhD, Department of Internal Medicine, Erasmus University Medical Center, BO Box 2040, 3000 CA Rotterdam, The Netherlands.
Title:Importance of cysteine residues in the thyroid hormone transporter MCT8.
Source:Endocrinology; 154(5):1948-55, 2013 May.
ISSN:1945-7170
Country of publication:United States
Language:eng
Abstract:The thyroid hormone (TH) transporter monocarboxylate transporter 8 (MCT8) is crucial for brain development as demonstrated by the severe psychomotor retardation in patients with MCT8 mutations. MCT8 contains 10 residues of the reactive amino acid cysteine (Cys) whose functional roles were studied using the Cys-specific reagent p-chloromercurybenzenesulfonate (pCMBS) and by site-directed mutagenesis. Pretreatment of JEG3 cells with pCMBS resulted in a dose- and time-dependent decrease of subsequent T3 uptake. Pretreatment with dithiothreitol did not affect TH transport or its inhibition by pCMBS. However, pCMBS inhibition of MCT8 was reversed by dithiothreitol. Inhibition of MCT8 by pCMBS was prevented in the presence of T3. The single and double mutation of C481A and C497A did not affect T3 transport, but the single mutants were less sensitive and the double mutant was completely insensitive to pCMBS. Similar effects on MCT8 were obtained using HgCl2 instead of pCMBS. In conclusion, we have identified Cys481 and Cys497 in MCT8 as the residues modified by pCMBS or HgCl2. These residues are probably located at or near the substrate-recognition site in MCT8. It remains to be investigated whether MCT8 function is regulated by modification of these Cys residues under pathophysiological conditions.
Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Name of substance:0 (Monocarboxylic Acid Transporters); 0 (SLC16A2 protein, human); 0 (Sulfhydryl Reagents); 5YIN07W42H (4-Chloromercuribenzenesulfonate); K848JZ4886 (Cysteine); OF5P57N2ZX (Alanine); T8ID5YZU6Y (Dithiothreitol)


  7 / 614 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text
PMID:21707653
Author:Hu L; Sun H; Li R; Zhang L; Wang S; Sui X; Zhang Z
Address:College of Agronomy and Biotechnology, China Agricultural University, Beijing 100193, China.
Title:Phloem unloading follows an extensive apoplasmic pathway in cucumber (Cucumis sativus L.) fruit from anthesis to marketable maturing stage.
Source:Plant Cell Environ; 34(11):1835-48, 2011 Nov.
ISSN:1365-3040
Country of publication:United States
Language:eng
Abstract:The phloem unloading pathway remains unclear in fruits of Cucurbitaceae, a classical stachyose-transporting species with bicollateral phloem. Using a combination of electron microscopy, transport of phloem-mobile symplasmic tracer carboxyfluorescein, assays of acid invertase and sucrose transporter, and [(14)C]sugar uptake, the phloem unloading pathway was studied in cucumber (Cucumis sativus) fruit from anthesis to the marketable maturing stage. Structural investigations showed that the sieve element-companion cell (SE-CC) complex of the vascular bundles feeding fruit flesh is apparently symplasmically restricted. Imaging of carboxyfluorescein unloading showed that the dye remained confined to the phloem strands of the vascular bundles in the whole fruit throughout the stages examined. A 37 kDa acid invertase was located predominantly in the cell walls of SE-CC complexes and parenchyma cells. Studies of [(14)C]sugar uptake suggested that energy-driven transporters may be functional in sugar trans-membrane transport within symplasmically restricted SE-CC complex, which was further confirmed by the existence of a functional plasma membrane sucrose transporter (CsSUT4) in cucumber fruit. These data provide a clear evidence for an apoplasmic phloem unloading pathway in cucumber fruit. A presumption that putative raffinose or stachyose transporters may be involved in soluble sugars unloading was discussed.
Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Name of substance:0 (Carbon Radioisotopes); 0 (Fluoresceins); 0 (Membrane Transport Proteins); 0 (Plant Proteins); 0 (sucrose transport protein, plant); 555-60-2 (Carbonyl Cyanide m-Chlorophenyl Hydrazone); 5YIN07W42H (4-Chloromercuribenzenesulfonate); EC 3.2.1.26 (beta-Fructofuranosidase); IY9XDZ35W2 (Glucose)


  8 / 614 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
PubMed Central Full text
Full text
PMID:21362624
Author:Parikh RB; Bali M; Akabas MH
Address:Department of Physiology & Biophysics, Albert Einstein College of Medicine of Yeshiva University, Bronx, New York 10461, USA.
Title:Structure of the M2 transmembrane segment of GLIC, a prokaryotic Cys loop receptor homologue from Gloeobacter violaceus, probed by substituted cysteine accessibility.
Source:J Biol Chem; 286(16):14098-109, 2011 Apr 22.
ISSN:1083-351X
Country of publication:United States
Language:eng
Abstract:GLIC is a homopentameric proton-gated, prokaryotic homologue of the Cys loop receptor family of neurotransmitter-gated ion channels. Recently, crystal structures of GLIC hypothesized to represent an open channel state were published. To explore the channel structure in functional GLIC channels, we tested the ability of p-chloromercuribenzenesulfonate to react with 30 individual cysteine substitution mutants in and flanking the M2 channel-lining segment in the closed state (pH 7.5) and in a submaximally activated state (pH 5.0). Nine mutants did not tolerate cysteine substitution and were not functional. From positions 10' to 27', p-chloromercuribenzenesulfonate significantly modified the currents at pH 7.5 and 5.0 in all mutants except H234C (11'), I235C (12'), V241C (18'), T243C (20'), L245C (22'), and Y250C (27'), which were not functional, except for 12'. Currents for P246C (23') and K247C (24') were only significantly altered at pH 5.0. The reaction rates were all >1000 m(-1) s(-1). The reactive residues were more accessible in the activated than in the resting state. We infer that M2 is tightly associated with the adjacent transmembrane helices at the intracellular end but is more loosely packed from 10' to the extracellular end than the x-ray structures suggest. We infer that the charge selectivity filter is in the cytoplasmic half of the channel. We also show that below pH 5.0, GLIC desensitizes on a time scale of minutes and infer that the crystal structures may represent a desensitized state.
Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
Name of substance:0 (Ion Channels); 0 (Membrane Proteins); 0 (Neurotransmitter Agents); 0 (Protons); 0 (Receptors, GABA); 0 (Receptors, Nicotinic); 0 (Receptors, Serotonin, 5-HT3); 5YIN07W42H (4-Chloromercuribenzenesulfonate); K848JZ4886 (Cysteine)


  9 / 614 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
PMID:21289433
Author:Rao RP; Rao JP
Address:Department of Biochemistry, Kasturba Medical College, Manipal University, Manipal 576 104, India.
Title:Evidence for functional interaction of plasma membrane electron transport, voltage-dependent anion channel and volume-regulated anion channel in frog aorta.
Source:J Biosci; 35(4):519-24, 2010 Dec.
ISSN:0973-7138
Country of publication:India
Language:eng
Abstract:Frog aortic tissue exhibits plasma membrane electron transport (PMET) owing to its ability to reduce ferricyanide even in the presence of mitochondrial poisons, such as cyanide and azide. Exposure to hypotonic solution (108 mOsmol/kg H2O) enhanced the reduction of ferricyanide in excised aortic tissue of frog. Increment in ferricyanide reductase activity was also brought about by the presence of homocysteine (100 microM dissolved in isotonic frog Ringer solution), a redox active compound and a potent modulator of PMET. Two plasma-membrane-bound channels, the volume-regulated anion channel (VRAC) and the voltage-dependent anion channel (VDAC), are involved in the response to hypotonic stress. The presence of VRAC and VDAC antagonists-tamoxifen, glibenclamide, fluoxetine and verapamil, and 4,4'-diisothiocyanatostilbene-2,2'-disulphonic acid (DIDS), respectively-inhibited this enhanced activity brought about by either hypotonic stress or homocysteine. The blockers do not affect the ferricyanide reductase activity under isotonic conditions. Taken together, these findings indicate a functional interaction of the three plasma membrane proteins, namely, ferricyanide reductase (PMET), VDAC and VRAC.
Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Name of substance:0 (Anions); 0 (Ferricyanides); 0 (Hypotonic Solutions); 0 (Ion Channels); 0LVT1QZ0BA (Homocysteine); 5YIN07W42H (4-Chloromercuribenzenesulfonate); EC 1.6.- (NADH, NADPH Oxidoreductases); EC 1.6.99.- (ferricyanide reductase); U4MAF9C813 (potassium ferricyanide)


  10 / 614 MEDLINE  
              first record previous record
select
to print
Photocopy
Full text
PMID:20933499
Author:Forcato D; Posada V; Beaugé L; Berberián G
Address:Laboratorio de Biofísica, Instituto de Investigación Médica Mercedes y Martín Ferreyra (INIMEC-CONICET), CC 389, 5000 Córdoba, Argentina.
Title:Optimal metabolic regulation of the mammalian heart Na(+)/Ca(2+) exchanger requires a spacial arrangements with a PtdIns(4)-5kinase.
Source:Biochem Biophys Res Commun; 402(1):147-52, 2010 Nov 05.
ISSN:1090-2104
Country of publication:United States
Language:eng
Abstract:In inside-out bovine heart sarcolemmal vesicles, p-chloromercuribenzenesulfonate (PCMBS) and n-ethylmaleimide (NEM) fully inhibited MgATP up-regulation of the Na(+)/Ca(2+) exchanger (NCX1) and abolished the MgATP-dependent PtdIns-4,5P2 increase in the NCX1-PtdIns-4,5P2 complex; in addition, these compounds markedly reduced the activity of the PtdIns(4)-5kinase. After PCMBS or NEM treatment, addition of dithiothreitol (DTT) restored a large fraction of the MgATP stimulation of the exchange fluxes and almost fully restored PtdIns(4)-5kinase activity; however, in contrast to PCMBS, the effects of NEM did not seem related to the alkylation of protein SH groups. By itself DTT had no effect on the synthesis of PtdIns-4,5P2 but affected MgATP stimulation of NCX1: moderate inhibition at 1mM MgATP and 1µM Ca(2+) and full inhibition at 0.25mM MgATP and 0.2µM Ca(2+). In addition, DDT prevented coimmunoprecipitation of NCX1 and PtdIns(4)-5kinase. These results indicate that, for a proper MgATP up-regulation of NCX1, the enzyme responsible for PtdIns-4,5P2 synthesis must be (i) functionally competent and (ii) set in the NCX1 microenvironment closely associated to the exchanger. This kind of supramolecular structure is needed to optimize binding of the newly synthesized PtdIns-4,5P2 to its target region in the exchanger protein.
Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Name of substance:0 (Enzyme Inhibitors); 0 (Phosphatidylinositol 4,5-Diphosphate); 0 (Sodium-Calcium Exchanger); 0 (sodium-calcium exchanger 1); 5YIN07W42H (4-Chloromercuribenzenesulfonate); 8L70Q75FXE (Adenosine Triphosphate); EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor)); EC 2.7.1.- (phosphatidylinositol 4,5-biphosphate kinase); EC 2.7.1.68 (1-phosphatidylinositol-4-phosphate 5-kinase); T8ID5YZU6Y (Dithiothreitol)



page 1 of 62 go to page                         
   


Refine the search
  Database : MEDLINE Advanced form   

    Search in field  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/PAHO/WHO - Latin American and Caribbean Center on Health Sciences Information