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Pesquisa : D03.383.679.149 [Categoria DeCS]
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PMID:27771997
Autor:Fan J; Guo M; Im CS; Pi-Anfruns J; Cui ZK; Kim S; Wu BM; Aghaloo TL; Lee M
Endereço:1 Division of Advanced Prosthodontics, School of Dentistry, University of California , Los Angeles, Los Angeles, California.
Título:Enhanced Mandibular Bone Repair by Combined Treatment of Bone Morphogenetic Protein 2 and Small-Molecule Phenamil.
Fonte:Tissue Eng Part A; 23(5-6):195-207, 2017 03.
ISSN:1937-335X
País de publicação:United States
Idioma:eng
Resumo:Growth factor-based therapeutics using bone morphogenetic protein 2 (BMP-2) presents a promising strategy to reconstruct craniofacial bone defects such as mandible. However, clinical applications require supraphysiological BMP doses that often increase inappropriate adipogenesis, resulting in well-documented, cyst-like bone formation. Here we reported a novel complementary strategy to enhance osteogenesis and mandibular bone repair by using small-molecule phenamil that has been shown to be a strong activator of BMP signaling. Phenamil synergistically induced osteogenic differentiation of human bone marrow mesenchymal stem cells with BMP-2 while suppressing their adipogenic differentiation induced by BMP-2 in vitro. The observed pro-osteogenic and antiadipogenic activity of phenamil was mediated by expression of tribbles homolog 3 (Trb3) that enhanced BMP-smad signaling and inhibited expression of peroxisome proliferator-activated receptor gamma (PPARγ), a master regulator of adipogenesis. The synergistic effect of BMP-2+phenamil on bone regeneration was further confirmed in a critical-sized rat mandibular bone defect by implanting polymer scaffolds designed to slowly release the therapeutic molecules. These findings indicate a new complementary osteoinductive strategy to improve clinical efficacy and safety of current BMP-based therapeutics.
Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
Nome de substância:0 (Bmp2 protein, rat); 0 (Bone Morphogenetic Protein 2); 0 (Drug Implants); 2038-35-9 (phenylamil); 7DZO8EB0Z3 (Amiloride)


  2 / 7289 MEDLINE  
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PMID:28468944
Autor:Montgomery DS; Yu L; Ghazi ZM; Thai TL; Al-Khalili O; Ma HP; Eaton DC; Alli AA
Endereço:Department of Physiology and Functional Genomics and Department of Medicine Division of Nephrology, Hypertension, and Renal Transplantation, University of Florida College of Medicine, Gainesville, Florida.
Título:ENaC activity is regulated by calpain-2 proteolysis of MARCKS proteins.
Fonte:Am J Physiol Cell Physiol; 313(1):C42-C53, 2017 Jul 01.
ISSN:1522-1563
País de publicação:United States
Idioma:eng
Resumo:We previously demonstrated a role for the myristoylated alanine-rich C kinase substrate (MARCKS) to serve as an adaptor protein in the anionic phospholipid phosphate-dependent regulation of the epithelial sodium channel (ENaC). Both MARCKS and ENaC are regulated by proteolysis. Calpains are a family of ubiquitously expressed intracellular Ca -dependent cysteine proteases involved in signal transduction. Here we examine the role of calpain-2 in regulating MARCKS and ENaC in cultured renal epithelial cells and in the mouse kidney. Using recombinant fusion proteins, we show that MARCKS, but not the ENaC subunits, are a substrate of calpain-2 in the presence of Ca Pharmacological inhibition of calpain-2 alters MARCKS protein expression in light-density sucrose gradient fractions from cell lysates of mouse cortical collecting duct cells. Calpain-dependent cleaved products of MARCKS are detectable in cultured renal cells. Ca mobilization and calpain-2 inhibition decrease the association between ENaC and MARCKS. The inhibition of calpain-2 reduces ENaC activity as demonstrated by single-channel patch-clamp recordings and transepithelial current measurements. These results suggest that calpain-2 proteolysis of MARCKS promotes its interaction with lipids and ENaC at the plasma membrane to allow for the phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent regulation of ENaC activity in the kidney.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Cysteine Proteinase Inhibitors); 0 (Epithelial Sodium Channels); 0 (Intracellular Signaling Peptides and Proteins); 0 (Marcks protein, mouse); 0 (Membrane Proteins); 0 (Phosphatidylinositol 4,5-Diphosphate); 0 (Recombinant Fusion Proteins); 125267-21-2 (Myristoylated Alanine-Rich C Kinase Substrate); 22144-77-0 (Cytochalasin D); 7DZO8EB0Z3 (Amiloride); EC 3.4.22.- (Calpain); EC 3.4.22.53 (Capn2 protein, mouse); SY7Q814VUP (Calcium)


  3 / 7289 MEDLINE  
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PMID:28678485
Autor:Sun L; Li B; Su X; Chen G; Li Y; Yu L; Li L; Wei W
Endereço:Shanghai Advanced Research Institute, Chinese Academy of Sciences, and University of Chinese Academy of Sciences, 99 Haike Road, Shanghai, 201210, China.
Título:An Ursolic Acid Derived Small Molecule Triggers Cancer Cell Death through Hyperstimulation of Macropinocytosis.
Fonte:J Med Chem; 60(15):6638-6648, 2017 Aug 10.
ISSN:1520-4804
País de publicação:United States
Idioma:eng
Resumo:Macropinocytosis is a transient endocytosis that internalizes extracellular fluid and particles into vacuoles. Recent studies suggest that hyperstimulation of macropinocytosis can induce a novel nonapoptotic cell death, methuosis. In this report, we describe the identification of an ursolic acid derived small molecule (compound 17), which induces cancer cell death through hyperstimulation of macropinocytosis. 17 causes the accumulation of vacuoles derived from macropinosomes based on transmission electron microscopy, time-lapse microscopy, and labeling with extracellular fluid phase tracers. The vacuoles induced by 17 separate from other cytoplasmic compartments but acquire some characteristics of late endosomes and lysosomes. Inhibiting hyperstimulation of macropinocytosis with the specific inhibitor amiloride blocks cell death, implicating that 17 leads to cell death via macropinocytosis, which is coincident with methuosis. Our results uncovered a novel cell death pathway involved in the activity of 17, which may provide a basis for further development of natural-product-derived scaffolds for drugs that trigger cancer cell death by methuosis.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (10-(4-cyanophenyl)-1,2,6a,6b,9,9,13a-heptamethyl-1,2,3,4,5,6,6a,6b,7,8,8a,9,10,13,13a,3b,14,15b-octadecahydro-4aH-chryseno(1,2-f)indazole-4a-carboxylic acid); 0 (Amines); 0 (Amino Acid Chloromethyl Ketones); 0 (Antineoplastic Agents); 0 (Fluorescent Dyes); 0 (Indazoles); 0 (Isoquinolines); 0 (Red DND-99); 0 (Triterpenes); 0 (benzyloxycarbonylvalyl-alanyl-aspartyl fluoromethyl ketone); 7DZO8EB0Z3 (Amiloride); 9654F8OVKE (lucifer yellow); P3M2575F3F (ursolic acid)


  4 / 7289 MEDLINE  
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PMID:28430823
Autor:Chang WH; Niu DM; Lu CY; Lin SY; Liu TC; Chang JG
Endereço:Department of Primary Care Medicine, Taipei Medical University Hospital, Taipei, Taiwan.
Título:Modulation the alternative splicing of GLA (IVS4+919G>A) in Fabry disease.
Fonte:PLoS One; 12(4):e0175929, 2017.
ISSN:1932-6203
País de publicação:United States
Idioma:eng
Resumo:While a base substitution in intron 4 of GLA (IVS4+919G>A) that causes aberrant alternative splicing resulting in Fabry disease has been reported, its molecular mechanism remains unclear. Here we reported that upon IVS4+919G>A transversion, H3K36me3 was enriched across the alternatively spliced region. PSIP1, an adapter of H3K36me3, together with Hsp70 and NONO were recruited and formed a complex with SF2/ASF and SRp20, which further promoted GLA splicing. Amiloride, a splicing regulator in cancer cells, could reverse aberrant histone modification patterns and disrupt the association of splicing complex with GLA. It could also reverse aberrant GLA splicing in a PP1-dependant manner. Our findings revealed the alternative splicing mechanism of GLA (IVS4+919G>A), and a potential treatment for this specific genetic type of Fabry disease by amiloride in the future.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Histones); 0 (RNA, Messenger); 7DZO8EB0Z3 (Amiloride); EC 3.2.1.22 (alpha-Galactosidase)


  5 / 7289 MEDLINE  
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PMID:28356292
Autor:Frindt G; Yang L; Uchida S; Weinstein AM; Palmer LG
Endereço:Department of Physiology and Biophysics, Weill-Cornell Medical College, New York, New York.
Título:Responses of distal nephron Na transporters to acute volume depletion and hyperkalemia.
Fonte:Am J Physiol Renal Physiol; 313(1):F62-F73, 2017 Jul 01.
ISSN:1522-1466
País de publicação:United States
Idioma:eng
Resumo:We assessed effects of acute volume reductions induced by administration of diuretics in rats. Direct block of Na transport produced changes in urinary electrolyte excretion. Adaptations to these effects appeared as alterations in the expression of protein for the distal nephron Na transporters NCC and ENaC. Two hours after a single injection of furosemide (6 mg/kg) or hydrochlorothiazide (HCTZ; 30 mg/kg) Na and K excretion increased but no changes in the content of activated forms of NCC (phosphorylated on residue T53) or ENaC (cleaved γ-subunit) were detected. In contrast, amiloride (0.6 mg/kg) evoked a similar natriuresis that coincided with decreased pT53NCC and increased cleaved γENaC. Alterations in posttranslational membrane protein processing correlated with an increase in plasma K of 0.6-0.8 mM. Decreased pT53NCC occurred within 1 h after amiloride injection, whereas changes in γENaC were slower and were blocked by the mineralocorticoid receptor antagonist spironolactone. Increased γENaC cleavage correlated with elevation of the surface expression of the subunit as assessed by in situ biotinylation. Na depletion induced by 2 h of furosemide or HCTZ treatment increases total NCC expression without affecting ENaC protein. However, restriction of Na intake for 10 h (during the day) or 18 h (overnight) increased the abundance of both total NCC and of cleaved α- and γENaC. We conclude that the kidneys respond acutely to hyperkalemic challenges by decreasing the activity of NCC while increasing that of ENaC. They respond to hypovolemia more slowly, increasing Na reabsorptive capacities of both of these transporters.
Tipo de publicação: COMPARATIVE STUDY; JOURNAL ARTICLE
Nome de substância:0 (Diuretics); 0 (Epithelial Sodium Channels); 0 (Scnn1g protein, rat); 0 (Slc12a3 protein, rat); 0 (Solute Carrier Family 12, Member 3); 0J48LPH2TH (Hydrochlorothiazide); 27O7W4T232 (Spironolactone); 7DZO8EB0Z3 (Amiloride); 7LXU5N7ZO5 (Furosemide); 9NEZ333N27 (Sodium); RWP5GA015D (Potassium)


  6 / 7289 MEDLINE  
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PMID:28348078
Autor:Lin S; Voyton C; Morris MT; Ackroyd PC; Morris JC; Christensen KA
Endereço:From the Departments of Chemistry and.
Título:pH regulation in glycosomes of procyclic form .
Fonte:J Biol Chem; 292(19):7795-7805, 2017 May 12.
ISSN:1083-351X
País de publicação:United States
Idioma:eng
Resumo:Here we report the use of a fluorescein-tagged peroxisomal targeting sequence peptide (F-PTS1, acetyl-C{K(FITC)}GGAKL) for investigating pH regulation of glycosomes in live procyclic form When added to cells, this fluorescent peptide is internalized within vesicular structures, including glycosomes, and can be visualized after 30-60 min. Using F-PTS1 we are able to observe the pH conditions inside glycosomes in response to starvation conditions. Previous studies have shown that in the absence of glucose, the glycosome exhibits mild acidification from pH 7.4 ± 0.2 to 6.8 ± 0.2. Our results suggest that this response occurs under proline starvation as well. This pH regulation is found to be independent from cytosolic pH and requires a source of Na ions. Glycosomes were also observed to be more resistant to external pH changes than the cytosol; placement of cells in acidic buffers (pH 5) reduced the pH of the cytosol by 0.8 ± 0.1 pH units, whereas glycosomal pH decreases by 0.5 ± 0.1 pH units. This observation suggests that regulation of glycosomal pH is different and independent from cytosolic pH regulation. Furthermore, pH regulation is likely to work by an active process, because cells depleted of ATP with 2-deoxyglucose and sodium azide were unable to properly regulate pH. Finally, inhibitor studies with bafilomycin and EIPA suggest that both V-ATPases and Na /H exchangers are required for glycosomal pH regulation.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Macrolides); 0 (Protozoan Proteins); 116764-51-3 (bafilomycin A); 7DZO8EB0Z3 (Amiloride); 8L70Q75FXE (Adenosine Triphosphate); 968JJ8C9DV (Sodium Azide); 9DLQ4CIU6V (Proline); 9G2MP84A8W (Deoxyglucose); IY9XDZ35W2 (Glucose); KOO5CM684H (Digitonin); RWP5GA015D (Potassium); VW50CE070T (ethylisopropylamiloride)


  7 / 7289 MEDLINE  
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PMID:28334404
Autor:Bigiani A
Endereço:Dipartimento di Scienze Biomediche, Metaboliche e Neuroscienze, Università di Modena e Reggio Emilia, Via G. Campi 287, 41125 Modena, Italy.
Título:Calcium Homeostasis Modulator 1-Like Currents in Rat Fungiform Taste Cells Expressing Amiloride-Sensitive Sodium Currents.
Fonte:Chem Senses; 42(4):343-359, 2017 May 01.
ISSN:1464-3553
País de publicação:England
Idioma:eng
Resumo:Salt reception by taste cells is still the less understood transduction process occurring in taste buds, the peripheral sensory organs for the detection of food chemicals. Although there is evidence suggesting that the epithelial sodium channel (ENaC) works as sodium receptor, yet it is not clear how salt-detecting cells signal the relevant information to nerve endings. Taste cells responding to sweet, bitter, and umami substances release ATP as neurotransmitter through a nonvesicular mechanism. Three different channel proteins have been proposed as conduit for ATP secretion: pannexin channels, connexin hemichannels, and calcium homeostasis modulator 1 (CALHM1) channels. In heterologous expression systems, these channels mediate outwardly rectifying membrane currents with distinct biophysical and pharmacological properties. I therefore tested whether also salt-detecting taste cells were endowed with these currents. To this aim, I applied the patch-clamp techniques to single cells in isolated taste buds from rat fungiform papillae. Salt-detecting cells were functionally identified by exploiting the effect of amiloride, which induces a current response by shutting down ENaCs. I looked for the presence of outwardly rectifying currents by using appropriate voltage-clamp protocols and specific pharmacological tools. I found that indeed salt-detecting cells possessed these currents with properties consistent with the presence, at least in part, of CALHM1 channels. Unexpectedly, CALHM1-like currents in taste cells were potentiated by known blockers of pannexin, suggesting a possible inhibitory action of this protein on CALMH1. These findings indicate that communication between salt-detecting cells and nerve endings might involve ATP release by CALMH1 channels.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (CALHM1 protein, rat); 0 (Calcium Channels); 0 (Epithelial Sodium Channel Blockers); 0 (Sodium Channels); 451W47IQ8X (Sodium Chloride); 7DZO8EB0Z3 (Amiloride)


  8 / 7289 MEDLINE  
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PMID:28250131
Autor:Delpeut S; Sisson G; Black KM; Richardson CD
Endereço:Department of Microbiology and Immunology, Dalhousie University, Halifax, Nova Scotia, Canada.
Título:Measles Virus Enters Breast and Colon Cancer Cell Lines through a PVRL4-Mediated Macropinocytosis Pathway.
Fonte:J Virol; 91(10), 2017 May 15.
ISSN:1098-5514
País de publicação:United States
Idioma:eng
Resumo:Measles virus (MeV) is a member of the family that causes a highly contagious respiratory disease but has emerged as a promising oncolytic platform. Previous studies of MeV entry focused on the identification of cellular receptors. However, the endocytic and trafficking pathways utilized during MeV entry remain poorly described. The contribution of each endocytic pathway has been examined in cells that express the MeV receptors SLAM (signaling lymphocyte-activating molecule) and PVRL4 (poliovirus receptor-like 4) (nectin-4). Recombinant MeVs expressing either firefly luciferase or green fluorescent protein together with a variety of inhibitors were used. The results showed that MeV uptake was dynamin independent in the Vero.hPVRL4, Vero.hSLAM, and PVRL4-positive MCF7 breast cancer cell lines. However, MeV infection was blocked by 5-( -ethyl- -propyl)amiloride (EIPA), the hallmark inhibitor of macropinocytosis, as well as inhibitors of actin polymerization. By using phalloidin staining, MeV entry was shown to induce actin rearrangements and the formation of membrane ruffles accompanied by transient elevated fluid uptake. Small interfering RNA (siRNA) knockdown of p21-activated kinase 1 (PAK1) demonstrated that MeV enters both Vero.hPVRL4 and Vero.hSLAM cells in a PAK1-independent manner using a macropinocytosis-like pathway. In contrast, MeV entry into MCF7 human breast cancer cells relied upon Rac1 and its effector PAK1 through a PVRL4-mediated macropinocytosis pathway. MeV entry into DLD-1 colon and HTB-20 breast cancer cells also appeared to use the same pathway. Overall, these findings provide new insight into the life cycle of MeV, which could lead to therapies that block virus entry or methods that improve the uptake of MeV by cancer cells during oncolytic therapy. In the past decades, measles virus (MeV) has emerged as a promising oncolytic platform. Previous studies concerning MeV entry focused mainly on the identification of putative receptors for MeV. Nectin-4 (PVRL4) was recently identified as the epithelial cell receptor for MeV. However, the specific endocytic and trafficking pathways utilized during MeV infections are poorly documented. In this study, we demonstrated that MeV enters host cells via a dynamin-independent and actin-dependent endocytic pathway. Moreover, we show that MeV gains entry into MCF7, DLD-1, and HTB-20 cancer cells through a PVRL4-mediated macropinocytosis pathway and identified the typical cellular GTPase and kinase involved. Our findings provide new insight into the life cycle of MeV, which may lead to the development of therapies that block the entry of the virus into the host cell or alternatively promote the uptake of oncolytic MeV into cancer cells.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Actins); 0 (Cell Adhesion Molecules); 0 (LNIR protein, human); 0 (RNA, Small Interfering); 7DZO8EB0Z3 (Amiloride); EC 2.7.11.1 (PAK1 protein, human); EC 2.7.11.1 (p21-Activated Kinases); VW50CE070T (ethylisopropylamiloride)


  9 / 7289 MEDLINE  
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PMID:28152000
Autor:Tang L; Fang X; Winesett SP; Cheng CY; Binder HJ; Rivkees SA; Cheng SX
Endereço:Department of Pediatrics, University of Florida, Gainesville, FL, United States of America.
Título:Bumetanide increases Cl--dependent short-circuit current in late distal colon: Evidence for the presence of active electrogenic Cl- absorption.
Fonte:PLoS One; 12(2):e0171045, 2017.
ISSN:1932-6203
País de publicação:United States
Idioma:eng
Resumo:Mammalian colonic epithelia consist of cells that are capable of both absorbing and secreting Cl-. The present studies employing Ussing chamber technique identified two opposing short-circuit current (Isc) responses to basolateral bumetanide in rat distal colon. Apart from the transepithelial Cl--secretory Isc in early distal colon that was inhibited by bumetanide, bumetanide also stimulated Isc in late distal colon that had not previously been identified. Since bumetanide inhibits basolateral Na+-K+-2Cl- cotransporter (NKCC) in crypt cells and basolateral K+-Cl- cotransporter (KCC) in surface epithelium, we proposed this stimulatory Isc could represent a KCC-mediated Cl- absorptive current. In support of this hypothesis, ion substitution experiments established Cl- dependency of this absorptive Isc and transport inhibitor studies demonstrated the involvement of an apical Cl- conductance. Current distribution and RNA sequencing analyses revealed that this Cl- absorptive Isc is closely associated with epithelial Na+ channel (ENaC) but is not dependent on ENaC activity. Thus, inhibition of ENaC by 10 µM amiloride or benzamil neither altered the direction nor its activity. Physiological studies suggested that this Cl- absorptive Isc senses dietary Cl- content; thus when dietary Cl- was low, Cl- absorptive Isc was up-regulated. In contrast, when dietary Cl- was increased, Cl- absorptive Isc was down-regulated. We conclude that an active Cl- extrusion mechanism exists in ENaC-expressing late distal colon and likely operates in parallel with ENaC to facilitate NaCl absorption.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Chlorides); 0 (Epithelial Sodium Channel Blockers); 0 (Epithelial Sodium Channels); 04659UUJ94 (benzamil); 0Y2S3XUQ5H (Bumetanide); 24GP945V5T (Barium); 7DZO8EB0Z3 (Amiloride); 9NEZ333N27 (Sodium); SX6K58TVWC (Glyburide)


  10 / 7289 MEDLINE  
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PMID:28107195
Autor:Zhu BY; Shang BY; Du Y; Li Y; Li L; Xu XD; Zhen YS
Endereço:Institute of Medicinal Biotechnology, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing 100050, China.
Título:A new HDAC inhibitor cinnamoylphenazine shows antitumor activity in association with intensive macropinocytosis.
Fonte:Oncotarget; 8(9):14748-14758, 2017 Feb 28.
ISSN:1949-2553
País de publicação:United States
Idioma:eng
Resumo:Previous studies have shown that intensive macropinocytosis occurs in cancer cells and neutral red (NR) is noted for its capability to enter into the cell massively through a process mimetic to macropinocytosis. In addition, trans-cinnamic acid (tCA) has been found to be an inhibitor of histone deacetylase (HDAC). In the present study, cinnamoylphenazine (CA-PZ) that consists of NR and tCA moieties was synthesized and evaluated. As shown, CA-PZ massively entered into colon carcinoma HT-29 cells and pancreatic carcinoma MIA PaCa-2 cells and this entry was blocked by 5-(N-ethyl-N-isopropyl) amiloride (EIPA, an inhibitor of macropinocytosis), indicating a macropinocytosis-mediated uptake. Furthermore, CA-PZ markedly increased the protein expression levels of acetyl-H3, acetyl-H4 and p21 in HT-29 cells and MIA PaCa-2 cells. CA-PZ significantly inhibited the growth of colon carcinoma HT-29 and pancreatic carcinoma MIA PaCa-2 xenografts. By in vivo imaging, CA-PZ displayed prominent accumulation in the tumor xenografts. The study indicates that the newly synthesized CA-PZ acts as an HDAC inhibitor in association with intensive macropinocytosis-mediated intracellular delivery in cancer cells. The use of neutral red for preparation of chimeric molecules with the attribute of macropinocytosis-mediated intracellular delivery might open an alternative way for development of HDAC inhibitors.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Cinnamates); 0 (Epithelial Sodium Channel Blockers); 0 (Histone Deacetylase Inhibitors); 0 (Phenazines); 0 (cinnamoylphenazine); 7DZO8EB0Z3 (Amiloride); VW50CE070T (ethylisopropylamiloride)



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