Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 20 de 33
Filtrar
Más filtros











Base de datos
Intervalo de año de publicación
1.
J Clin Neurosci ; 71: 293-295, 2020 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-31548089

RESUMEN

INTRODUCTION: Diffuse midline glioma is a newly WHO defined entity (grade IV) (Louis et al., 2016) which includes diffuse intrinsic pontine glioma (DIPG) reported in pediatric population and, occasionally, in young adults. Here, we present a detailed description of an atypical case of diffuse midline glioma in a 53 years old woman. CASE REPORT: A caucasian woman aged 53 from Ukraine, was referred to another neurological department complaining of 3 months history of progressive postural instability and gait impairment with frequent falling. Magnetic resonance demonstrated two brainstem lesions, hyperintense in FLAIR with "patchy" peripheral enhancement, leptomeningeal and cranial nerves enhancement. CSF was normal. Due to positive antinuclear antibodies test (ANA 1:360), intravenous steroid treatment was administered and reported to initially improve the patient condition. However, the following weeks the lady worsened. Imaging features were unchanged. Because quantiferon test resulted positive, MRI-Spectroscopy showed an inflammatory pattern and MRI perfusion study and brain FDG-PET, were normal, tubercolar granulomatous hypothesis was initially favored. Antitubercular therapy with isoniazid, pyrazinamide, ethambutol and rifampicin was started without any clinical improvement. Hence, the biopsy was proposed. The procedure revealed a diffuse midline pontine glioma. Considering the advanced stage of the disease, radiotherapy was not indicated. Patient died after eight months from the onset of neurological disturbances. CONCLUSION: Our case shows that diffuse midline glioma is a CNS tumor not limited to young population but occurring also in middle aged patients with an insidious pattern. We therefore recommend to perform biopsy at very early stages in patients with atypical brainstem lesions.


Asunto(s)
Neoplasias del Tronco Encefálico/diagnóstico , Neoplasias del Tronco Encefálico/patología , Glioma/diagnóstico , Glioma/patología , Puente/patología , Femenino , Humanos , Persona de Mediana Edad
2.
J Neuroendocrinol ; 20 Suppl 1: 26-34, 2008 May.
Artículo en Inglés | MEDLINE | ID: mdl-18426496

RESUMEN

N-acylethanolamines, which include the endocannabinoid anandamide and the cannabinoid receptor-inactive saturated compounds N-palmitoyl ethanolamine and N-stearoyl ethanolamine, are ethanolamines of long-chain fatty acids degraded by fatty acid amide hydrolase (FAAH) known to accumulate in degenerating tissues and cells. Whilst much evidence supports a protective anti-inflammatory role of both anandamide and N-palmitoyl ethanolamine, very little information is available with regard to the bioactivity of N-stearoyl ethanolamine. Employing a murine model of passive IgE-induced cutaneous anaphylaxis, we have found that N-stearoyl ethanolamine is endowed with marked anti-inflammatory properties in vivo, supporting the hypothesis that endogenous N-stearoyl ethanolamine is, in analogy to N-palmitoyl ethanolamine, a bioactive signalling lipid capable of downregulating allergic inflammation in the skin. This effect, although mimicked by synthetic, non-selective, CB(1)/CB(2) receptor agonists, such as WIN55, 212-2, was not sensitive to CB(1) or CB(2) receptor antagonists, but rather was fully reversed by capsazepine, a competitive antagonist of the TRPV1 receptor. Moreover, CB(1) receptor antagonists, although effective in antagonising the WIN55,212-2-induced hypothermia, did not reduce the anti-inflammatory effect of WIN55,212-2, whilst CB(2) receptor antagonists, per se inactive, potentiated the WIN55,212-2 effect, suggesting an involvement of non-CB(1)/CB(2) receptors in the anti-inflammatory action of WIN55,212-2. All this, together with demonstration of FAAH as a major regulator of the in vivo concentrations of saturated N-stearoyl ethanolamine, in addition to N-palmitoyl ethanolamine, raise the speculation that pharmacological treatments with saturated N-acylethanolamines such as N-stearoyl ethanolamine, or alternatively FAAH inhibitors able to increase their local concentration, rather than selective CB receptor agonists, might be of promising therapeutic benefit in reducing allergic inflammation in the skin.


Asunto(s)
Antiinflamatorios/farmacología , Etanolaminas/farmacología , Inflamación/tratamiento farmacológico , Ácidos Palmíticos/farmacología , Amidas , Animales , Antiinflamatorios/uso terapéutico , Benzoxazinas/farmacología , Temperatura Corporal/efectos de los fármacos , Canfanos/farmacología , Agonistas de Receptores de Cannabinoides , Antagonistas de Receptores de Cannabinoides , Cannabinoides/antagonistas & inhibidores , Cannabinoides/farmacología , Pabellón Auricular/efectos de los fármacos , Pabellón Auricular/patología , Edema/etiología , Edema/patología , Endocannabinoides , Etanolaminas/química , Etanolaminas/uso terapéutico , Ácidos Grasos/farmacología , Ácidos Grasos/uso terapéutico , Femenino , Ratones , Ratones Endogámicos BALB C , Morfolinas/farmacología , Naftalenos/farmacología , Ácidos Palmíticos/química , Ácidos Palmíticos/uso terapéutico , Anafilaxis Cutánea Pasiva/efectos de los fármacos , Anafilaxis Cutánea Pasiva/fisiología , Piperidinas/farmacología , Pirazoles/farmacología , Rimonabant , Ácidos Esteáricos/farmacología , Factores de Tiempo
3.
Phys Rev Lett ; 94(16): 167002, 2005 Apr 29.
Artículo en Inglés | MEDLINE | ID: mdl-15904261

RESUMEN

We study decoherence due to low frequency noise in Josephson qubits. Non-Markovian classical noise due to switching impurities determines inhomogeneous broadening of the signal. The theory is extended to include effects of high-frequency quantum noise, due to impurities or to the electromagnetic environment. The interplay of slow noise with intrinsically non-Gaussian noise sources may explain the rich physics observed in the spectroscopy and in the dynamics of charge based devices.

4.
J Cell Sci ; 114(Pt 12): 2255-63, 2001 Jun.
Artículo en Inglés | MEDLINE | ID: mdl-11493665

RESUMEN

Hrs, an essential tyrosine kinase substrate, has been implicated in intracellular trafficking and signal transduction pathways. The protein contains several distinctive domains, including an N-terminal VHS domain, a phosphatidylinositol 3-phosphate (PtdIns(3)P)-binding FYVE domain and two coiled-coil domains. Here we have investigated the roles of these domains in the subcellular localisation of Hrs. Hrs was found to colocalise extensively with EEA1, an established marker of early endosomes. While the membrane association of EEA1 was abolished in the presence of a dominant negative mutant of the endosomal GTPase Rab5, the localisation of Hrs to early endosomes was Rab5 independent. The VHS-domain was nonessential for the subcellular targeting of Hrs. In contrast, the FYVE domain as well as the second coiled-coil domain, which has been shown to bind to SNAP-25, were required for targeting of Hrs to early endosomes. A small construct consisting of only these two domains was correctly localised to early endosomes, whereas a point mutation (R183A) in the PtdIns(3)P-binding pocket of the FYVE domain inhibited the membrane targeting of Hrs. Thus, like EEA1, the endosomal targeting of Hrs is mediated by a PtdIns(3)P-binding FYVE domain in cooperation with an additional domain. We speculate that binding to PtdIns(3)P and a SNAP-25-related molecule may target Hrs specifically to early endosomes.


Asunto(s)
Endosomas/metabolismo , Fosfoproteínas/química , Fosfoproteínas/metabolismo , Secuencias de Aminoácidos , Sustitución de Aminoácidos , Animales , Línea Celular , Cricetinae , Complejos de Clasificación Endosomal Requeridos para el Transporte , Endosomas/ultraestructura , Humanos , Inositol 1,4,5-Trifosfato/metabolismo , Proteínas de la Membrana/genética , Proteínas de la Membrana/metabolismo , Ratones , Microscopía Confocal , Microscopía Electrónica , Microscopía Fluorescente , Mutación , Proteínas del Tejido Nervioso/metabolismo , Fosfoproteínas/genética , Fosfoproteínas/ultraestructura , Unión Proteica , Estructura Terciaria de Proteína , Transporte de Proteínas , Proteína 25 Asociada a Sinaptosomas , Técnicas del Sistema de Dos Híbridos , Proteínas de Transporte Vesicular , Proteínas de Unión al GTP rab5/genética , Proteínas de Unión al GTP rab5/fisiología
6.
Phys Rev Lett ; 86(4): 600-3, 2001 Jan 22.
Artículo en Inglés | MEDLINE | ID: mdl-11177891

RESUMEN

The two-neutron halo nucleus (14)Be has been investigated in a kinematically complete measurement of the fragments ((12)Be and neutrons) produced in dissociation at 35 MeV/nucleon on C and Pb targets. Two-neutron removal cross sections, neutron angular distributions, and invariant mass spectra were measured, and the contributions from electromagnetic dissociation (EMD) were deduced. Comparison with three-body model calculations suggests that the halo wave function contains a large nu(2s(1/2))(2) admixture. The EMD invariant mass spectrum exhibited enhanced strength near threshold consistent with a nonresonant soft-dipole excitation.

7.
J Biol Chem ; 274(41): 28857-60, 1999 Oct 08.
Artículo en Inglés | MEDLINE | ID: mdl-10506127

RESUMEN

The fusion of transport vesicles with their cognate target membranes, an essential event in intracellular membrane trafficking, is regulated by SNARE proteins and Rab GTPases. Rab GTPases are thought to act prior to SNAREs in vesicle docking, but the exact biochemical relationship between the two classes of molecules is not known. We recently identified the early endosomal autoantigen EEA1 as an effector of Rab5 in endocytic membrane fusion. Here we demonstrate that EEA1 interacts directly and specifically with syntaxin-6, a SNARE implicated in trans-Golgi network to early endosome trafficking. The binding site for syntaxin-6 overlaps with that of Rab5-GTP at the C terminus of EEA1. Syntaxin-6 and EEA1 were found to colocalize extensively on early endosomes, although syntaxin-6 is present in the trans-Golgi network as well. Our results indicate that SNAREs can interact directly with Rab effectors, and suggest that EEA1 may participate in trans-Golgi network to endosome as well as in endocytic membrane traffic.


Asunto(s)
Proteínas de la Membrana/metabolismo , Proteínas de Transporte Vesicular , Proteínas de Unión al GTP rab5/metabolismo , Animales , Línea Celular , Cricetinae , Endocitosis , Endosomas/metabolismo , Técnica del Anticuerpo Fluorescente , Genes Reporteros , Aparato de Golgi/metabolismo , Humanos , Fusión de Membrana , Proteínas de la Membrana/genética , Proteínas Qa-SNARE , Proteínas SNARE , Transfección , Levaduras/genética
8.
Curr Opin Cell Biol ; 11(4): 460-5, 1999 Aug.
Artículo en Inglés | MEDLINE | ID: mdl-10449332

RESUMEN

Phosphoinositides serve as direct local modulators or recruiters of the protein machineries that control membrane trafficking. In the past year, examples of phosphoinositide effectors include regulators of small GTPases in coat assembly, dynamin in clathrin coated vesicle formation and FYVE finger proteins in endocytic membrane traffic. A novel phosphoinositide appears to regulate effectors involved in the formation of multivesicular endosomes.


Asunto(s)
Membrana Celular/metabolismo , Fosfatidilinositoles/metabolismo , Animales , Transporte Biológico , Endocitosis/fisiología , Exocitosis/fisiología
9.
Chem Phys Lipids ; 98(1-2): 87-94, 1999 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-10358931

RESUMEN

Phosphatidylinositol 3-phosphate (PtdIns(3)P), generated via the phosphorylation of phosphatidylinositol by phosphatidylinositol 3-kinase (PI 3-kinase), plays an essential role in intracellular membrane traffic. The underlying mechanism is still not understood in detail, but the recent identification of the FYVE finger as a protein domain that binds specifically to PtdIns(3)P provides a number of potential effectors for PtdIns(3)P. The FYVE finger (named after the first letter of the four proteins containing it; Fab1p, YOTB, Vac1p and EEA1) is a double-zinc binding domain that is conserved in more than 30 proteins from yeast to mammals. It is found in several proteins involved in intracellular traffic, and FYVE finger mutations that affect zinc binding are associated with the loss of function of several of these proteins. The interaction of FYVE fingers with PtdIns(3)P may serve three alternative functions: First, to recruit cytosolic FYVE finger proteins to PtdIns(3)P-containing membranes (in concert with accessory molecules); second, to enrich for membrane bound FYVE finger proteins into PtdIns(3)P containing microdomains within the membrane; and third, to modulate the activity of membrane bound FYVE finger proteins.


Asunto(s)
Fosfatidilinositol 3-Quinasas/metabolismo , Fosfatos de Fosfatidilinositol/metabolismo , Dedos de Zinc , Secuencia de Aminoácidos , Animales , Secuencia de Consenso , Secuencia Conservada , Humanos , Membranas Intracelulares/fisiología , Datos de Secuencia Molecular , Transducción de Señal
11.
Eur J Cell Biol ; 72(2): 95-103, 1997 Feb.
Artículo en Inglés | MEDLINE | ID: mdl-9157016

RESUMEN

The small GTPase Rab5 is an important regulator of membrane fusion in the early endocytic pathway. Here we have studied at the light microscopy level the morphology of early endosomes in MDCK cells stably expressing a GTPase-deficient Rab5 mutant, Rab5 Q79L, N-terminally tagged with a myc-epitope. These cells contain large vacuoles, readily visible by phase-contrast microscopy. Confocal immunofluorescence microscopy showed the presence of the epitopetagged protein on large perinuclear vacuoles, as well as on smaller peripheral structures. A subset of the perinuclear vacuoles appeared to colocalize with the late endosomal GTPase, Rab7. In addition, a population of very large Rab7-positive, Rab5 Q79L-negative structures were observed, suggesting that an increase in the size of early endosomes may be accompanied by an increased size of later or more mature endocytic structures. Using antibodies against the myc epitope and the early endosomal autoantigen EEA1 as markers, we found that endosomes in wild-type and mutant MDCK cells rapidly tubulate in the presence of bafilomycin A1, an inhibitor of vacuolar H(+)-ATPase. Elongated or tubular endosomes partially colocalized with microtubules and were redistributed upon preincubation with the microtubule depolymerizing agent nocodazole before bafilomycin A1 treatment. Treatment of the Rab5 Q79L expressing cells with nocodazole alone led to a spatial redistribution and a significant decrease in the size of EEA1-positive structures, whereas their number increased. These results implicate microtubules in the bafilomycin A1-induced tubulation of endosomes as well as in the vacuolation of endosomes caused by Rab5 Q79L.


Asunto(s)
Antibacterianos/farmacología , Endosomas/efectos de los fármacos , Inhibidores Enzimáticos/farmacología , Proteínas de Unión al GTP/metabolismo , Macrólidos , Microtúbulos/efectos de los fármacos , ATPasas de Translocación de Protón/antagonistas & inhibidores , Animales , Línea Celular , Perros , Endocitosis/efectos de los fármacos , Endosomas/metabolismo , Endosomas/ultraestructura , Técnica del Anticuerpo Fluorescente Indirecta , Proteínas de Unión al GTP/genética , Microtúbulos/metabolismo , Microtúbulos/ultraestructura , Mutación Puntual , Ricina/farmacocinética , Vacuolas/efectos de los fármacos , Vacuolas/metabolismo , Vacuolas/ultraestructura , Proteínas de Unión al GTP rab5
12.
J Biol Chem ; 271(39): 24048-54, 1996 Sep 27.
Artículo en Inglés | MEDLINE | ID: mdl-8798641

RESUMEN

EEA1, a 162-kDa autoantigen associated with subacute cutaneous systemic lupus erythematosus, is a coiled-coil protein localized to early endosomes and cytosol. At its C terminus, the protein contains a cysteine-rich motif, which is shared with Vps27, Fab1, and Vac1, yeast proteins implicated in membrane traffic (Mu, F. T., Callaghan, J. M., Steele-Mortimer, O., Stenmark, H., Parton, R. G., Campbell, P. L., McCluskey, J., Yeo, J. P., Tock, E. P., and Toh, B. H. (1995) J. Biol. Chem. 270, 13503-13511). Here we show that this motif constitutes a genuine zinc binding domain, which we term the FYVE finger (based on the first letters of four proteins containing this motif). Profile-based data base searches identified the FYVE finger in 11 distinct proteins. The FYVE finger-containing C terminus of EEA1 was found to bind 2 mol equivalents of Zn2+. Mutations of conserved histidine and cysteine residues in the FYVE motif independently reduced zinc binding to 1 mol equivalent. Confocal immunofluorescence microscopy of transfected HEp2 cells revealed that the C-terminal part (residues 1277-1411) of EEA1 colocalizes extensively with a GTPase-deficient mutant of the early endosomal GTPase Rab5, while deletion of the FYVE finger or mutations that interfere with zinc binding cause a cytosolic localization. These results implicate the FYVE finger in the specific localization of EEA1 to endosomes.


Asunto(s)
Autoantígenos/metabolismo , Compartimento Celular , Endosomas/metabolismo , Proteínas de la Membrana/metabolismo , Dedos de Zinc , Zinc/metabolismo , Secuencia de Aminoácidos , Autoantígenos/química , Línea Celular , Técnica del Anticuerpo Fluorescente Indirecta , Humanos , Lupus Eritematoso Sistémico , Proteínas de la Membrana/química , Microscopía Confocal , Datos de Secuencia Molecular , Alineación de Secuencia , Proteínas de Transporte Vesicular
13.
FEBS Lett ; 370(1-2): 69-74, 1995 Aug 14.
Artículo en Inglés | MEDLINE | ID: mdl-7649306

RESUMEN

Two isoforms of mammalian cytochrome b5, which have homologous cytosolic amino-terminal catalytic domains, are located one on endoplasmic reticulum (ER b5) the other on mitochondrial outer membranes (OM b5). A cDNA coding for the previously unknown carboxyl-terminal domain of OM b5 was cloned and a chimera between the catalytic domain of ER b5 and the carboxyl-terminal region of OM b5 was expressed in cultured mammalian cells. The chimera localized to mitochondria, indicating that the carboxyl-terminal 43 amino acids of OM b5 contain sufficient information to target the catalytic domain of ER b5 to the mitochondrial outer membrane.


Asunto(s)
Citocromos b5/química , Citocromos b5/metabolismo , Membranas Intracelulares/metabolismo , Mitocondrias/metabolismo , Secuencia de Aminoácidos , Animales , Secuencia de Bases , Sitios de Unión , Línea Celular , Chlorocebus aethiops , Clonación Molecular , Citocromos b5/biosíntesis , Cartilla de ADN , Retículo Endoplásmico/metabolismo , Riñón , Hígado/metabolismo , Mamíferos , Datos de Secuencia Molecular , Reacción en Cadena de la Polimerasa , Ratas , Proteínas Recombinantes de Fusión/biosíntesis , Proteínas Recombinantes de Fusión/química , Proteínas Recombinantes de Fusión/metabolismo , Homología de Secuencia de Aminoácido , Transfección
14.
Science ; 268(5219): 1915-7, 1995 Jun 30.
Artículo en Inglés | MEDLINE | ID: mdl-7604266

RESUMEN

The molecular defects responsible for tumor cell hypermutability in humans have not yet been fully identified. Here the gene encoding a G/T mismatch-binding protein (GTBP) was localized to within 1 megabase of the related hMSH2 gene on chromosome 2 and was found to be inactivated in three hypermutable cell lines. Unlike cells defective in other mismatch repair genes, which display widespread alterations in mononucleotide, dinucleotide, and other simple repeated sequences, the GTBP-deficient cells showed alterations primarily in mononucleotide tracts. These results suggest that GTBP is important for maintaining the integrity of the human genome and document molecular defects accounting for variation in mutator phenotype.


Asunto(s)
Neoplasias Colorrectales/genética , Reparación del ADN/genética , ADN de Neoplasias/genética , Proteínas de Unión al ADN/genética , Mutación del Sistema de Lectura , Secuencia de Bases , Mapeo Cromosómico , Cromosomas Humanos Par 2 , Codón , Neoplasias Colorrectales Hereditarias sin Poliposis/genética , ADN Satélite/genética , Marcadores Genéticos , Mutación de Línea Germinal , Humanos , Datos de Secuencia Molecular , Células Tumorales Cultivadas
15.
Science ; 268(5219): 1912-4, 1995 Jun 30.
Artículo en Inglés | MEDLINE | ID: mdl-7604265

RESUMEN

DNA mismatch recognition and binding in human cells has been thought to be mediated by the hMSH2 protein. Here it is shown that the mismatch-binding factor consists of two distinct proteins, the 100-kilodalton hMSH2 and a 160-kilodalton polypeptide, GTBP (for G/T binding protein). Sequence analysis identified GTBP as a new member of the MutS homolog family. Both proteins are required for mismatch-specific binding, a result consistent with the finding that tumor-derived cell lines devoid of either protein are also devoid of mismatch-binding activity.


Asunto(s)
Reparación del ADN , ADN de Neoplasias/metabolismo , Proteínas de Unión al ADN/metabolismo , Ácidos Nucleicos Heterodúplex/metabolismo , Secuencia de Aminoácidos , Composición de Base , Secuencia de Bases , Clonación Molecular , Neoplasias Colorrectales , Reparación del ADN/genética , Proteínas de Unión al ADN/química , Proteínas de Unión al ADN/genética , Células HeLa , Humanos , Datos de Secuencia Molecular , Peso Molecular , Análisis de Secuencia , Células Tumorales Cultivadas
17.
FEBS Lett ; 325(1-2): 70-5, 1993 Jun 28.
Artículo en Inglés | MEDLINE | ID: mdl-8513896

RESUMEN

Cytochrome b5 and NADH-cytochrome b5 reductase are integral membrane proteins with cytosolic active domains and short membrane anchors, which are inserted post-translationally into their target membranes. Both are produced as different isoforms, with different localizations, in mammalian cells. In the rat, the reductase gene generates two transcripts by an alternative promoter mechanism: a ubiquitous mRNA coding for the myristylated membrane-bound form, and an erythroid mRNA which generates both the soluble form and a nonmyristylated membrane-binding form. The available evidence indicates that the ubiquitous myristylated form binds to the cytosolic face of both outer mitochondrial membranes and ER. In contrast, two genes code for two homologous forms of cytochrome b5, one of which is found on outer mitochondrial membranes, the other on the ER. The gene specifying the ER form probably also generates an erythroid-specific mRNA by alternative splicing, which codes for soluble cytochrome b5. Possible molecular mechanisms responsible for the observed localizations of these different enzyme isoforms are discussed.


Asunto(s)
Reductasas del Citocromo/metabolismo , Citocromos b5/metabolismo , Retículo Endoplásmico/metabolismo , Procesamiento Proteico-Postraduccional , Animales , Reductasas del Citocromo/genética , Citocromo-B(5) Reductasa , Citocromos b5/genética , Membranas Intracelulares/metabolismo , ARN Mensajero/metabolismo
18.
J Biol Chem ; 268(4): 2802-8, 1993 Feb 05.
Artículo en Inglés | MEDLINE | ID: mdl-8428954

RESUMEN

Two forms of cytochrome b5 are present in rat tissues, with a sequence identity of approximately 60% in the cytoplasmically exposed, tryptic fragments (Lederer, F., Ghrir, R., Guiard, B., Cortial, S., and Ito, A. (1983) Eur. J. Biochem. 132, 95-102). It has been suggested that the two isoforms have partially overlapping subcellular distributions, with each form localized to some extent on both endoplasmic reticulum and outer mitochondrial membranes (Ito, A. (1980) J. Biochem. (Tokyo) 87, 73-80). To investigate the degree of specificity of the localization of cytochrome b5 isoforms, we studied their subcellular distributions with antipeptide antibodies, one specific for microsomal cytochrome b5, one specific for outer membrane cytochrome b, and one against a sequence common to the two cytochromes. We first identified outer membrane Cyt b as a tightly bound, Triton X-114-extractable, 23-kDa polypeptide. We then analyzed biochemically characterized rat liver subcellular fractions by Western blotting and found that outer mitochondrial membrane cytochrome b was not present on endoplasmic reticulum membranes. Conversely, microsomal cytochrome b5 was present on outer mitochondrial membranes in extremely low concentration, at a level < 5% of that on endoplasmic reticulum membranes. Thus, the subcellular distribution of microsomal cytochrome b5 is more restricted than previously thought, suggesting that novel posttranslational targeting mechanisms direct it to the endoplasmic reticulum.


Asunto(s)
Citocromos b5/metabolismo , Secuencia de Aminoácidos , Animales , Compartimento Celular , Citocromos b5/inmunología , Isoenzimas/metabolismo , Masculino , Proteínas de la Membrana/inmunología , Proteínas de la Membrana/metabolismo , Microsomas Hepáticos/enzimología , Mitocondrias Hepáticas/enzimología , Datos de Secuencia Molecular , Peso Molecular , Fragmentos de Péptidos/inmunología , Ratas , Ratas Sprague-Dawley , Alineación de Secuencia
20.
Phys Rev C Nucl Phys ; 46(4): 1437-1444, 1992 Oct.
Artículo en Inglés | MEDLINE | ID: mdl-9968252
SELECCIÓN DE REFERENCIAS
DETALLE DE LA BÚSQUEDA