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1.
Semin Ultrasound CT MR ; 33(1): 65-77, 2012 Feb.
Artículo en Inglés | MEDLINE | ID: mdl-22264904

RESUMEN

The placenta functions to nourish and protect the fetus. Imaging of the placenta can have a profound impact on patient management, owing to the morbidity and mortality associated with various placental conditions. To fully appreciate placental pathology, its physiology, anatomy, and variant anatomy will be outlined. Placental conditions affecting the mother and fetus include molar pregnancies, placental hematoma, abruption, previa, accreta, vasa previa, choriocarcinoma, and retained products of conception. Ultrasonography remains the definitive modality in diagnosing most of these conditions, with magnetic resonance imaging remaining an adjunctive measure. Computed tomography is occasionally used in cases of trauma and tumor staging.


Asunto(s)
Enfermedades Placentarias/diagnóstico , Complicaciones del Embarazo/diagnóstico , Diagnóstico Prenatal/métodos , Tomografía Computarizada por Rayos X/métodos , Ultrasonografía/métodos , Femenino , Humanos , Embarazo , Estadística como Asunto
2.
J Bacteriol ; 185(7): 2354-61, 2003 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-12644507

RESUMEN

We have investigated the conditions required for polar localization of the CheZ phosphatase by using a CheZ-green fluorescent protein fusion protein that, when expressed from a single gene in the chromosome, restored chemotaxis to a DeltacheZ strain. Localization was observed in wild-type, DeltacheZ, DeltacheYZ, and DeltacheRB cells but not in cells with cheA, cheW, or all chemoreceptor genes except aer deleted. Cells making only CheA-short (CheA(S)) or CheA lacking the P2 domain also retained normal localization, whereas cells producing only CheA-long or CheA missing the P1 and P2 domains did not. We conclude that CheZ localization requires the truncated C-terminal portion of the P1 domain present in CheA(S). Missense mutations targeting residues 83 through 120 of CheZ also abolished localization. Two of these mutations do not disrupt chemotaxis, indicating that they specifically prevent interaction with CheA(S) while leaving other activities of CheZ intact.


Asunto(s)
Proteínas Bacterianas/metabolismo , Células Quimiorreceptoras/metabolismo , Proteínas Quinasas/metabolismo , Secuencia de Aminoácidos , Proteínas Bacterianas/química , Proteínas Bacterianas/genética , Quimiotaxis/genética , Secuencia Conservada , Enterobacteriaceae/metabolismo , Proteínas Fluorescentes Verdes , Interacciones Hidrofóbicas e Hidrofílicas , Proteínas Luminiscentes/genética , Proteínas Luminiscentes/metabolismo , Modelos Moleculares , Datos de Secuencia Molecular , Mutación , Conformación Proteica , Proteínas Quinasas/química , Proteínas Quinasas/genética , Estructura Terciaria de Proteína , Proteínas Recombinantes de Fusión/genética , Proteínas Recombinantes de Fusión/metabolismo , Homología de Secuencia de Aminoácido , Fracciones Subcelulares
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