12 research outputs found
Manual práctico de QuimiometrĂa
La QuĂmica AnalĂtica tiene en la EstadĂstica una de sus herramientas fundamentales. Esta imprescindible relaciĂłn ha dado lugar en los Ăşltimos años al desarrollo de la QuimiometrĂa, una disciplina que aplica las tĂ©cnicas matemáticas de la estadĂstica a los problemas analĂticos de la identificaciĂłn y cuantificaciĂłn de las sustancias quĂmicas, siendo habitual el uso de la quimiometrĂa en cualquier análisis quĂmico. En la actualidad, esta disciplina ha ganado importancia debido sobre todo por cantidad de informaciĂłn que obtenemos a travĂ©s de los equipos instrumentales (los cuales generan una gran cantidad de datos numĂ©ricos) y por el incremento en la capacidad de cálculo de los ordenadores actuales.
La EstadĂstica describe el comportamiento aleatorio de las variables analĂticas que usamos en el laboratorio. AsĂ, se puede usar para deducir las leyes de la probabilidad que rigen dichos comportamientos, con el fin de hacer previsiones sobre los mismos, tomar decisiones u obtener conclusiones. Por lo tanto, podemos clasificar a la estadĂstica como descriptiva, la cual nos dará solo informaciĂłn detallada de un conjunto de datos, e inferencial, cuando el objetivo del estudio se centra en derivar las conclusiones obtenidas de nuestro estudio a un conjunto de datos más amplio, es decir, hacer predicciones de los comportamientos de las variables analĂticas.
AsĂ, el siguiente manual describe conceptos básicos de probabilidad, de estadĂstica descriptiva e inferencial, siempre desde un punto de vista práctico y aplicado al análisis quĂmico. Fruto de ese enfoque práctico, se ofrecen alternativas para el desarrollo de los estudios estadĂsticos a travĂ©s de numerosos recursos gratuitos disponibles actualmente en internet. Es importante constar que para una mayor profundizaciĂłn en los conceptos teĂłricos aquĂ comentados, se recomienda consultar los textos didácticos referenciados que se han seguido para elaborar este texto, asĂ como las diversas fuentes de informaciĂłn comentadas en el Ăşltimo capĂtulo de este manual
video_2.mp4
<p>Centrosome- and Golgi-localized protein kinase N-associated protein (CG-NAP), also known as AKAP450, is a cytosolic scaffolding protein involved in the targeted positioning of multiple signaling molecules, which are critical for cellular functioning. Here, we show that CG-NAP is predominantly expressed in human primary T-lymphocytes, localizes in close proximity (<0.2 μm) with centrosomal and Golgi structures and serves as a docking platform for Protein Kinase A (PKA). GapmeR-mediated knockdown of CG-NAP inhibits LFA-1-induced T-cell migration and impairs T-cell chemotaxis toward the chemokine SDF-1α. Depletion of CG-NAP dislocates PKARIIα, disrupts centrosomal and non-centrosomal microtubule nucleation, causes Golgi fragmentation, and impedes α-tubulin tyrosination and acetylation, which are important for microtubule dynamics and stability in migrating T-cells. Furthermore, we show that CG-NAP coordinates PKA-mediated phosphorylation of pericentrin and dynein in T-cells. Overall, our findings provide critical insights into the roles of CG-NAP in regulating cytoskeletal architecture and T-cell migration.</p
video_3.mp4
<p>Centrosome- and Golgi-localized protein kinase N-associated protein (CG-NAP), also known as AKAP450, is a cytosolic scaffolding protein involved in the targeted positioning of multiple signaling molecules, which are critical for cellular functioning. Here, we show that CG-NAP is predominantly expressed in human primary T-lymphocytes, localizes in close proximity (<0.2 μm) with centrosomal and Golgi structures and serves as a docking platform for Protein Kinase A (PKA). GapmeR-mediated knockdown of CG-NAP inhibits LFA-1-induced T-cell migration and impairs T-cell chemotaxis toward the chemokine SDF-1α. Depletion of CG-NAP dislocates PKARIIα, disrupts centrosomal and non-centrosomal microtubule nucleation, causes Golgi fragmentation, and impedes α-tubulin tyrosination and acetylation, which are important for microtubule dynamics and stability in migrating T-cells. Furthermore, we show that CG-NAP coordinates PKA-mediated phosphorylation of pericentrin and dynein in T-cells. Overall, our findings provide critical insights into the roles of CG-NAP in regulating cytoskeletal architecture and T-cell migration.</p
Presentation_1.PDF
<p>Centrosome- and Golgi-localized protein kinase N-associated protein (CG-NAP), also known as AKAP450, is a cytosolic scaffolding protein involved in the targeted positioning of multiple signaling molecules, which are critical for cellular functioning. Here, we show that CG-NAP is predominantly expressed in human primary T-lymphocytes, localizes in close proximity (<0.2 μm) with centrosomal and Golgi structures and serves as a docking platform for Protein Kinase A (PKA). GapmeR-mediated knockdown of CG-NAP inhibits LFA-1-induced T-cell migration and impairs T-cell chemotaxis toward the chemokine SDF-1α. Depletion of CG-NAP dislocates PKARIIα, disrupts centrosomal and non-centrosomal microtubule nucleation, causes Golgi fragmentation, and impedes α-tubulin tyrosination and acetylation, which are important for microtubule dynamics and stability in migrating T-cells. Furthermore, we show that CG-NAP coordinates PKA-mediated phosphorylation of pericentrin and dynein in T-cells. Overall, our findings provide critical insights into the roles of CG-NAP in regulating cytoskeletal architecture and T-cell migration.</p
video_4.avi
<p>Centrosome- and Golgi-localized protein kinase N-associated protein (CG-NAP), also known as AKAP450, is a cytosolic scaffolding protein involved in the targeted positioning of multiple signaling molecules, which are critical for cellular functioning. Here, we show that CG-NAP is predominantly expressed in human primary T-lymphocytes, localizes in close proximity (<0.2 μm) with centrosomal and Golgi structures and serves as a docking platform for Protein Kinase A (PKA). GapmeR-mediated knockdown of CG-NAP inhibits LFA-1-induced T-cell migration and impairs T-cell chemotaxis toward the chemokine SDF-1α. Depletion of CG-NAP dislocates PKARIIα, disrupts centrosomal and non-centrosomal microtubule nucleation, causes Golgi fragmentation, and impedes α-tubulin tyrosination and acetylation, which are important for microtubule dynamics and stability in migrating T-cells. Furthermore, we show that CG-NAP coordinates PKA-mediated phosphorylation of pericentrin and dynein in T-cells. Overall, our findings provide critical insights into the roles of CG-NAP in regulating cytoskeletal architecture and T-cell migration.</p
video_5.avi
<p>Centrosome- and Golgi-localized protein kinase N-associated protein (CG-NAP), also known as AKAP450, is a cytosolic scaffolding protein involved in the targeted positioning of multiple signaling molecules, which are critical for cellular functioning. Here, we show that CG-NAP is predominantly expressed in human primary T-lymphocytes, localizes in close proximity (<0.2 μm) with centrosomal and Golgi structures and serves as a docking platform for Protein Kinase A (PKA). GapmeR-mediated knockdown of CG-NAP inhibits LFA-1-induced T-cell migration and impairs T-cell chemotaxis toward the chemokine SDF-1α. Depletion of CG-NAP dislocates PKARIIα, disrupts centrosomal and non-centrosomal microtubule nucleation, causes Golgi fragmentation, and impedes α-tubulin tyrosination and acetylation, which are important for microtubule dynamics and stability in migrating T-cells. Furthermore, we show that CG-NAP coordinates PKA-mediated phosphorylation of pericentrin and dynein in T-cells. Overall, our findings provide critical insights into the roles of CG-NAP in regulating cytoskeletal architecture and T-cell migration.</p
video_1.mp4
<p>Centrosome- and Golgi-localized protein kinase N-associated protein (CG-NAP), also known as AKAP450, is a cytosolic scaffolding protein involved in the targeted positioning of multiple signaling molecules, which are critical for cellular functioning. Here, we show that CG-NAP is predominantly expressed in human primary T-lymphocytes, localizes in close proximity (<0.2 μm) with centrosomal and Golgi structures and serves as a docking platform for Protein Kinase A (PKA). GapmeR-mediated knockdown of CG-NAP inhibits LFA-1-induced T-cell migration and impairs T-cell chemotaxis toward the chemokine SDF-1α. Depletion of CG-NAP dislocates PKARIIα, disrupts centrosomal and non-centrosomal microtubule nucleation, causes Golgi fragmentation, and impedes α-tubulin tyrosination and acetylation, which are important for microtubule dynamics and stability in migrating T-cells. Furthermore, we show that CG-NAP coordinates PKA-mediated phosphorylation of pericentrin and dynein in T-cells. Overall, our findings provide critical insights into the roles of CG-NAP in regulating cytoskeletal architecture and T-cell migration.</p
Histological comparison of antral (n = 85) and corpus (n = 83) gastric mucosa of <i>H. pylori (HP)</i>-positive children and antral (n = 202) and corpus (n = 214) gastric mucosa of <i>H. pylori</i>-negative children.<sup>*</sup>.
*<p>Twenty-four antral and 13 corpus gastric biopsy specimens were deemed to be inadequate for histology assessment. n, number.</p
Multiple linear regression models including ferritin or haemoglobin as dependent variables and age, gender and <i>H. pylori</i> (HP) infection as independent variables in children from United Kingdom (n = 81), Chile (n = 105) and Brazil (n = 125).
<p>Multiple linear regression models including ferritin or haemoglobin as dependent variables and age, gender and <i>H. pylori</i> (HP) infection as independent variables in children from United Kingdom (n = 81), Chile (n = 105) and Brazil (n = 125).</p
Multiple linear regression models including ferritin or haemoglobin as dependent variables and age, gender, country of birth and <i>H. pylori</i> infection as independent variables in children from United Kingdom, Chile and Brazil (n = 311).
<p>Multiple linear regression models including ferritin or haemoglobin as dependent variables and age, gender, country of birth and <i>H. pylori</i> infection as independent variables in children from United Kingdom, Chile and Brazil (n = 311).</p