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1.
Childs Nerv Syst ; 31(7): 1037-59, 2015 Jul.
Artículo en Inglés | MEDLINE | ID: mdl-25930727

RESUMEN

BACKGROUND: As important as the vertebral ligaments are in maintaining the integrity of the spinal column and protecting the contents of the spinal canal, a single detailed review of their anatomy and function is missing in the literature. METHODS: A literature search using online search engines was conducted. RESULTS: Single comprehensive reviews of the spinal ligaments are not found in the extant medical literature. CONCLUSIONS: This review will be useful to those who treat patients with pathology of the spine or who interpret imaging or investigate the anatomy of the ligaments of the vertebral column.


Asunto(s)
Ligamentos Longitudinales/anatomía & histología , Ligamentos Longitudinales/fisiología , Vértebras Lumbares/anatomía & histología , Vértebras Lumbares/fisiología , Humanos
2.
Childs Nerv Syst ; 31(7): 1061-6, 2015 Jul.
Artículo en Inglés | MEDLINE | ID: mdl-25939717

RESUMEN

BACKGROUND: As important as the vertebral ligaments are in maintaining the integrity of the spinal column and protecting the contents of the spinal canal, a single detailed review of their histology and embryology is missing in the literature. METHODS: A literature search using online search engines was conducted. RESULTS: Single comprehensive reviews of the histology and embryology of the spinal ligaments are not found in the extant medical literature. CONCLUSIONS: This review will be useful to those who study or treat patients with pathology of the spine.


Asunto(s)
Ligamentos Longitudinales/citología , Ligamentos Longitudinales/embriología , Vértebras Lumbares/citología , Vértebras Lumbares/embriología , Humanos
3.
Mol Biol Rep ; 39(4): 4663-72, 2012 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-22020851

RESUMEN

The complex life cycle of plasmodial parasites makes the selection of a single subunit protein a less than optimal strategy to generate an efficient vaccinal protection against malaria. Moreover, the full protection afforded by malarial proteins carried by intact parasites implies that immune responses against different antigens expressed in different phases of the cycle are required, but also suggests that native malarial antigens are presented to the host immune system in a manner that recombinant proteins do not achieve. The malarial apical membrane antigen 1 (AMA1) represents a suitable vaccine candidate because AMA1 is expressed on sporozoites and merozoites and allows them to invade hepatocytes and erythrocytes, respectively. Anti-AMA1 antibodies and cytotoxic T-cells are therefore expected to interfere both with the primary invasion of hepatocytes by sporozoites and with the later propagation of merozoites in erythrocytes, and thus efficiently counteract parasite development in its human host. AMA1 bears potential glycosylation sites and the human erythrocytic O-linked N-acetylglucosamine transferase (OGT) could glycosylate AMA1 through combinatorial metabolism. This hypothesis was tested in silico by developing binding models of AMA1 with human OGT complexed with UDP-GlcNc, and followed by the binding of O-GlcNAc with the hydroxyl group of AMA1 serine and threonine residues. Our results suggests that AMA1 shows potential for glycosylation at Thr517 and Ser498 and that O-GlcNAc AMA1 may constitute a conformationally more appropriate antigen for developing a protective anti-malarial immune response.


Asunto(s)
Acetilglucosamina/metabolismo , Biología Computacional , Vacunas contra la Malaria/inmunología , Plasmodium falciparum/inmunología , Procesamiento Proteico-Postraduccional , Proteínas Protozoarias/química , Proteínas Protozoarias/inmunología , Secuencia de Aminoácidos , Aminoácidos/metabolismo , Glicosilación , Humanos , Enlace de Hidrógeno , Modelos Moleculares , Datos de Secuencia Molecular , N-Acetilglucosaminiltransferasas/química , Estructura Secundaria de Proteína , Alineación de Secuencia
4.
J Cell Biochem ; 112(1): 138-46, 2011 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-21053365

RESUMEN

The multifunctionality of proteins is dictated by post-translational modifications (PTMs) which involve the attachment of small functional groups such as phosphate and acetate, as well as carbohydrate moieties. These functional groups make the protein perform various functions in different environments. PTMs play a crucial role in memory and learning. Phosphorylation of synaptic proteins and transcription factors regulate the generation and storage of memory. Among these is the cAMP-regulated element binding protein CREB that regulates CRE containing genes like c-fos. Both phosphorylation and acetylation control the function of CREB as a transcription factor. CREB is also susceptible to O-GlcNAc modification, which inhibits its activity. O-GlcNAc modification occurs on the same or neighboring Ser/Thr residues akin to phosphorylation. An interplay between these modifications was shown to operate in nuclear and cytoplasmic proteins. In this study computational methods were utilized to predict different modification sites in CREB. These in silico results suggest that phosphorylation, O-GlcNAc modification and acetylation modulate the transcriptional activity of CREB and thus dictate its contribution to synaptic plasticity.


Asunto(s)
Proteína de Unión a Elemento de Respuesta al AMP Cíclico/metabolismo , Hipocampo/metabolismo , Potenciación a Largo Plazo/fisiología , Secuencia de Aminoácidos , Animales , Biología Computacional/métodos , Humanos , Datos de Secuencia Molecular , Fosforilación , Procesamiento Proteico-Postraduccional , Transducción de Señal
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