Juan Pablo Reyes-Grajeda

Dr. Juan Pablo Reyes-Grajeda

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Research Focus & Metrics

Academic Career Length

26Years (2001-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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1 January 2015 in Journal of Immunology Research
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Journal Article
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RARodrigo Arreola
Rodrigo Arreola
SQSaray Saray Quintero Quintero
Saray Saray Quintero Quintero
RRRocio Ivette Lopez Roa
Rocio Ivette Lopez Roa
EFEnrique Octavio Flores-Gutiérrez
Enrique Octavio Flores-Gutiérrez
JRJuan Pablo Reyes-Grajeda
Juan Pablo Reyes-Grajeda
Daniel Ortuño-SahagúnDaniel Ortuño-Sahagún
Daniel Ortuño-Sahagún
The benefits of garlic to health have been proclaimed for centuries; however, only recently haveAllium sativumand its derivatives been proposed as promising candidates for maintaining the homeostasis of the immune system. The complex biochemistry of garlic makes it possible for variations in processing to yield different preparations with differences in final composition and compound proportion. In this review, we assess the most recent experimental results, which indicate that garlic appears to enhance the functioning of the immune system by stimulating certain cell types, such as macrophages, lymphocytes, natural killer (NK) cells, dendritic cells, and eosinophils, by mechanisms including modulation of cytokine secretion, immunoglobulin production, phagocytosis, and macrophage activation. Finally, because immune dysfunction plays an important role in the development and progress of several diseases, we critically examined immunoregulation by garlic extracts and compounds isolated, which can contribute to the treatment and prevention of pathologies such as obesity, metabolic syndrome, cardiovascular disorders, gastric ulcer, and even cancer. We concluded thatA. sativummodulates cytokine secretion and that such modulation may provide a mechanism of action for many of their therapeutic effects.

27 January 2010 in Journal of Agricultural and Food Chemistry
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Journal Article
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VVVictoria M. Virador
Victoria M. Virador
JRJuan Pablo Reyes-Grajeda
Juan Pablo Reyes-Grajeda
ABAlejandro Blanco-Labra
Alejandro Blanco-Labra
EMElizabeth Mendiola-Olaya
Elizabeth Mendiola-Olaya
GSGary M. Smith
Gary M. Smith
JWJohn R. Whitaker
John R. Whitaker

18 July 2016 in Neuroscience Bulletin
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Journal Article
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Philippe LeffPhilippe Leff
Philippe Leff
IMIsmael Mancilla-Herrera
Ismael Mancilla-Herrera
MFMónica Flores-Ramos
Mónica Flores-Ramos
CCCarlos Cruz-Fuentes
Carlos Cruz-Fuentes
JRJuan Pablo Reyes-Grajeda
Juan Pablo Reyes-Grajeda
DPDavid Ellioth Pulido-Ascencio
David Ellioth Pulido-Ascencio

26 September 2008 in Journal of Experimental & Clinical Cancer Research
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Journal Article
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GMGustavo Ulises Martinez-Ruiz
Gustavo Ulises Martinez-Ruiz
VMVilma Maldonado
Vilma Maldonado
GCGisela Ceballos-Cancino
Gisela Ceballos-Cancino
JRJuan Pablo Reyes-Grajeda
Juan Pablo Reyes-Grajeda
JMJorge Melendez-Zajgla
Jorge Melendez-Zajgla
Second mitochondria-derived activator of caspase/direct inhibitor of apoptosis-binding protein with low pI (Smac/DIABLO) is a proapoptogenic mitochondrial protein that is released to the cytosol in response to diverse apoptotic stimuli, including commonly used chemotherapeutic drugs. In the cytosol, Smac/DIABLO interacts and antagonizes inhibitors of apoptosis proteins (IAPs), thus allowing the activation of caspases and apoptosis. This activity has prompted the synthesis of peptidomimetics that could potentially be used in cancer therapy. For these reasons, several authors have analyzed the expression levels of Smac/DIABLO in samples of patients from different tumors. Although dissimilar results have been found, a tissue-specific role of this protein emerges from the data. The objective of this review is to present the current knowledge of the Smac/DIABLO role in cancer and its possible use as a marker or therapeutic target for drug design.

1 October 2012 in International Dairy Journal
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Journal Article
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RRRebeca Rojas-Ronquillo
Rebeca Rojas-Ronquillo
ACAlma Cruz-Guerrero
Alma Cruz-Guerrero
AFAngélica Flores-Nájera
Angélica Flores-Nájera
GRGabriela Rodríguez-Serrano
Gabriela Rodríguez-Serrano
LGLorena Gómez-Ruiz
Lorena Gómez-Ruiz
MGMariano García-Garibay
Mariano García-Garibay

1 September 2004 in Journal of Biological Chemistry
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Journal Article
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JRJuan Pablo Reyes-Grajeda
Juan Pablo Reyes-Grajeda
AMAbel Moreno
Abel Moreno
ARAntonio Romero
Antonio Romero
Ovocleidin-17 (OC17) from Gallus gallus is one of the best candidates to control and regulate the deposition of calcium carbonate in the calcified eggshell layer. Here, the crystal structure of monomeric OC17, determined at a resolution of 1.5 Å, was refined to a crystallographic R-factor of 20.1%. This is the first protein directly involved in a non-pathological biomineralization process resolved by x-ray diffraction to date. The protein has a mixed α/β structure containing a single C-type lectin-like domain. However, although OC17 shares the conserved scaffold of the C-type lectins, it does not bind carbohydrates. Nevertheless, in vitro OC17 modifies the crystalline habit of calcium carbonate (CaCO3) and the pattern of crystal growth at intervals of 5–200 μg/ml. Determining the three-dimensional structure of OC17 contributes to a better understanding of the biological behavior of structurally related biomolecules and of the mechanisms involved in eggshell and other mineralization processes.