scispace - formally typeset
G

Guillermo Mendoza-Hernández

Researcher at National Autonomous University of Mexico

Publications -  131
Citations -  2947

Guillermo Mendoza-Hernández is an academic researcher from National Autonomous University of Mexico. The author has contributed to research in topics: Protein subunit & ATP synthase. The author has an hindex of 27, co-authored 131 publications receiving 2680 citations.

Papers
More filters
Journal ArticleDOI

Identification of novel bacterial plasminogen-binding proteins in the human pathogen Mycobacterium tuberculosis.

TL;DR: Proteomic analysis together with ligand blotting assays identified several major Plg‐binding spots in Mycobacterium tuberculosis soluble extracts and culture filtrate proteins suggesting that M. tuberculosis posses several Plg receptors suggesting that bound Plg to bacteria surface, can be activated to Plm, endowing bacteria with the ability to break down ECM and basal membranes proteins contributing to tissue injury in tuberculosis.
Journal ArticleDOI

Identification of Novel Mitochondrial Protein Components of Chlamydomonas reinhardtii. A Proteomic Approach

TL;DR: Pure mitochondria of the photosynthetic algaChlamydomonas reinhardtii were analyzed using blue native-polyacrylamide gel electrophoresis (BN-PAGE) and a 60-kD protein, associated with the mitochondrial ATP synthase and with no known counterpart in any other organism, is reported.
Journal ArticleDOI

Increased synthesis of α-tocopherol, paramylon and tyrosine by Euglena gracilis under conditions of high biomass production.

TL;DR: To analyse the production of different metabolites by dark‐grown Euglena gracilis under conditions found to render high cell growth, and to evaluate the role of phytochemical signaling in cell growth.
Journal ArticleDOI

Mycobacterium tuberculosis glycoproteomics based on ConA-lectin affinity capture of mannosylated proteins.

TL;DR: A Mycobacterium tuberculosis culture filtrate enriched with mannose-containing proteins was resolved by 2-DE gel and 41 proteins were identified as putative glycoproteins with 34 of them new probably mannosylated proteins, contributing to the construction of the ConA affinity glycoprotein database of M. tuberculosis.
Journal ArticleDOI

Recombinant soluble betaglycan is a potent and isoform-selective transforming growth factor-beta neutralizing agent.

TL;DR: Results indicate that baculoviral soluble betaglycan has the biochemical and functional properties that would make it a suitable agent for the treatment of the diseases in which excess TGF-beta plays a central physiopathological role.