Experimental and computational evidence that Calpain-10 binds to the carboxy terminus of Na1.2 and Na1.6.

Voltage-gated sodium channels (Na) are pivotal proteins responsible for initiating and transmitting action potentials. Emerging evidence suggests that proteolytic cleavage of sodium channels by calpains is pivotal in diverse physiological scenarios, including ischemia, brain injury, and neuropathic pain associated with diabetes. Despite this significance, the precise mechanism by which calpains recognize sodium channels, especially given the multiple calpain isoforms expressed in neurons, remains elusive.

Molecular docking analysis of a dermatan sulfate tetra-saccharide to human alpha-L-iduronidase.

Human alpha-L-iduronidase (IDUA) is a 653 amino acid protein involved in the sequential degradation of glycos-amino-glycans (GAG), heparan sulfate (HS), and dermatan sulfate (DS). Some variants in the IDUA gene produce a deficient enzyme that causes un-degraded DS and HS to accumulate in multiple tissues, leading to an organ dysfunction known as muco-poly-saccharidosis type I (MPS I). Molecular and catalytic activity assays of new or rare variants of IDUA do not predict the phenotype that a patient will develop.

Atomistic mechanism of leptin and leptin-receptor association.

The leptin-leptin receptor complex is at the very core of energy homeostasis and immune system regulation, among many other functions. In this work, we built homology models of leptin and the leptin binding domain (LBD) of the receptor from humans and mice. Docking analyses were used to obtain the coordinates of the native leptin-LBD complexes and a mixed heterodimer formed by human leptin and mouse LBD.

Identification of an allergenic calmodulin from Amaranthus palmeri pollen.

Introduction: Pollens are an important source of allergens that trigger rhinitis or asthma. The allergenic extracts of pollens used to diagnose and treat allergies contain different allergenic antigens. Isolated allergenic proteins are employed in in vitro assays, skin tests and allergenic-specific immunotherapy.

Biochemical and Biophysical Characterization of the Enolase from .

Enolase, which catalyses the conversion of 2-phospho-D-glycerate to phosphoenolpyruvate, is an important enzyme in the classic glycolysis pathway in cells. Enolase is highly conserved in organisms from bacteria to humans, indicating its importance in cells. Thus, enolase is a good target for developing new drugs.

Structural Basis for the Limited Response to Oxidative and Thiol-Conjugating Agents by Triosephosphate Isomerase From the Photosynthetic Bacteria .

In plants, the ancestral cyanobacterial triosephosphate isomerase (TPI) was replaced by a duplicated version of the cytosolic TPI. This isoform acquired a transit peptide for chloroplast localization and functions in the Calvin-Benson cycle. To gain insight into the reasons for this gene replacement in plants, we characterized the TPI from the photosynthetic bacteria (SyTPI).

Characterization of multiple enolase genes from Trichomonas vaginalis. Potential novel targets for drug and vaccine design.

Trichomonas vaginalis is the protist parasite that causes the most common, non-viral sexually transmitted infection called trichomonosis. Enolase is a moonlighting protein that apart from its canonical function as a glycolytic enzyme, serves as a plasminogen receptor on the cell surface of T. vaginalis and, in consequence, it has been stablished as a virulence factor in this parasite.

A competent catalytic active site is necessary for substrate induced dimer assembly in triosephosphate isomerase.

The protozoan parasite Trichomonas vaginalis contains two nearly identical triosephosphate isomerases (TvTIMs) that dissociate into stable monomers and dimerize upon substrate binding. Herein, we compare the role of the "ball and socket" and loop 3 interactions in substrate assisted dimer assembly in both TvTIMs. We found that point mutants at the "ball" are only 39 and 29-fold less catalytically active than their corresponding wild-type counterparts, whereas Δloop 3 deletions are 1502 and 9400-fold less active.

[Determination and analysis of protein profile of different transfer factors].

Background: The transfer factor (TF) is the dialyzable extract of leukocytes with cellular immunity transfer properties. Its use has spread in the treatment of a wide range of immunologic, infectious, and even oncological diseases. However, important aspects in their protein profile, component concentrations, and a well-defined action mechanism are not completely unknown.

Structural insights from a novel invertebrate triosephosphate isomerase from Litopenaeus vannamei.

Triosephosphate isomerase (TIM; EC 5.3.1.

[Profilins: allergens with clinical relevance].

Introduction: Profilins are small ubiquitous proteins of 12-19 kDa involved in actin dynamics. These proteins are found in all eukaryotic organisms studied to date. Profilins have aminoacid sequences and tridimensional structure highly conserved.