Luciano Puzer

• Abstract

  Protease inhibitors can directly or indirectly affect the active proteolytic enzyme, limiting or eliminating their ability to catalyze the cleavage of peptide bonds. These molecules may also act selectively or specifically, endogenously controlling various physiological processes. In recent years our group has been working on developing inhibitors for proteases, particularly against human…

  Development of Inhibitors for Human Tissue Kallikreins, AP.R

• Abstract

  The human tissue kallikreins (KLKs) are a group of 15 serine proteases distributed over a wide range of tissues. They appear involved in several pathological events, and therefore it is believed that specific inhibitors to these enzymes may represent new therapeutic procedures for certain pathologies. The KLKs also appear differentially expressed in cancer, and for this reason they are po…

  Development of mutant serpins for inhibition of human tissue kallikreins, AP.R

• Abstract

  Human kallikreins 5 (KLK5) and 7 (KLK7) are members of the human tissue kallikreins, comprising 15 kallikrein like serine peptidases (KLKs). KLK5 is found in many tissues, including breast, central nervous system, prostate, testis and trachea; and KLK7 was reported to be present at esophagus, kidney, liver and salivary gland. Moreover, both enzymes appear to be most abundantly expressed i…

  Development of inhibitors for human tissue kallikreins 5 and 7 (KLK5 and KLK7), AP.R

(Only some records are available in English at this moment)

• Abstract

  Protease inhibitors are molecules capable of directly or indirectly affecting the active site of proteolytic enzymes, limiting or eliminating their ability to catalyze the cleavage of peptide bonds. These molecules can still act selectively or specifically, endogenously controlling the most diverse physiological processes. In addition, protease inhibitors also represent a considerable sha…

  Expression and inhibitory characterization of scFv antibody fragments against kallikrein 7, BP.IC

• Abstract

  Human tissue kallikreins (KLKs) are a group of serine proteases found in many tissues and cells, therefore they are related to a variety of physiological processes. Kallikreins also catch attention for being differentially expressed in cancer tissues, what suggests that they can be used as cancer biomarkers. Several studies with fluorescent peptides have contributed towards the characteri…

  Development of a recombinant serpins library for specificity study of the human tissue kallikreins, BP.DR

• Abstract

  Serpin is the name given to the superfamily of proteins with a wide variety of biological functions, and that has as main characteristic the inhibition of serine proteases. Our group recently described and characterized the first of the serpin Sphenophorus levis, popularly known as "bicudo de cana", which attacks the Brazilian sugar cane causing great damage to this crop. Until recently i…

  BACTERIAL SERPINS: PRODUCTION, CHARACTERIZATION AND ACTIVITY AGAINST MELANOMA CELLS, BP.DR

(Only some records are available in English at this moment)

• Abstract

  The human tissue kallikreins (KLKs) comprise a family of 15 serine proteases distributed over various tissues and biological fluids. These enzymes are indicated as acting in different pathologies such as Alzheimer's disease, cancer, atopic dermatitis, multiple sclerosis, Parkinson's disease, psoriasis, and others. Thus, there is a demand for specific inhibitors for each of the KLKs, and …

  Production of recombinant antibodies for human tissue kallikreins using phage display, BE.PQ

• Abstract

  The human tissue kallikreins (KLKs) comprise a family of fifteen serine proteases found in a diversity of biological fluids and tissues. These enzymes are identified as having function in different diseases such as Alzheimer's, cancer, atopic dermatitis, multiple sclerosis, Parkinson's, psoriasis, and others. Thus there is a growing demand for specific inhibitors for each of these kallikr…

  Development of inhibitors for human tissue kallikreins 3 and 5 (KLK3 and KLK5) through a phage display library based on the human alpha-1 antitrypsin, BE.EP.DR