<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Secchiero, P</style></author><author><style face="normal" font="default" size="100%">Perri, P</style></author><author><style face="normal" font="default" size="100%">Melloni, E</style></author><author><style face="normal" font="default" size="100%">Martini, A</style></author><author><style face="normal" font="default" size="100%">Lamberti, G</style></author><author><style face="normal" font="default" size="100%">Sebastiani, A</style></author><author><style face="normal" font="default" size="100%">Zauli, G</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Decreased levels of soluble TNF-related apoptosis-inducing ligand (TRAIL) in the conjunctival sac fluid of patients with diabetes affected by proliferative retinopathy.</style></title><secondary-title><style face="normal" font="default" size="100%">Diabet Med</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Diabet. Med.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Apoptosis Regulatory Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Body Fluids</style></keyword><keyword><style  face="normal" font="default" size="100%">Conjunctiva</style></keyword><keyword><style  face="normal" font="default" size="100%">Diabetic Retinopathy</style></keyword><keyword><style  face="normal" font="default" size="100%">Female</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Male</style></keyword><keyword><style  face="normal" font="default" size="100%">Middle Aged</style></keyword><keyword><style  face="normal" font="default" size="100%">Receptors, TNF-Related Apoptosis-Inducing Ligand</style></keyword><keyword><style  face="normal" font="default" size="100%">TNF-Related Apoptosis-Inducing Ligand</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2011</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2011 Oct</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">28</style></volume><pages><style face="normal" font="default" size="100%">1277-8</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><issue><style face="normal" font="default" size="100%">10</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/21923698?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Bosco, R</style></author><author><style face="normal" font="default" size="100%">Melloni, E</style></author><author><style face="normal" font="default" size="100%">Celeghini, C</style></author><author><style face="normal" font="default" size="100%">Rimondi, E</style></author><author><style face="normal" font="default" size="100%">Vaccarezza, M</style></author><author><style face="normal" font="default" size="100%">Zauli, G</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Fine tuning of protein kinase C (PKC) isoforms in cancer: shortening the distance from the laboratory to the bedside.</style></title><secondary-title><style face="normal" font="default" size="100%">Mini Rev Med Chem</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Mini Rev Med Chem</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Antineoplastic Agents</style></keyword><keyword><style  face="normal" font="default" size="100%">Biological Products</style></keyword><keyword><style  face="normal" font="default" size="100%">Enzyme Inhibitors</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Isoenzymes</style></keyword><keyword><style  face="normal" font="default" size="100%">Neoplasms</style></keyword><keyword><style  face="normal" font="default" size="100%">Oligonucleotides, Antisense</style></keyword><keyword><style  face="normal" font="default" size="100%">Peptides</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Kinase C</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2011</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2011 Mar</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">11</style></volume><pages><style face="normal" font="default" size="100%">185-99</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The serine/threonine protein kinase C (PKC) family was first identified as intracellular receptor(s) for the tumor promoting agents phorbol esters. Thirty years after the discovery of PKC, the role of specific PKC isoforms has been described in relationship with an altered pattern of expression in different types of cancer and a good number of small molecule inhibitors (inhibitory peptides, antisense oligonucleotides or natural compounds) targeting PKC are now available. Despite all these achievements and a huge amount of basic research studies on the biochemical regulation of PKC, there has been a delay in clinical trials with drugs targeting PKC function. This delay is easily explained taking into account the extreme biological complexity of the PKC family of isoforms and the incomplete understanding of the specific role of each PKC isozyme in different types of cancers. Some of the difficulties in developing pharmacological compounds selectively tuning the different PKCs have started to be overcome. In this review, the growing evidences of the role of the PKC isoforms α, βII, δ, ε, ζ and ι is in promoting or counteracting tumor progression will be discussed in relationship with promising therapeutic perspectives.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">3</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/21534929?dopt=Abstract</style></custom1></record></records></xml>