University of Medicine and Dentistry of New Jersey

About: University of Medicine and Dentistry of New Jersey is a based out in . It is known for research contribution in the topics: Population & Poison control. The organization has 14634 authors who have published 19610 publications receiving 1041794 citations.

A multi-center randomized trial of buprenorphine–naloxone versus clonidine for opioid detoxification: findings from the National Institute on Drug Abuse Clinical Trials Network

Abstract: Aims The clinical effectiveness of buprenorphine–naloxone (bup-nx) and clonidine for opioid detoxification in in-patient and out-patient community treatment programs was investigated in the first studies of the National Institute of Drug Abuse Clinical Trials Network.

Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1).

Abstract: Sin3 is an evolutionarily conserved corepressor that exists in different complexes with the histone deacetylases HDAC1 and HDAC2. Sin3-HDAC complexes are believed to deacetylate nucleosomes in the vicinity of Sin3-regulated promoters, resulting in a repressed chromatin structure. We have previously found that a human Sin3-HDAC complex includes HDAC1 and HDAC2, the histone-binding proteins RbAp46 and RbAp48, and two novel polypeptides SAP30 and SAP18. SAP30 is a specific component of Sin3 complexes since it is absent in other HDAC1/2-containing complexes such as NuRD. SAP30 mediates interactions with different polypeptides providing specificity to Sin3 complexes. We have identified p33ING1b, a negative growth regulator involved in the p53 pathway, as a SAP30-associated protein. Two distinct Sin3-p33ING1b-containing complexes were isolated, one of which associates with the subunits of the Brg1-based Swi/Snf chromatin remodeling complex. The N terminus of p33ING1b, which is divergent among a family of ING1 polypeptides, associates with the Sin3 complex through direct interaction with SAP30. The N-terminal domain of p33 is present in several uncharacterized human proteins. We show that overexpression of p33ING1b suppresses cell growth in a manner dependent on the intact Sin3-HDAC-interacting domain.

Jak-Stat signal transduction pathway through the eyes of cytokine class II receptor complexes.

Abstract: Cells of the immune system communicate with each other to initiate, establish and maintain immune responses. The communication occurs through cell-to-cell contact or through a variety of intercellular mediators that include cytokines, chemokines, growth factors and hormones. In the case of cytokines, the signal is transmitted from the outside to the inside of a cell through cell surface receptors specific for each cytokine. At this step the signal is also decoded and amplified: ligand binding causes recruitment and/or activation of numerous cytoplasmic proteins. One cytokine can activate a number of signal transduction pathways leading to regulation of a wide array of biological activities. One of these pathways, the Jak-Stat pathway, is briefly reviewed here with respect to the class II cytokine receptors. Signal transduction through receptors for interferons Type I (IFN-alpha, IFN-beta, IFN-omega) and Type II (IFN-gamma), and interleukin 10 (IL-10) is described in detail. In addition, a complex between tissue factor (TF) and coagulation factor VIIa, and two new receptors related to the class II cytokine receptor family are discussed. Oncogene (2000).