Identification of pp120, an endogenous substrate for the hepatocyte insulin receptor tyrosine kinase, as an integral membrane glycoprotein of the bile canalicular domain. [PDF]
Proceedings of the National Academy of Sciences of the United States of America, 1988 An endogenous membrane-bound substrate of the insulin receptor beta-subunit tyrosine kinase in liver, pp120, has been identified as HA4, a 110-kDa membrane glycoprotein localized primarily to the bile canalicular domain of the hepatocyte. HA4 has been implicated in bile salt transport and cell adhesion.
Ronald N Margolis +2 more
exaly +4 more sources
Angular Leaf Spot: A Bacterial Disease in Strawberries in Florida
EDIS, 2005 Angular Leaf Spot (ALS) is a bacterial disease caused by Xanthomonas fragariae Kennedy & King, a pathogen highly specific to wild and cultivated strawberry, Fragaria x ananassa Duchesne (Legard et al. 2003).
Natalia A. Peres +3 more
doaj +9 more sources
Corporate Social Responsibility of Export Organizations: Relation between Strategy, Activities and Communication on Foreign Markets [PDF]
Interdisciplinary Description of Complex Systems, 2021 The concept of corporate social responsibility has been recognized as a successful differentiation strategy for European export organizations in foreign markets.
Andrija Barić +2 more
doaj +3 more sources
Afadin loss induces breast cancer metastasis through destabilisation of E-cadherin to F-actin linkage. [PDF]
J PatholAbstract Afadin is a multimodal scaffolding protein with essential functions in cell–cell adhesion. Although its loss of expression has been linked to breast cancer invasion and metastasis, the underlying mechanisms driving tumour progression upon mutational Afadin (AFDN) loss in breast cancers remains unclear.
Rätze MA +12 more
europepmc +2 more sources
The Cytoplasmic Tyrosine Kinase FER Is Associated with the Catenin-Like Substrate pp120 and Is Activated by Growth Factors [PDF]
Molecular and Cellular Biology, 1995 The FER gene encodes a cytoplasmic tyrosine kinase with a single SH2 domain and an extensive amino terminus. In order to understand the cellular function of the FER kinase, we analyzed the effect of growth factor stimulation on the phosphorylation and activity of FER.
Tai Wai Wong, Leung Kim
exaly +3 more sources
Cloning and Characterization of a Functional Promoter of the Rat pp120 Gene, Encoding a Substrate of the Insulin Receptor Tyrosine Kinase [PDF]
Journal of Biological Chemistry, 1996 Cloning of the 5 -flanking region of the rat pp120 gene has indicated that it is a housekeeping gene: it lacks a functional TATA box and contains several Sp1 binding sites and multiple transcription initiation sites at nucleotides -101, -71, -41, and -27 spread over a GC-rich area.
Sonia M Najjar +2 more
exaly +3 more sources
Biochemistry, 1995 Insulin binding to the alpha-subunit of its receptor stimulates the receptor tyrosine kinase to phosphorylate the beta-subunit and several endogenous protein substrates, including pp120/HA4, a liver-specific plasma membrane glycoprotein of M(r) 20,000.
Sonia M Najjar +2 more
exaly +6 more sources
Memorias do Instituto Oswaldo Cruz, 2003 Two regulons, soxRS and marRAB, are associated with resistance to quinolones or multiple antibiotic in Salmonella enterica serovar Typhimurium. These regulons are activated by nitric oxide and redox-cycling drugs, such as paraquat and cause on activation
Coban AY, Durupinar B
doaj +3 more sources
The Role of Insulin Receptor Isoforms in Diabetes and Its Metabolic and Vascular Complications. [PDF]
J Diabetes Res, 2017 The insulin receptor (IR) presents by alternative splicing two isoforms: IRA and IRB. The differential physiological and pathological role of both isoforms is not completely known, and it is determinant the different binding affinity for insulin‐like growth factor.
Escribano O +4 more
europepmc +2 more sources
Insulin stimulates phosphorylation of a 120-kDa glycoprotein substrate (pp120) for the receptor-associated protein kinase in intact H-35 hepatoma cells. [PDF]
Proceedings of the National Academy of Sciences of the United States of America, 1987 The insulin receptor possesses protein kinase activity, which may play a role in mediating insulin action. Recently, we have identified a glycoprotein (pp120) in rat liver plasma membranes that is phosphorylated by the solubilized insulin receptor in a cell-free system. We now report that insulin stimulates phosphorylation of pp120 in intact H-35 cells.
Nicola Perrotti +2 more
exaly +3 more sources