Results 251 to 260 of about 67,145 (262)
Some of the next articles are maybe not open access.
Identification of a new protein that interacts with the tight junction protein ZO‐2
The FASEB Journal, 2008The purpose of this study is to identify new proteins that interact with the middle portion of ZO‐2. We found a new protein pb3PSG (protein binding to 3PSG) and we want to characterize it in epithelial MDCK cells. We performed a two‐hybrid system using the 3PSG segment of ZO‐2 as bait.
Susana Lechuga +2 more
openaire +1 more source
Annals of the New York Academy of Sciences, 2017
ZO‐2 is a peripheral tight junction protein that belongs to the membrane‐associated guanylate kinase protein family. Here, we explain the modular and supramodular organization of ZO‐2 that allows it to interact with a wide variety of molecules, including cell–cell adhesion proteins, cytoskeletal components, and nuclear factors.
Lorenza, González-Mariscal +4 more
openaire +2 more sources
ZO‐2 is a peripheral tight junction protein that belongs to the membrane‐associated guanylate kinase protein family. Here, we explain the modular and supramodular organization of ZO‐2 that allows it to interact with a wide variety of molecules, including cell–cell adhesion proteins, cytoskeletal components, and nuclear factors.
Lorenza, González-Mariscal +4 more
openaire +2 more sources
Organization and expression of the human zo-2 gene (tjp-2) in normal and neoplastic tissues
Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 2000One of the tight junction components, zonula occludens protein 2 (ZO-2), is expressed as two isoforms, ZO-2A and ZO-2C, in normal epithelia. In pancreatic adenocarcinoma of the ductal type ZO-2A is absent, but none of the common mechanisms of gene inactivation is responsible for lack of ZO-2A expression.
A, Chlenski +5 more
openaire +2 more sources
Annals of the New York Academy of Sciences, 2012
ZO‐2 is a membrane‐associated guanylate kinase homologue (MAGUK) tight protein associated with the cytoplasmic surface of tight junctions. Here, we describe how ZO‐2 is a multidomain molecule that binds to a variety of cell signaling proteins, to the actin cytoskeleton, and to gap, tight, and adherens junction proteins.
Lorenza, Gonzalez-Mariscal +3 more
openaire +2 more sources
ZO‐2 is a membrane‐associated guanylate kinase homologue (MAGUK) tight protein associated with the cytoplasmic surface of tight junctions. Here, we describe how ZO‐2 is a multidomain molecule that binds to a variety of cell signaling proteins, to the actin cytoskeleton, and to gap, tight, and adherens junction proteins.
Lorenza, Gonzalez-Mariscal +3 more
openaire +2 more sources
[LIM protein KyoT2 interacts with human tight junction protein ZO-2-i3].
Yi chuan xue bao = Acta genetica Sinica, 2003It was reported that LIM protein KyoT2 negatively regulated transcription by association with the RBP-J DNA-binding protein. Using yeast two-hybrid system with LIM protein KyoT2 as a bait, we have isolated an alternatively spliced form of human tight junction protein 2--ZO-2-i3.
Hong-Yan, Huang +6 more
openaire +1 more source
Toxicology and Applied Pharmacology, 2018
Methamidophos (MET) is an organophosphate (OP) pesticide widely used in agriculture in developing countries. MET causes adverse effects in male reproductive function in humans and experimental animals, but the underlying mechanisms remain largely unknown.
José Mario Ortega-Olvera +7 more
openaire +2 more sources
Methamidophos (MET) is an organophosphate (OP) pesticide widely used in agriculture in developing countries. MET causes adverse effects in male reproductive function in humans and experimental animals, but the underlying mechanisms remain largely unknown.
José Mario Ortega-Olvera +7 more
openaire +2 more sources
International Journal of Cancer, 1999
Differential display of hamster mRNA identified a fragment present in normal pancreatic duct cells that is not expressed in pancreatic duct carcinoma cells. Sequence analysis showed an 88% and 82% identity, respectively, to the cDNA of the canine and human tight junction zo-2 gene.
A, Chlenski +6 more
openaire +2 more sources
Differential display of hamster mRNA identified a fragment present in normal pancreatic duct cells that is not expressed in pancreatic duct carcinoma cells. Sequence analysis showed an 88% and 82% identity, respectively, to the cDNA of the canine and human tight junction zo-2 gene.
A, Chlenski +6 more
openaire +2 more sources
Experimental Cell Research, 2004
ZO-2 is a membrane-associated guanylate kinase (MAGUK) protein present at the tight junction (TJ) of epithelial cells. While confluent monolayers have ZO-2 at their cellular borders, sparse cultures conspicuously show ZO-2 at the nuclei. To study the role of nuclear ZO-2, we tested by pull-down assays and gel shift analysis the interaction between ZO-2
Abigail, Betanzos +5 more
openaire +2 more sources
ZO-2 is a membrane-associated guanylate kinase (MAGUK) protein present at the tight junction (TJ) of epithelial cells. While confluent monolayers have ZO-2 at their cellular borders, sparse cultures conspicuously show ZO-2 at the nuclei. To study the role of nuclear ZO-2, we tested by pull-down assays and gel shift analysis the interaction between ZO-2
Abigail, Betanzos +5 more
openaire +2 more sources
A
Contact inhibition of proliferation is a critical cell density control mechanism governed by the Hippo signalling pathway. The biochemical signalling underlying cell density‐dependent cues regulating Hippo signalling and its downstream effectors, YAP, remains poorly understood.
Olivia Xuan Liu +6 more
openaire +2 more sources
Intracellular Traffic and Non-canonical Roles of ZO-2 Protein
2022Lorenza González-Mariscal +5 more
openaire +1 more source