Dr Qiuping Zhang Research fellows Supervisors Senior Research Fellow Research subject areas Cardiovascular Contact details qp.zhang@kcl.ac.uk +44 (0) 20 7848 5222
Nesprin-2 is a novel scaffold protein for telethonin and FHL-2 in the cardiomyocyte sarcomere Nesprin-1: Novel Regulator of Striated Muscle Nuclear Positioning and Mechanotransduction SUN1/2 are essential for RhoA/ROCK regulated actomyosin activity in isolated vascular smooth muscle cells Nesprin-1-alpha2 associates with kinesin at myotube outer nuclear membranes, but is restricted to neuromuscular junction nuclei in adult muscle Mouse models of nesprin related diseases Nesprin-1/2: roles in nuclear envelope organisation, myogenesis and muscle disease Novel nesprin-1 mutations associated with dilated cardiomyopathy cause nuclear envelope disruption and defects in myogenesis Identification and Validation of Putative Nesprin Variants N-terminal nesprin-2 variants regulate β-catenin signalling Selumetinib, an Oral Anti-Neoplastic Drug, May Attenuate Cardiac Hypertrophy via Targeting the ERK Pathway. Specific localization of nesprin-1-α2, the short isoform of nesprin-1 with a KASH domain, in developing, fetal and regenerating muscle, using a new monoclonal antibody Nesprin-2-dependent ERK1/2 compartmentalisation regulates the DNA damage response in vascular smooth muscle cell ageing. Bidirectional Cross-Regulation between the Endothelial Nitric Oxide Synthase and β-Catenin Signaling Pathways Nesprins: Tissue-Specific Expression of Epsilon and Other Short Isoforms Novel nesprin-1 mutations disrupt NE organization and induce dilated cardiomyopathy Multiple Novel Nesprin-1 and Nesprin-2 Variants Act as Versatile Tissue-Specific Intracellular Scaffolds The roles of nesprins in cardiac cell function Nesprin-1 and actin contribute to nuclear and cytoskeletal defects in lamin A/C-deficient cardiomyopathy Novel nuclear nesprin-2 variants tether active extracellular signal-regulated MAPK1 and MAPK2 at promyelocytic leukemia protein nuclear bodies and act to regulate smooth muscle cell proliferation Paternal Uniparental Isodisomy of Chromosome 6 Causing a Complex Syndrome Including Complete IFN-gamma Receptor 1 Deficiency Distinct functional domains in nesprin-1alpha and nesprin-2beta bind directly to emerin and both interactions are disrupted in X-linked Emery-Dreifuss muscular dystrophy Nesprin-1 and -2 are involved in the pathogenesis of Emery Dreifuss muscular dystrophy and are critical for nuclear envelope integrity Nesprin-2 is a multi-isomeric protein that binds lamin and emerin at the nuclear envelope and forms a subcellular network in skeletal muscle Nesprins: intracellular scaffolds that maintain cell architecture and coordinate cell function? Osteo/chondrocytic transcription factors and their target genes exhibit distinct patterns of expression in human arterial calcification The nesprins are giant actin-binding proteins, orthologous to Drosophila melanogaster muscle protein MSP-300 Nesprins: a novel family of spectrin-repeat-containing proteins that localize to the nuclear membrane in multiple tissues View all publications