ORCID Profile
0000-0001-7264-6378
Current Organisations
UNSW Sydney
,
Getúlio Sales Diagnósticos
,
International Research Group
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Publisher: Elsevier BV
Date: 11-2019
Publisher: Elsevier BV
Date: 10-2021
Publisher: Elsevier BV
Date: 06-2021
Publisher: Elsevier BV
Date: 09-2023
Publisher: Elsevier BV
Date: 12-2020
Publisher: Royal Society of Chemistry (RSC)
Date: 2011
DOI: 10.1039/D1TA06978K
Abstract: Precise skin temperature monitoring with a 0.14 °C resolution is realized through (a) reducing strain interference with an optimized kirigami pattern and (b) increasing temperature sensitivity with low melting temperature TPU as the dielectric core.
Publisher: Elsevier BV
Date: 2021
Publisher: Elsevier BV
Date: 02-2021
Publisher: Elsevier BV
Date: 03-2019
Publisher: Royal Society of Chemistry (RSC)
Date: 2021
DOI: 10.1039/D0TA08775K
Abstract: A multilayer structured cathode for zinc ion batteries is created by using vertical graphene nano-maze to hold MnO 2 and encapsulating with an ionic conductive PEDOT:PSS layer. The new electrode exhibits exceptional capacity and cycle performance.
Publisher: Royal Society of Chemistry (RSC)
Date: 2021
DOI: 10.1039/D1TA08521B
Abstract: In this work, we present a new method of creating fibre-metal composites to effectively modulate the in-plane fracture behaviour of brittle conductive thin metal films on stretchable PDMS substrates via insertion of a toughening interlayer of CNFs.
Publisher: Elsevier BV
Date: 03-2022
DOI: 10.1016/J.JPROT.2021.104474
Abstract: Syndecans belong to the family of transmembrane heparan sulfate proteoglycans and are associated with many physiopathological processes, including oral cancer. As previously shown soluble syndecan-1 (SDC1) fragments and synthetic SDC1 peptide were able to induce cell migration in oral cancer cell lines. In order to explore the role of SDC1 in oral cancer, we have investigated SDC1 interacting partners and its functional role in oral cancer models. Here we have shown that SDC1 interacts with follistatin-related protein 1 (FSTL1) by its ectodomain (ectoSDC1) and extracellular juxtamembrane peptide (pepSDC1) and that their transcript levels can affect tumor events. Using orthotopic mouse model we identified that the knock-down for FSTL1 (shFSTL1) or for both FSTL1 and SDC1 (sh2KD) produced less aggressive and infiltrative tumors, with lower keratinization deposition, but with increased levels of epithelial-mesenchymal transition and proliferation compared to control and SDC1 knock-down. Based on cell culture assays, we suggest that the shFSTL1 effect on tumor tissues might be from significant increase of mRNA levels of Activin A (ActA) and its resceptors. This study shows for the first time two different complexes, SDC1 and FSTL1 pepSDC1 and FSTL1, exhibiting a close relationship in cell signaling events, as FSTL1 promotes a more aggressive phenotype. SIGNIFICANCE: This work contributes to the understanding of new SDC1 functions, based on the investigation of protein-protein complex formation in Oral Squamous cell carcinoma (OSCC) models. The FSTL1 identification, as an interacting partner of SDC1 ectodomain and of its derived peptide promotes molecular events that favors cancer development and progression, as highlighted by Activin A (ActA) and Epithelial-mesenchymal transition (EMT) gene expression and by changes in the phenotype of orthotopic OSCC mouse tumor tissues when SDC1-FSTL1 expression is modulated.
Publisher: Elsevier BV
Date: 05-2023
No related grants have been discovered for ZHAO SHA.