gebhart/patrepeval huggingface dataset:
Morphologically controlled rapid fabrication of rhodium sulfide (Rh2S3) thin films for superior and robust hydrogen evolution reaction (2020)

Rh<sub>2</sub>S<sub>3</sub> thin film electrodes prepared by a facile and rapid fabrication route exhibit superior HER catalysis performance in acidic media.
Phytochemical analysis and bioactivity screening of three medicinal plants of Saudi Arabia (2020)

Purpose: To investigate the phytochemical analysis and bioactivity screening of some Asteraceae medicinal plants.&#x0D; Methods: The chemical constituents were isolated by column chromatography and elucidated using chemical and extensive spectroscopic methodologies including gas chromatoraphy-mass spectrometry (GC-MS), Fourier transform infrared spectroscopy (FTIR), as well as 1D and 2D nuclear magnetic resonance (NMR). The plant extracts were obtained by solvent extraction method while hydrodistillation was used to isolate plant essential oils. Furthermore, cup-plate agar diffusion was applied for antimicrobial activity evaluation while minimum inhibitory concentration (MIC) was assessed by microdilution technique.&#x0D; Results: Centaurea pseudosinaica, Tripleurospermum auriculatum, and Koelpinia linearis afforded previously undescribed three coumarins (xanthotoxin, cirsimaritin, salvigenins) from C. pseudosinaica, one steroid (estradiol) and a pentacyclic triterpene (β-amyrin) from T. auriculatum and a coumarin (santin) from K. linearis in good yields. In addition, the plant extracts and oils exhibited remarkable bioactivities including antifungal, antibacterial and antipyretic etc.&#x0D; Conclusion: The results reveal the presence of bioactive phytomolecules from Asteraceae plant extracts and volatile oils from three Asteraceae plants.&#x0D; Keywords: C. pseudosinaica, T. auriculatum, K. linearis, Xanthotoxin, Salvigenin, Cirsimaritin, Santin, Estradiol, β-amyrin, Antimicrobial activity
p185 HER2/neu Epitope Mapping with Murine Monoclonal Antibodies (1992)

In order to obtain further information on the biological role of the HER2/neu oncoprotein, 7 new monoclonal antibodies (MAbs) were produced against the p185HER2 extracellular domain. These MAbs, together with two others previously produced, were used to investigate the p185HER2 expression in breast carcinomas and compare the recognized antigenic determinants. The 7 reagents (MGR4,5,6,7,8,9 and 10), were shown to define five distinct epitopes. Three of these MAbs (MGR5,7,10), as well as one previously produced (MGR2), recognize the same epitope (Epitope-1) which seems, therefore, to be highly immunogenic for the murine immune system. Epitope-2 recognized by the MGR4 MAb, appears to be closely related to epitope-1 due to a cross inhibition between MGR4 and MGR10, but not MGR2. Epitope-2 is the only one of the 5 also present on the product of the neu oncogene, the rat analogue of the human HER2/neu gene. None of the reagents against epitope-1 and epitope-2 were found to mediate receptor internalization, whereas MGR6 as well as a previously produced MAb (MGR3), both of which define epitope-3 and MGR8 which defines epitope-4, were found to do so. Epitope-4 like the neu-specific peptide recognized by the reference c-neu Ab3 MAb, was detectable on all p185HER2 positive breast cancer, independently from the quantitative content of the oncoprotein, at variance with the other 4 epitopes whose availability on p185HER2 for the relevant MAbs varied with the degree of overexpression. Epitope-5, recognized by the MGR9 MAb, on the contrary to the other epitopes, was prevalently localized at the basal membrane level of the tumor nodule.