Publications by authors named "Wenbing Cao"

Article Synopsis
  • Fluorescent proteins are vital in research, serving as tools for studying biological processes due to their ability to emit light when excited.
  • Inspired by natural fluorophores, researchers created fluorescent molecular rotor amino acids (FMR-AAs) that mimic the fluorescence properties of these proteins.
  • By integrating FMR-AAs into various proteins, scientists can create artificial fluorescent proteins and effective biosensors to monitor interactions and changes within proteins in live cells and lab settings.
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The construction and optimization of microbial cell factories are crucial steps and key technologies in achieving green biomanufacturing. As concern has been aroused regarding the excessive carbon dioxide (CO) emissions and food security, a new and promising research field, microbial conversion of CO into food compounds, has emerged. The research in this field not only holds significant implications for achieving the carbon peaking and carbon neutrality goals but also plays a role in maintaining food security.

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Objective: To establish a porcine osteoporotic vertebral compression fracture model and compare the impact of unilateral vertebroplasty using trajectory-adjustable bone cement filling device to traditional surgical tools on vertebral biomechanics.

Methods: Twenty-four fresh adult porcine vertebrae were used to establish an osteoporotic vertebral compression fracture model. The specimens were divided into 4 groups (A, B, C, and D), each consisting of 6 vertebrae.

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Article Synopsis
  • RNA binding proteins (RBPs), particularly RBM34, play a significant role in tumor progression and the immune response, yet their mechanisms in cancer remain partially understood, highlighting the need for more research.
  • The study leveraged various databases to analyze RBM34's expression and localization across multiple tumor types, using survival analyses to connect RBM34 levels with clinical outcomes and immune environment.
  • Results indicated RBM34's expression correlated with patient survival and immune response—showing potential as a prognostic factor in osteosarcoma and linking its expression to tumor immunity and treatment efficacy.
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Background: The choice of polypectomy device and surveillance intervals for colorectal polyps are primarily decided by polyp size. We developed a deep learning-based system (ENDOANGEL-CPS) to estimate colorectal polyp size in real time.

Methods: ENDOANGEL-CPS calculates polyp size by estimating the distance from the endoscope lens to the polyp using the parameters of the lens.

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Research on the implications of ferroptosis in tumors has increased rapidly in the last decades. There are evidences that ferroptosis is involved in several aspects of cancer biology, including tumor progression, metastasis, immunomodulation, and therapeutic response. Nonetheless, the interaction between ferroptosis-related lncRNAs (FRLs) and the osteosarcoma immune microenvironment is poorly understood.

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Structurally diverse acylations have been identified as post-translational modifications (PTMs) on histone lysine residues, but their functions and regulations remain largely unknown. Interestingly, in nature, a lysine acylation analog, pyrrolysine, is introduced as a co-translational modification (CTM) through genetic encoding. To explore this alternative life form, we created a model organism Saccharomyces cerevisiae containing site-specific lysine CTMs (acetyl-lysine, crotonyl-lysine, or another synthetic analog) at histone H3K56 using non-canonical amino acid mutagenesis to afford a chemically modified nucleosome in lieu of their own in vivo.

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Objective: Osteosarcoma is the most frequent primary bone malignancy, associated with frequent recurrence and lung metastasis. RNA-binding proteins (RBPs) are pivotal in regulating several aspects of cancer biology. Nonetheless, interaction between RBPs and the osteosarcoma immune microenvironment is poorly understood.

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Silane-functionalized carbon dots (SiCDs) can be exploited as effective color converting materials for the solid-state light-emitting devices. However, most of SiCDs reported thus far have shown photoluminescence emissions in the blue and green spectral range, which limit them to construct an efficient white light-emitting diodes (WLEDs) due to the lack of long-wavelength emission. Herein, a series of double silane-functionalized carbon dots (DSiCDs) were prepared via a one-step solvothermal method.

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Supramolecular chemistry for targeting proteins is of great interest for the development of novel approaches to recognize, isolate and control proteins. Taking advantage of chemical biology approaches, such as genetic-code expansion and enzyme-mediated ligation, guest recognition elements can be built into proteins of interest, allowing supramolecular control of protein function and regulation. In this viewpoint article, we will discuss the methods, applications, limitations, and future perspectives of supramolecular chemistry for targeting proteins in a site-specific manner.

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Regulation of specific protein function is of great importance for both research and therapeutic development. Many small or large molecules have been developed to control specific protein function, but there is a lack of a universal approach to regulate the function of any given protein. We report a general host-guest molecular recognition approach involving modification of the protein functional surfaces with genetically encoded unnatural amino acids bearing guest side chains that can be specifically recognized by cucurbit[7]uril.

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Genetic code expansion (GCE) is a powerful technique for site-specific incorporation of noncanonical amino acids (ncAAs) into proteins in living cells, which is achieved through evolved aminoacyl-tRNA synthetase mutants. Stability is important for promoting enzyme evolution, and we found that many of the evolved synthetase mutants have reduced thermostabilities. In this study, we characterized two novel pyrrolysyl-tRNA synthetases (PylRSs) derived from thermophilic archaea: () and ().

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The -derived tyrosyl-tRNA synthetase was the first enzyme engineered for genetic code expansion in a eukaryotic system but can charge only a limited set of structurally simple noncanonical amino acids. In contrast, the thermophilic -derived tyrosyl-tRNA synthetase mutants, used in only a prokaryotic system, can charge a surprisingly large set of structurally diverse ncAAs, due to their remarkable structural ability to tolerate mutations. Inspired by this, we characterized a new class of tyrosyl-tRNA synthetase/tRNA pairs from thermophilic bacterium , which is homologous to the tyrosyl-tRNA synthetase but with better thermostability.

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Protein tyrosine phosphatases (PTPs) play critical roles in cell signaling pathways, but identification of unknown PTPs for a given substrate in live cells remain technically challenging. Here, we synthesized a series of tyrosine-based irreversible PTP inhibitors and characterized by site-specific encoding on substrate proteins in cells with an expanded genetic code. By fine-tuning the chemical reactivity, we identified optimal active amino acid probes to covalently cross-link a PTP and its substrate both in vitro and in mammalian cells.

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In this manuscript, we present a simple route to enhance upconversion (UC) emission by producing two different coordination sites of trivalent cations in a matrix material and adjusting crystal field asymmetry by Hf(4+) co-doping. A cubic phase, Y3.2Al0.

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Influences of structural properties on the stability of fullerenols are studied using experimental techniques including laser-induced dissociation associated with a time-of-flight measurement, synchrotron radiation XPS, and FT-IR spectroscopy. Stabilities of a family of fullerenols (C(OH), C(OH), C(OH), C(OH), C(OH), and C(OH)) as functions of structural parameters-the hydroxyl number, intensity of the impure group, and the ratio of the carbonyl to hydroxyl groups-are investigated. It is found that the molecular stability largely depends on the quantity of impure groups, especially the highly oxygenated carbons in fullerenols, but less on the hydroxyl number.

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