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1.
Sensors (Basel) ; 24(4)2024 Feb 08.
Artículo en Inglés | MEDLINE | ID: mdl-38400286

RESUMEN

The monitoring of the lifetime of cutting tools often faces problems such as life data loss, drift, and distortion. The prediction of the lifetime in this situation is greatly compromised with respect to the accuracy. The recent rise of deep learning, such as Gated Recurrent Unit Units (GRUs), Hidden Markov Models (HMMs), Convolutional Neural Networks (CNNs), Recurrent Neural Networks (RNNs), Attention networks, and Transformers, has dramatically improved the data problems in tool lifetime prediction, substantially enhancing the accuracy of tool wear prediction. In this paper, we introduce a novel approach known as PCHIP-Enhanced ConvGRU (PECG), which leverages multiple-feature fusion for tool wear prediction. When compared to traditional models such as CNNs, the CNN Block, and GRUs, our method consistently outperformed them across all key performance metrics, with a primary focus on the accuracy. PECG addresses the challenge of missing tool wear measurement data in relation to sensor data. By employing PCHIP interpolation to fill in the gaps in the wear values, we have developed a model that combines the strengths of both CNNs and GRUs with data augmentation. The experimental results demonstrate that our proposed method achieved an exceptional relative accuracy of 0.8522, while also exhibiting a Pearson's Correlation Coefficient (PCC) exceeding 0.95. This innovative approach not only predicts tool wear with remarkable precision, but also offers enhanced stability.

2.
Commun Biol ; 7(1): 649, 2024 May 27.
Artículo en Inglés | MEDLINE | ID: mdl-38802531

RESUMEN

Salivary complement inhibitors occur in many of the blood feeding arthropod species responsible for transmission of pathogens. During feeding, these inhibitors prevent the production of proinflammatory anaphylatoxins, which may interfere with feeding, and limit formation of the membrane attack complex which could damage arthropod gut tissues. Salivary inhibitors are, in many cases, novel proteins which may be pharmaceutically useful or display unusual mechanisms that could be exploited pharmaceutically. Albicin is a potent inhibitor of the alternative pathway of complement from the saliva of the malaria transmitting mosquito, Anopheles albimanus. Here we describe the cryo-EM structure of albicin bound to C3bBb, the alternative C3 convertase, a proteolytic complex that is responsible for cleavage of C3 and amplification of the complement response. Albicin is shown to induce dimerization of C3bBb, in a manner similar to the bacterial inhibitor SCIN, to form an inactive complex unable to bind the substrate C3. Size exclusion chromatography and structures determined after 30 minutes of incubation of C3b, factor B (FB), factor D (FD) and albicin indicate that FBb dissociates from the inhibited dimeric complex leaving a C3b-albicin dimeric complex which apparently decays more slowly.


Asunto(s)
Anopheles , Microscopía por Crioelectrón , Proteínas de Insectos , Animales , Proteínas de Insectos/química , Proteínas de Insectos/metabolismo , Anopheles/metabolismo , Anopheles/inmunología , Anopheles/parasitología , Complemento C3b/metabolismo , Complemento C3b/química , Proteínas y Péptidos Salivales/química , Proteínas y Péptidos Salivales/metabolismo , Modelos Moleculares
3.
Biomolecules ; 14(5)2024 Apr 25.
Artículo en Inglés | MEDLINE | ID: mdl-38785923

RESUMEN

Viruses are obligate intracellular parasites that rely on cell surface receptor molecules to complete the first step of invading host cells. The experimental method for virus receptor screening is time-consuming, and receptor molecules have been identified for less than half of known viruses. This study collected known human viruses and their receptor molecules. Through bioinformatics analysis, common characteristics of virus receptor molecules (including sequence, expression, mutation, etc.) were obtained to study why these membrane proteins are more likely to become virus receptors. An in-depth analysis of the cataloged virus receptors revealed several noteworthy findings. Compared to other membrane proteins, human virus receptors generally exhibited higher expression levels and lower sequence conservation. These receptors were found in multiple tissues, with certain tissues and cell types displaying significantly higher expression levels. While most receptor molecules showed noticeable age-related variations in expression across different tissues, only a limited number of them exhibited gender-related differences in specific tissues. Interestingly, in contrast to normal tissues, virus receptors showed significant dysregulation in various types of tumors, particularly those associated with dsRNA and retrovirus receptors. Finally, GateView, a multi-omics platform, was established to analyze the gene features of virus receptors in human normal tissues and tumors. Serving as a valuable resource, it enables the exploration of common patterns among virus receptors and the investigation of virus tropism across different tissues, population preferences, virus pathogenicity, and oncolytic virus mechanisms.


Asunto(s)
Neoplasias , Receptores Virales , Humanos , Neoplasias/genética , Neoplasias/metabolismo , Neoplasias/virología , Receptores Virales/genética , Receptores Virales/metabolismo , Biología Computacional/métodos , Multiómica
4.
Cell Rep ; 43(6): 114285, 2024 Jun 25.
Artículo en Inglés | MEDLINE | ID: mdl-38819987

RESUMEN

Proprotein convertase subtilisin/kexin type 9 (PCSK9) is a plasma protein that controls cholesterol homeostasis. Here, we design a human PCSK9 mimic, named HIT01, with no consecutive 9-residue stretch in common with any human protein as a potential heart attack vaccine. Murine immunizations with HIT01 reduce low-density lipoprotein (LDL) and cholesterol levels by 40% and 30%, respectively. Immunization of cynomolgus macaques with HIT01-K21Q-R218E, a cleavage-resistant variant, elicits high-titer PCSK9-directed antibody responses and significantly reduces serum levels of cholesterol 2 weeks after each immunization. However, HIT01-K21Q-R218E immunizations also increase serum PCSK9 levels by up to 5-fold, likely due to PCSK9-binding antibodies altering the half-life of PCSK9. While vaccination with a PCSK9 mimic can induce antibodies that block interactions of PCSK9 with the LDL receptor, PCSK9-binding antibodies appear to alter homeostatic levels of PCSK9, thereby confounding its vaccine impact. Our results nevertheless suggest a mechanism for increasing the half-life of soluble regulatory factors by vaccination.


Asunto(s)
Colesterol , Inmunización , Macaca fascicularis , Proproteína Convertasa 9 , Proproteína Convertasa 9/inmunología , Proproteína Convertasa 9/metabolismo , Animales , Humanos , Ratones , Colesterol/metabolismo , Colesterol/sangre , Inmunización/métodos , Receptores de LDL/metabolismo , Femenino , Ratones Endogámicos C57BL
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