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1.
Sensors (Basel) ; 23(20)2023 Oct 13.
Artigo em Inglês | MEDLINE | ID: mdl-37896530

RESUMO

Due to the swift growth in the scale of remote sensing imagery, scholars have progressively directed their attention towards achieving efficient and adaptable cross-modal retrieval for remote sensing images. They have also steadily tackled the distinctive challenge posed by the multi-scale attributes of these images. However, existing studies primarily concentrate on the characterization of these features, neglecting the comprehensive investigation of the complex relationship between multi-scale targets and the semantic alignment of these targets with text. To address this issue, this study introduces a fine-grained semantic alignment method that adequately aggregates multi-scale information (referred to as FAAMI). The proposed approach comprises multiple stages. Initially, we employ a computing-friendly cross-layer feature connection method to construct a multi-scale feature representation of an image. Subsequently, we devise an efficient feature consistency enhancement module to rectify the incongruous semantic discrimination observed in cross-layer features. Finally, a shallow cross-attention network is employed to capture the fine-grained semantic relationship between multiple-scale image regions and the corresponding words in the text. Extensive experiments were conducted using two datasets: RSICD and RSITMD. The results demonstrate that the performance of FAAMI surpasses that of recently proposed advanced models in the same domain, with significant improvements observed in R@K and other evaluation metrics. Specifically, the mR values achieved by FAAMI are 23.18% and 35.99% for the two datasets, respectively.

2.
Micromachines (Basel) ; 12(5)2021 May 04.
Artigo em Inglês | MEDLINE | ID: mdl-34064378

RESUMO

Microcontact force measurement is widely applied in micro/nano manufacturing, medicine and microelectromechanical systems. Most microcontact force measurements are performed by using mass comparators, nano-indenter and precision electronic balance, and weighing sensors. However, these instruments have a complex structure and high cost. Nevertheless, the rapid development of microsensor technology provides a new, simple and low-cost approach for microcontact force measurement. In this study, we present a method of microcontact force measurement by using micropressure sensors and study the relationship amongst the microcontact force, output voltage and contact position of the sensor. We use a microcapacitance pressure sensor as an example, then we perform a simulation calculation and construct a microcontact force experiment system to verify the simulation results. The experimental and simulation results are consistent. In addition, an equation that describes the relationship amongst the microcontact force, output voltage and contact position of the sensor is obtained. Based on this simple and low-cost method, we build a micro-manipulation system, which indicates that the micropressure sensors can be used to measure microcontact force in various applications easily and cost-effectively. Furthermore, it is considerably relevant to research and application in this field.

3.
Mol Cell Biol ; 25(18): 8273-84, 2005 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-16135815

RESUMO

SRC-3/AIB1/ACTR/pCIP/RAC3/TRAM1 is a primary transcriptional coregulator for estrogen receptor (ER). Six SRC-3 phosphorylation sites have been identified, and these can be induced by steroids, cytokines, and growth factors, involving multiple kinase signaling pathways. Using phosphospecific antibodies for six phosphorylation sites, we investigated the mechanisms involved in estradiol (E2)-induced SRC-3 phosphorylation and found that this occurs only when either activated estrogen receptor alpha (ERalpha) or activated ERbeta is present. Both the activation function 1 and the ligand binding domains of ERalpha are required for maximal induction. Mutations in the coactivator binding groove of the ERalpha ligand binding domain inhibit E2-stimulated SRC-3 phosphorylation, as do mutations in the nuclear receptor-interacting domain of SRC-3, suggesting that ERalpha must directly contact SRC-3 for this posttranslational modification to take place. A transcriptionally inactive ERalpha mutant which localizes to the cytoplasm supports E2-induced SRC-3 phosphorylation. Mutations of the ERalpha DNA binding domain did not block this rapid E2-dependent SRC-3 phosphorylation. Together these data demonstrate that E2-induced SRC-3 phosphorylation is dependent on a direct interaction between SRC-3 and ERalpha and can occur outside of the nucleus. Our results provide evidence for an early nongenomic action of ER on SRC-3 that supports the well-established downstream genomic roles of estrogen and coactivators.


Assuntos
Acetiltransferases/metabolismo , Citoplasma/metabolismo , Estradiol/farmacologia , Receptor alfa de Estrogênio/metabolismo , Receptor beta de Estrogênio/metabolismo , Proteínas Oncogênicas/metabolismo , Transativadores/metabolismo , Acetiltransferases/imunologia , Motivos de Aminoácidos , Anticorpos Fosfo-Específicos/imunologia , Núcleo Celular/metabolismo , Citoplasma/química , DNA/metabolismo , Receptor alfa de Estrogênio/análise , Receptor alfa de Estrogênio/genética , Receptor beta de Estrogênio/análise , Receptor beta de Estrogênio/genética , Histona Acetiltransferases , Humanos , Mutação , Proteínas Nucleares/metabolismo , Coativador 3 de Receptor Nuclear , Proteínas Oncogênicas/imunologia , Fosforilação/efeitos dos fármacos , Estrutura Terciária de Proteína , Receptores de Interferon/metabolismo , Moduladores Seletivos de Receptor Estrogênico/farmacologia , Transativadores/imunologia
4.
Clin Cancer Res ; 8(5): 986-93, 2002 May.
Artigo em Inglês | MEDLINE | ID: mdl-12006510

RESUMO

PURPOSE: Ansamycin antibiotics, including 17allylamino-17-demethoxygeldanamycin (17-AAG), inhibit Hsp90 function and cause the selective degradation of signaling proteins that require this chaperone for folding. Because mutations in the androgen receptor (AR) and activation of HER2 and Akt may account, in part, for prostate cancer progression after castration or treatment with antiandrogens, we sought to determine whether an inhibitor of Hsp90 function could degrade these Hsp90 client proteins and inhibit the growth of prostate cancer xenografts with an acceptable therapeutic index. EXPERIMENTAL DESIGN: The effect of 17-AAG on the expression of Hsp90 regulated signaling proteins in prostate cancer cells and xenografts was determined. The pharmacodynamics of target protein degradation was associated with the toxicology and antitumor activity of the drug. RESULTS: 17-AAG caused the degradation of HER2, Akt, and both mutant and wild-type AR and the retinoblastoma-dependent G1 growth arrest of prostate cancer cells. At nontoxic doses, 17-AAG caused a dose-dependent decline in AR, HER2, and Akt expression in prostate cancer xenografts. This decline was rapid, with a 97% loss of HER2 and an 80% loss of AR expression at 4 h. 17-AAG treatment at doses sufficient to induce AR, HER2, and Akt degradation resulted in the dose-dependent inhibition of androgen-dependent and -independent prostate cancer xenograft growth without toxicity. CONCLUSIONS: These data demonstrate that, at a tolerable dose, inhibition of Hsp90 function by 17-AAG results in a marked reduction in HER2, AR, and Akt expression and inhibition of prostate tumor growth in mice. These results suggest that this drug may represent a new strategy for the treatment of prostate cancer.


Assuntos
Neoplasias da Próstata/prevenção & controle , Receptor ErbB-2/efeitos dos fármacos , Receptores Androgênicos/efeitos dos fármacos , Rifabutina/análogos & derivados , Rifabutina/farmacologia , Androgênios/fisiologia , Animais , Benzoquinonas , Divisão Celular/efeitos dos fármacos , Regulação para Baixo/efeitos dos fármacos , Feminino , Fase G1/fisiologia , Proteínas de Choque Térmico HSP90/efeitos dos fármacos , Proteínas de Choque Térmico HSP90/metabolismo , Humanos , Lactamas Macrocíclicas , Masculino , Camundongos , Camundongos Nus , Transplante de Neoplasias , Antígeno Prostático Específico/sangue , Antígeno Prostático Específico/efeitos dos fármacos , Neoplasias da Próstata/metabolismo , Neoplasias da Próstata/patologia , Receptor ErbB-2/metabolismo , Receptor ErbB-3/efeitos dos fármacos , Receptor ErbB-3/metabolismo , Receptores Androgênicos/metabolismo , Proteína do Retinoblastoma/fisiologia , Resultado do Tratamento , Células Tumorais Cultivadas , Ensaios Antitumorais Modelo de Xenoenxerto
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