为解决由于无人机视角下毛竹林的形状和纹理复杂,现有方法在分割精度和鲁棒性方面表现不佳的问题,提出了一种应用跨领域适应和偏移量引导的毛竹林分割网络——BFSNet。以百山祖国家公园为试验区,利用无人机拍摄周边毛竹林图像构建数据...为解决由于无人机视角下毛竹林的形状和纹理复杂,现有方法在分割精度和鲁棒性方面表现不佳的问题,提出了一种应用跨领域适应和偏移量引导的毛竹林分割网络——BFSNet。以百山祖国家公园为试验区,利用无人机拍摄周边毛竹林图像构建数据集。为增强模型的特征提取能力,提出跨领域适应模块以有效利用源模型的强特征提取能力,并结合自主学习提取适用于毛竹林分割任务的特征,利用两者的优势进行互补。为提高模型对于不同形状毛竹林的识别和定位能力,结合可变形卷积的偏移量引导模块,引入可学习的偏移量参数,以适应不同形状的毛竹林目标。将BFSNet在DeepGlobe Land Cover Classification Challenge和自制数据集上进行模型训练和测试,并与多种主流图像分割方法进行对比。结果表明:BFSNet在交并比、Dice系数、精确率和召回率4项指标上均取得了最优的性能表现,分别获得了76.04%和71.93%的交并比。与多种主流的图像分割模型相比,BFSNet在毛竹林的分割效果方面表现最为出色,对毛竹林形状的精确建模能力能够有效地应对不同形态的毛竹林。展开更多
GEMIN5 is a predominantly cytoplasmic multifunctional protein, known to be involved in recognizing snRNAs through its WD40 repeats domain placed at the N-terminus. A dimerization domain in the middle region acts as a ...GEMIN5 is a predominantly cytoplasmic multifunctional protein, known to be involved in recognizing snRNAs through its WD40 repeats domain placed at the N-terminus. A dimerization domain in the middle region acts as a hub for protein–protein interaction, while a non-canonical RNA-binding site is placed towards the C-terminus. The singular organization of structural domains present in GEMIN5 enables this protein to perform multiple functions through its ability to interact with distinct partners, both RNAs and proteins. This protein exerts a different role in translation regulation depending on its physiological state, such that while GEMIN5 down-regulates global RNA translation, the C-terminal half of the protein promotes translation of its mRNA. Additionally, GEMIN5 is responsible for the preferential partitioning of mRNAs into polysomes. Besides selective translation, GEMIN5 forms part of distinct ribonucleoprotein complexes, reflecting the dynamic organization of macromolecular complexes in response to internal and external signals. In accordance with its contribution to fundamental cellular processes, recent reports described clinical loss of function mutants suggesting that GEMIN5 deficiency is detrimental to cell growth and survival. Remarkably, patients carrying GEMIN5 biallelic variants suffer from neurodevelopmental delay, hypotonia, and cerebellar ataxia. Molecular analyses of individual variants, which are defective in protein dimerization, display decreased levels of ribosome association, reinforcing the involvement of the protein in translation regulation. Importantly, the number of clinical variants and the phenotypic spectrum associated with GEMIN5 disorders is increasing as the knowledge of the protein functions and the pathways linked to its activity augments. Here we discuss relevant advances concerning the functional and structural features of GEMIN5 and its separate domains in RNA-binding, protein interactome, and translation regulation, and how these data can help to understand the involvement of protein malfunction in clinical variants found in patients developing neurodevelopmental disorders.展开更多
文摘为解决由于无人机视角下毛竹林的形状和纹理复杂,现有方法在分割精度和鲁棒性方面表现不佳的问题,提出了一种应用跨领域适应和偏移量引导的毛竹林分割网络——BFSNet。以百山祖国家公园为试验区,利用无人机拍摄周边毛竹林图像构建数据集。为增强模型的特征提取能力,提出跨领域适应模块以有效利用源模型的强特征提取能力,并结合自主学习提取适用于毛竹林分割任务的特征,利用两者的优势进行互补。为提高模型对于不同形状毛竹林的识别和定位能力,结合可变形卷积的偏移量引导模块,引入可学习的偏移量参数,以适应不同形状的毛竹林目标。将BFSNet在DeepGlobe Land Cover Classification Challenge和自制数据集上进行模型训练和测试,并与多种主流图像分割方法进行对比。结果表明:BFSNet在交并比、Dice系数、精确率和召回率4项指标上均取得了最优的性能表现,分别获得了76.04%和71.93%的交并比。与多种主流的图像分割模型相比,BFSNet在毛竹林的分割效果方面表现最为出色,对毛竹林形状的精确建模能力能够有效地应对不同形态的毛竹林。
基金partially supported by grants PID2020-115096RB-I00 and PID2023-148273NB-I00 from Ministerio de Ciencia y Universidad (MICIU/AEI)(to EMS)。
文摘GEMIN5 is a predominantly cytoplasmic multifunctional protein, known to be involved in recognizing snRNAs through its WD40 repeats domain placed at the N-terminus. A dimerization domain in the middle region acts as a hub for protein–protein interaction, while a non-canonical RNA-binding site is placed towards the C-terminus. The singular organization of structural domains present in GEMIN5 enables this protein to perform multiple functions through its ability to interact with distinct partners, both RNAs and proteins. This protein exerts a different role in translation regulation depending on its physiological state, such that while GEMIN5 down-regulates global RNA translation, the C-terminal half of the protein promotes translation of its mRNA. Additionally, GEMIN5 is responsible for the preferential partitioning of mRNAs into polysomes. Besides selective translation, GEMIN5 forms part of distinct ribonucleoprotein complexes, reflecting the dynamic organization of macromolecular complexes in response to internal and external signals. In accordance with its contribution to fundamental cellular processes, recent reports described clinical loss of function mutants suggesting that GEMIN5 deficiency is detrimental to cell growth and survival. Remarkably, patients carrying GEMIN5 biallelic variants suffer from neurodevelopmental delay, hypotonia, and cerebellar ataxia. Molecular analyses of individual variants, which are defective in protein dimerization, display decreased levels of ribosome association, reinforcing the involvement of the protein in translation regulation. Importantly, the number of clinical variants and the phenotypic spectrum associated with GEMIN5 disorders is increasing as the knowledge of the protein functions and the pathways linked to its activity augments. Here we discuss relevant advances concerning the functional and structural features of GEMIN5 and its separate domains in RNA-binding, protein interactome, and translation regulation, and how these data can help to understand the involvement of protein malfunction in clinical variants found in patients developing neurodevelopmental disorders.
