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303 results on '"Wang, Luwen"'

8. Bioinspired soft robots for deep-sea exploration

Author

Li, Guorui, Wong, Tuck-Whye, Shih, Benjamin, Guo, Chunyu, Wang, Luwen, Liu, Jiaqi, Wang, Tao, Liu, Xiaobo, Yan, Jiayao, Wu, Baosheng, Yu, Fajun, Chen, Yunsai, Liang, Yiming, Xue, Yaoting, Wang, Chengjun, He, Shunping, Wen, Li, Tolley, Michael T., Zhang, A-Man, Laschi, Cecilia, and Li, Tiefeng

Published
2023
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10. Female urinary incontinence in China after 15 years’ efforts: Results from large-scale nationwide surveys

Author

Zhu, Jiming, Pang, Haiyu, Wang, Peicheng, Chen, Yanhua, Li, Huihui, Liu, Qing, Wang, Luwen, Jin, Hangmei, Gong, Liyan, Xie, Jingyan, Lai, Ting, Li, Aiyang, Liu, Lubin, Yan, Mengsha, Zhou, Lifei, Luan, Yanqiu, Wang, Lin, Li, Xiaoli, Luo, Xiping, Fu, Yingjie, Niu, Jumin, Zhao, Wen, Liu, Qiming, Zhao, Renfeng, Lou, Wenjia, Morse, Abraham N., Yin, Jiahui, Dang, Le, Yang, Hua, Li, Liming, Lv, Jun, and Zhu, Lan

Published
2024
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12. FAM222A encodes a protein which accumulates in plaques in Alzheimer's disease.

Author

Yan, Tingxiang, Liang, Jingjing, Gao, Ju, Wang, Luwen, Fujioka, Hisashi, Alzheimer Disease Neuroimaging Initiative, Zhu, Xiaofeng, and Wang, Xinglong

Subjects
Alzheimer Disease Neuroimaging Initiative, Brain, Animals, Mice, Transgenic, Humans, Mice, Alzheimer Disease, Disease Models, Animal, Atrophy, Genetic Predisposition to Disease, Nerve Tissue Proteins, Polymorphism, Single Nucleotide, Aged, Aged, 80 and over, Middle Aged, Female, Male, Genome-Wide Association Study, Amyloid beta-Peptides, Plaque, Amyloid, Amyloidogenic Proteins, Datasets as Topic, Protein Aggregation, Pathological, Cognitive Dysfunction
Abstract

Alzheimer's disease (AD) is characterized by amyloid plaques and progressive cerebral atrophy. Here, we report FAM222A as a putative brain atrophy susceptibility gene. Our cross-phenotype association analysis of imaging genetics indicates a potential link between FAM222A and AD-related regional brain atrophy. The protein encoded by FAM222A is predominantly expressed in the CNS and is increased in brains of patients with AD and in an AD mouse model. It accumulates within amyloid deposits, physically interacts with amyloid-β (Aβ) via its N-terminal Aβ binding domain, and facilitates Aβ aggregation. Intracerebroventricular infusion or forced expression of this protein exacerbates neuroinflammation and cognitive dysfunction in an AD mouse model whereas ablation of this protein suppresses the formation of amyloid deposits, neuroinflammation and cognitive deficits in the AD mouse model. Our data support the pathological relevance of protein encoded by FAM222A in AD.

Published
2020

43. Author Correction: FAM222A encodes a protein which accumulates in plaques in Alzheimer’s disease (Nature Communications, (2020), 11, 1, (411), 10.1038/s41467-019-13962-0)

Author

Yan, Tingxiang, Liang, Jingjing, Gao, Ju, Wang, Luwen, Fujioka, Hisashi, Weiner, Michael W., Schuff, Norbert, Rosen, Howard J., Miller, Bruce L., Perry, David, Aisen, Paul, Toga, Arthur W., Jimenez, Gustavo, Donohue, Michael, Gessert, Devon, Harless, Kelly, Salazar, Jennifer, Cabrera, Yuliana, Walter, Sarah, Hergesheimer, Lindsey, Crawford, Karen, Neu, Scott, Schneider, Lon S., Pawluczyk, Sonia, Becerra, Mauricio, Teodoro, Liberty, Spann, Bryan M., Petersen, Ronald, and Finger, Elizabeth

Abstract

In the original version of the manuscript, the image shown in Figure 4g, bottom row (Aβ1–42 + rAggregatin), under “6h” was incorrect. This image incorrectly showed the same sample as shown in the original Figure 4g, top row (Aβ1–42), under “0.5h”. The correct version of figure 4g is as follows: (Figure presented.) which replaces the previous incorrect version: (Figure presented.).

Published
2022

45. The inhibition of TDP-43 mitochondrial localization blocks its neuronal toxicity

Author

Wang, Wenzhang, Wang, Luwen, Lu, Junjie, Siedlak, Sandra L., Fujioka, Hisashi, Liang, Jingjing, Jiang, Sirui, Ma, Xiaopin, Jiang, Zhen, da Rocha, Edroaldo Lummertz, Sheng, Max, Choi, Heewon, Lerou, Paul H., Li, Hu, and Wang, Xinglong

Subjects
Gene mutations -- Health aspects, Binding proteins -- Properties, Gene expression -- Health aspects, Nervous system -- Degeneration, Molecular targeted therapy -- Innovations, Biological sciences, Health
Abstract

Genetic mutations in TAR DNA-binding protein 43 (TARDBP, also known as TDP-43) cause amyotrophic lateral sclerosis (ALS), and an increase in the presence of TDP-43 (encoded by TARDBP) in the cytoplasm is a prominent histopathological feature of degenerating neurons in various neurodegenerative diseases. However, the molecular mechanisms by which TDP-43 contributes to ALS pathophysiology remain elusive. Here we have found that TDP-43 accumulates in the mitochondria of neurons in subjects with ALS or frontotemporal dementia (FTD). Disease-associated mutations increase TDP-43 mitochondrial localization. In mitochondria, wild-type (WT) and mutant TDP-43 preferentially bind mitochondria- transcribed messenger RNAs (mRNAs) encoding respiratory complex I subunits ND3 and ND6, impair their expression and specifically cause complex I disassembly. The suppression of TDP-43 mitochondrial localization abolishes WT and mutant TDP-43- induced mitochondrial dysfunction and neuronal loss, and improves phenotypes of transgenic mutant TDP-43 mice. Thus, our studies link TDP-43 toxicity directly to mitochondrial bioenergetics and propose the targeting of TDP-43 mitochondrial localization as a promising therapeutic approach for neurodegeneration., ALS is the most common motor disease characterized by progressive motor neuron degeneration in the brain stem and spinal cord (1), and FTD is the second-most common form of early-onset [...]

Published
2016
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