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| 1 | The endosomal-lysosomal system: from acidification and cargo sorting to neurodegeneration显示文摘The endosomal-lysosomal system is made up of a set of intracellular membranous compartments that dynamically interconvert,which is comprised of early endosomes,recycling endosomes,late endosomes,and the lysosome.In addition,autophagosomes execute autophagy,which delivers intracellular contents to the lysosome.Maturation of endosomes and/or autophagosomes into a lysosome creates an unique acidic environment within the cell for proteolysis and recycling of unneeded cellular components into usable amino acids and other biomolecular building blocks.In the endocytic pathway,gradual maturation of endosomes into a lysosome and acidification of the late endosome are accompanied by vesicle trafficking,protein sorting and targeted degradation of some sorted cargo.Two opposing sorting systems are operating in these processes:the endosomal sorting complex required for transport(ESCRT)supports targeted degradation and the retromer supports retrograde retrieval of certain cargo.The endosomal-lysosomal system is emerging as a central player in a host of neurodegenerative diseases,demonstrating potential roles which are likely to be revealed in pathogenesis and for viable therapeutic strategies.Here we focus on the physiological process of endosomal-lysosomal maturation,acidification and sorting systems along the endocytic pathway,and further discuss relationships between abnormalities in the endosomal-lysosomal system and neurodegenerative diseases,especially Alzheimer’s disease(AD). | Yong-Bo Hu Eric B Dammer Ru-Jing Ren Gang Wang | 2015 | Translational Neurodegeneration2015，4，1： | 4 |
| 2 | Asparaginyl endopeptidase cleaves TDP‐43 in brain显示文摘 | Jeremy H. Herskowitz Yair M. Gozal Duc M. Duong Eric B. Dammer Marla Gearing Keqiang Ye James J. Lah Junmin Peng Allan I. Levey Nicholas T. Seyfried | 2012 | Proteomics . 2012 (15-1)2012，，15： | 1 |
| 3 | Genetic profiles of familial late-onset Alzheimer’s disease in China:The Shanghai FLOAD study显示文摘Compared with early-onset familial AD(FAD),the heritability of most familial lateonset Alzheimer’s disease(FLOAD)cases still remains unclear.However,there are few reported genetic profiles of FLOAD to date.In the present study,targeted sequencing of selected candidate genes was conducted for each of 90 probands with FLOAD and 101 unrelated matched normal controls among Chinese Han population.Results show a significantly lower rate of mutation in APP and PSENs,and APOE e4 genetic risk is higher for FLOAD.Among the Chinese FLOAD population,the most frequent variant was CR1 rs116806486[5.6%,95%CI(1.8%,12.5%)],followed by coding variants of TREM2(4.4%,95%CI(1.2%,10.9%))and novel mutations of ACE[3.3%,95%CI(0.7%,9.4%)].Next,we found that novel pathogenic mutations in ACE including frame-shift and nonsense mutations were in association with FLOAD regardless of APOE e4 status.Evidence from the Alzheimer’s disease Neuroimaging Initiative(ADNI)database also supported this finding in different ethnicities.Results of in vitro analysis suggest that frame-shift and nonsense mutations in ACE may be involved in LOAD through decreased ACE protein levels without affecting direct processing of APP. | Xin-Yi Xie Qian-Hua Zhao Qiang Huang a Eric Dammer Sheng-di Chen Ru-Jing Ren Gang Wang the Alzheimer’s Disease Neuroimaging Initiative | 2022 | Genes & Diseases2022，9，6： | 1 |
| 4 | Proteomics of protein post-translational modifications implicated in neurodegeneration显示文摘Mass spectrometry(MS)-based proteomics has developed into a battery of approaches that is exceedingly adept at identifying with high mass accuracy and precision any of the following:oxidative damage to proteins(redox proteomics),phosphorylation(phosphoproteomics),ubiquitination(diglycine remnant proteomics),protein fragmentation(degradomics),and other posttranslational modifications(PTMs).Many studies have linked these PTMs to pathogenic mechanisms of neurodegeneration.To date,identifying PTMs on specific pathology-associated proteins has proven to be a valuable step in the evaluation of functional alteration of proteins and also elucidates biochemical and structural explanations for possible pathophysiological mechanisms of neurodegenerative diseases.This review provides an overview of methods applicable to the identification and quantification of PTMs on proteins and enumerates historic,recent,and potential future research endeavours in the field of proteomics furthering the understanding of PTM roles in the pathogenesis of neurodegeneration. | Ru-Jing Ren Eric B Dammer Gang Wang Nicholas T Seyfried Allan I Levey | 2014 | Translational Neurodegeneration2014，3，1： | 1 |
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