Jacobs journal of molecular and translational medicine最新文献_第4页

The Role of Mast Cells in the Pathophysiology of Pulmonary Fibrosis 肥大细胞在肺纤维化病理生理中的作用

Jacobs journal of molecular and translational medicine Pub Date : 2018-11-11 DOI: 10.1007/978-3-319-98143-7_6

C. Shimbori, C. Upagupta, Paul Forsythe, Paul Forsythe, M. Kolb

引用次数: 0

Tipping the Balance from Angiogenesis to Fibrosis in Chronic Kidney Disease 慢性肾脏疾病从血管生成到纤维化的失衡

Jacobs journal of molecular and translational medicine Pub Date : 2018-11-11 DOI: 10.1007/978-3-319-98143-7_16

Y. Hirakawa, Tetsuhiro Tanaka, M. Nangaku

引用次数: 1

Dynamic Reciprocity: The Role of the Extracellular Matrix Microenvironment in Amplifying and Sustaining Pathological Lung Fibrosis 动态互易:细胞外基质微环境在放大和维持病理性肺纤维化中的作用

Jacobs journal of molecular and translational medicine Pub Date : 2018-11-11 DOI: 10.1007/978-3-319-98143-7_9

J. Burgess, K. Muizer, C. Brandsma, Hilde Heijink

引用次数: 3

Probing of Amyloid Aβ (14-23) Trimers by Single-Molecule Force Spectroscopy. 单分子力谱法探测淀粉样蛋白Aβ(14-23)三聚体

Jacobs journal of molecular and translational medicine Pub Date : 2016-02-01 Epub Date: 2015-06-09

Sibaprasad Maity, Yuri L Lyubchenko

{"title":"Probing of Amyloid Aβ (14-23) Trimers by Single-Molecule Force Spectroscopy.","authors":"Sibaprasad Maity, Yuri L Lyubchenko","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Self-assembly and aggregation of amyloid peptides, such as Aβ(1-40) and Aβ(1-42), lead to the development of Alzheimer disease and similar neurodegenerative disorders associated with protein aggregation. The structures of large aggregates, specifically fibrils, are well characterized. However, our understanding about the structure of oligomeric forms of amyloids is incomplete and needs to be expanded, particularly given the finding that oligomeric rather than fibrillar amyloid morphologies are neurotoxic. This lack of knowledge is primarily due to the existence of transient oligomeric forms that require the use of non-traditional approaches capable of probing transiently existing amyloid forms. We have recently developed the Single-Molecule Force Spectroscopy (SMFS) approach enabling us to probe dimeric forms of amyloids. These studies suggest that the assembly of amyloid proteins into dimers leads to extremely stabilized amyloids in non-native, misfolded states [1]. Herein, we applied the SMFS approach to probe amyloid trimers. We used the Aβ(14-23) segment of Aβ42 protein that is responsible for full-size protein aggregation. The dimerization of this peptide was recently characterized [2]. The dimeric form of Aβ (14-23) was assembled by the use of a tandem Aβ(14-23)-YNGK-Aβ(14-23), in which the YNGK motif between the two Aβ(14-23) monomers makes a β turn to form a hairpin loop with an antiparallel arrangement of Aβ(14-23) monomers[3]. The Aβ(14-23) monomer was tethered to the AFM tip, and trimers were formed by approaching the tip to the mica surface on which the Aβ(14-23)-YNGK-Aβ(14-23) dimer was immobilized via a polyethylene glycol tether. We identified trimers by rupture forces that were considerably larger than those for dimers. Models for the trimer assembly process are discussed.</p>","PeriodicalId":91893,"journal":{"name":"Jacobs journal of molecular and translational medicine","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2016-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5321571/pdf/nihms797190.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"34766302","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0