Journal of Structural Biology: X最新文献_第8页

Structural characterization of two solute-binding proteins for N,N′-diacetylchitobiose/N,N′,N′′-triacetylchitotoriose of the gram-positive bacterium, Paenibacillus sp. str. FPU-7 革兰氏阳性菌Paenibacillus sp.str.FPU-7的N，N′-二乙酰壳二糖/N，N′，N′′-三乙酰壳多糖两种溶质结合蛋白的结构表征

IF 2.9

Journal of Structural Biology: X Pub Date : 2021-01-01 DOI: 10.1016/j.yjsbx.2021.100049

Takafumi Itoh, Misaki Yaguchi, Akari Nakaichi, Moe Yoda, Takao Hibi, Hisashi Kimoto

{"title":"Structural characterization of two solute-binding proteins for N,N′-diacetylchitobiose/N,N′,N′′-triacetylchitotoriose of the gram-positive bacterium, Paenibacillus sp. str. FPU-7","authors":"Takafumi Itoh, Misaki Yaguchi, Akari Nakaichi, Moe Yoda, Takao Hibi, Hisashi Kimoto","doi":"10.1016/j.yjsbx.2021.100049","DOIUrl":"https://doi.org/10.1016/j.yjsbx.2021.100049","url":null,"abstract":"<div><p>The chitinolytic bacterium <em>Paenibacillus</em> sp. str. FPU-7 efficiently degrades chitin into oligosaccharides such as <em>N</em>-acetyl-D-glucosamine (GlcNAc) and disaccharides (GlcNAc)<sub>2</sub> through multiple secretory chitinases. Transport of these oligosaccharides by <em>P</em>. str. FPU-7 has not yet been clarified. In this study, we identified <em>nagB1</em>, predicted to encode a sugar solute-binding protein (SBP), which is a component of the ABC transport system. However, the genes next to <em>nagB1</em> were predicted to encode two-component regulatory system proteins rather than transmembrane domains (TMDs). We also identified <em>nagB2</em>, which is highly homologous to <em>nagB1</em>. Adjacent to <em>nagB2</em>, two genes were predicted to encode TMDs. Binding experiments of the recombinant NagB1 and NagB2 to several oligosaccharides using differential scanning fluorimetry and surface plasmon resonance confirmed that both proteins are SBPs of (GlcNAc)<sub>2</sub> and (GlcNAc)<sub>3</sub>. We determined their crystal structures complexed with and without chitin oligosaccharides at a resolution of 1.2 to 2.0 Å. The structures shared typical SBP structural folds and were classified as subcluster D-I. Large domain motions were observed in the structures, suggesting that they were induced by ligand binding via the “Venus flytrap” mechanism. These structures also revealed chitin oligosaccharide recognition mechanisms. In conclusion, our study provides insight into the recognition and transport of chitin oligosaccharides in bacteria.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":"5 ","pages":"Article 100049"},"PeriodicalIF":2.9,"publicationDate":"2021-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.yjsbx.2021.100049","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72114796","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

Structural analysis of missense mutations occurring in the DNA-binding domain of HSF4 associated with congenital cataracts 先天性白内障相关HSF4 dna结合区错义突变的结构分析

IF 2.9

Journal of Structural Biology: X Pub Date : 2020-01-01 DOI: 10.1016/j.yjsbx.2019.100015

Zaiyu Xiao , Ling Guo , Yang Zhang , Liwei Cui , Yujie Dai , Zhu Lan , Qinghua Zhang , Sheng Wang , Wei Liu

{"title":"Structural analysis of missense mutations occurring in the DNA-binding domain of HSF4 associated with congenital cataracts","authors":"Zaiyu Xiao , Ling Guo , Yang Zhang , Liwei Cui , Yujie Dai , Zhu Lan , Qinghua Zhang , Sheng Wang , Wei Liu","doi":"10.1016/j.yjsbx.2019.100015","DOIUrl":"10.1016/j.yjsbx.2019.100015","url":null,"abstract":"<div><p>Congenital cataract (CC) is the major cause of childish blindness, and nearly 50% of CCs are hereditary disorders. HSF4, a member of the heat shock transcription factor family, acts as a key regulator of cell growth and differentiation during the development of sensory organs. Missense mutations in the HSF4-encoding gene have been reported to cause CC formation; in particular, those occurring within the DNA-binding domain (DBD) are usually autosomal dominant mutations. To address how the identified mutations lead to HSF4 malfunction by placing adverse impacts on protein structure and DNA-binding specificity and affinity, we determined two high-resolution structures of the wild-type DBD and the K23N mutant of human HSF4, built DNA-binding models, conducted <em>in silico</em> mutations and molecular dynamics simulations. Our analysis suggests four possible structural mechanisms underlining the missense mutations in HSF4-DBD and cataractogenesis: (i), disruption of HSE recognition; (ii), perturbation of protein-DNA interactions; (iii), alteration of protein folding; (iv), other impacts, e.g. inhibition of protein oligomerization.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":"4 ","pages":"Article 100015"},"PeriodicalIF":2.9,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.yjsbx.2019.100015","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38137263","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: 5

FMN riboswitch aptamer symmetry facilitates conformational switching through mutually exclusive coaxial stacking configurations FMN核开关适体对称通过互斥的同轴堆叠结构促进构象切换

IF 2.9

Journal of Structural Biology: X Pub Date : 2020-01-01 DOI: 10.1016/j.yjsbx.2020.100035

Haley M. Wilt , Ping Yu , Kemin Tan , Yun-Xing Wang , Jason R. Stagno

{"title":"FMN riboswitch aptamer symmetry facilitates conformational switching through mutually exclusive coaxial stacking configurations","authors":"Haley M. Wilt , Ping Yu , Kemin Tan , Yun-Xing Wang , Jason R. Stagno","doi":"10.1016/j.yjsbx.2020.100035","DOIUrl":"10.1016/j.yjsbx.2020.100035","url":null,"abstract":"<div><p>Knowledge of both apo and holo states of riboswitches aid in elucidating the various mechanisms of ligand-induced conformational “switching” that underpin their gene-regulating capabilities. Previous structural studies on the flavin mononucleotide (FMN)-binding aptamer of the FMN riboswitch, however, have revealed minimal conformational changes associated with ligand binding that do not adequately explain the basis for the switching behavior. We have determined a 2.7-Å resolution crystal structure of the ligand-free FMN riboswitch aptamer that is distinct from previously reported structures, particularly in the conformation and orientation of the P1 and P4 helices. The nearly symmetrical tertiary structure provides a mechanism by which one of two pairs of adjacent helices (P3/P4 or P1/P6) undergo collinear stacking in a mutually exclusive manner, in the absence or presence of ligand, respectively. Comparison of these structures suggests the stem-loop that includes P4 and L4 is important for maintaining a global conformational state that, in the absence of ligand, disfavors formation of the P1 regulatory helix. Together, these results provide further insight to the structural basis for conformational switching of the FMN riboswitch.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":"4 ","pages":"Article 100035"},"PeriodicalIF":2.9,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.yjsbx.2020.100035","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38529452","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: 9

In situ structural analysis of the flagellum attachment zone in Trypanosoma brucei using cryo-scanning transmission electron tomography 应用冷冻扫描透射电子断层扫描技术对布氏锥虫鞭毛附着区的原位结构分析

IF 2.9

Journal of Structural Biology: X Pub Date : 2020-01-01 DOI: 10.1016/j.yjsbx.2020.100033

Sylvain Trépout

{"title":"In situ structural analysis of the flagellum attachment zone in Trypanosoma brucei using cryo-scanning transmission electron tomography","authors":"Sylvain Trépout","doi":"10.1016/j.yjsbx.2020.100033","DOIUrl":"https://doi.org/10.1016/j.yjsbx.2020.100033","url":null,"abstract":"<div><p>The flagellum of <em>Trypanosoma brucei</em> is a 20 µm-long organelle responsible for locomotion and cell morphogenesis. The flagellum attachment zone (FAZ) is a multi-protein complex whose function is to attach the flagellum to the cell body but also to guide cytokinesis. Cryo-transmission electron microscopy is a tool of choice to access the structure of the FAZ in a close-to-native state. However, because of the large dimension of the cell body, the whole FAZ cannot be structurally studied <em>in situ</em> at the nanometre scale in 3D using classical transmission electron microscopy approaches. In the present work, cryo-scanning transmission electron tomography, a new method capable of investigating cryo-fixed thick biological samples, has been used to study whole <em>T. brucei</em> cells at the bloodstream stage. The method has been used to visualise and characterise the structure and organisation of the FAZ filament. It is composed of an array of cytoplasmic stick-like structures. These sticks are heterogeneously distributed between the posterior part and the anterior tip of the cell. This cryo-STET investigation provides new insights into the structure of the FAZ filament. In combination with protein structure predictions, this work proposes a new model for the elongation of the FAZ.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":"4 ","pages":"Article 100033"},"PeriodicalIF":2.9,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.yjsbx.2020.100033","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72113477","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: 9

Specificity and regulation of phosphotyrosine signaling through SH2 domains 磷酸化酪氨酸信号通过SH2结构域的特异性和调控

IF 2.9

Journal of Structural Biology: X Pub Date : 2020-01-01 DOI: 10.1016/j.yjsbx.2020.100026

Michelangelo Marasco , Teresa Carlomagno

引用次数: 17

Essential role of calcium in extending RTX adhesins to their target 钙在将RTX粘连蛋白延伸到其靶标中的重要作用

IF 2.9

Journal of Structural Biology: X Pub Date : 2020-01-01 DOI: 10.1016/j.yjsbx.2020.100036

Tyler D.R. Vance , Qilu Ye, Brigid Conroy, Peter L. Davies

{"title":"Essential role of calcium in extending RTX adhesins to their target","authors":"Tyler D.R. Vance , Qilu Ye, Brigid Conroy, Peter L. Davies","doi":"10.1016/j.yjsbx.2020.100036","DOIUrl":"10.1016/j.yjsbx.2020.100036","url":null,"abstract":"<div><p>RTX adhesins are long, multi-domain proteins present on the outer membrane of many Gram-negative bacteria. From this vantage point, adhesins use their distal ligand-binding domains for surface attachment leading to biofilm formation. To expand the reach of the ligand-binding domains, RTX adhesins maintain a central extender region of multiple tandem repeats, which makes up most of the proteins’ large molecular weight. Alignments of the 10-15-kDa extender domains show low sequence identity between adhesins. Here we have produced and structurally characterized protein constructs of four tandem repeats (tetra-tandemers) from two different RTX adhesins. In comparing the tetra-tandemers to each other and already solved structures from <em>Marinomonas primoryensis</em> and <em>Salmonella enterica</em>, the extender domains fold as diverse beta-sandwich structures with widely differing calcium contents. However, all the tetra-tandemers have at least one calcium ion coordinated in the linker region between beta-sandwich domains whose role appears to be the rigidification of the extender region to help the adhesin extend its reach.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":"4 ","pages":"Article 100036"},"PeriodicalIF":2.9,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.yjsbx.2020.100036","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38426633","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: 4

High resolution CryoEM structure of the ring-shaped virulence factor EspB from Mycobacterium tuberculosis 结核分枝杆菌环状毒力因子EspB的高分辨率CryoEM结构

IF 2.9

Journal of Structural Biology: X Pub Date : 2020-01-01 DOI: 10.1016/j.yjsbx.2020.100029

Jérémie Piton , Florence Pojer , Soichi Wakatsuki , Cornelius Gati , Stewart T. Cole

{"title":"High resolution CryoEM structure of the ring-shaped virulence factor EspB from Mycobacterium tuberculosis","authors":"Jérémie Piton , Florence Pojer , Soichi Wakatsuki , Cornelius Gati , Stewart T. Cole","doi":"10.1016/j.yjsbx.2020.100029","DOIUrl":"https://doi.org/10.1016/j.yjsbx.2020.100029","url":null,"abstract":"<div><p>The EspB protein of <em>Mycobacterium tuberculosis</em> is a 60 kDa virulence factor, implicated in conjugation and exported by the ESX-1 system of which it may also be a component. Previous attempts to obtain high-resolution maps of EspB by cryo-electron microscopic examination of single particles have been thwarted by severe orientation bias of the particles. This was overcome by using detergent as a surfactant thereby allowing reconstruction of the EspB structure at 3.37 Å resolution. The final structure revealed the N-terminal domain of EspB to be organized as a cylindrical heptamer with dimensions of 90 Å x 90 Å and a central channel of 45 Å diameter whereas the C-terminal domain was unstructured. New atomic insight was obtained into the helical packing required for protomer interactions and the overall electrostatic potential. The external surface is electronegatively charged while the channel is lined with electropositive patches. EspB thus has many features of a pore-like transport protein that might allow the passage of an ESX-1 substrate such as the 35 Å diameter EsxA-EsxB heterodimer or B-form DNA consistent with its proposed role in DNA uptake.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":"4 ","pages":"Article 100029"},"PeriodicalIF":2.9,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.yjsbx.2020.100029","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72076018","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: 17

In crystallo-screening for discovery of human norovirus 3C-like protease inhibitors 人诺如病毒3C样蛋白酶抑制剂的晶体内筛选

IF 2.9

Journal of Structural Biology: X Pub Date : 2020-01-01 DOI: 10.1016/j.yjsbx.2020.100031

Jingxu Guo , Alice Douangamath , Weixiao Song , Alun R. Coker , A.W. Edith Chan , Steve P. Wood , Jonathan B. Cooper , Efrat Resnick , Nir London , Frank von Delft

{"title":"In crystallo-screening for discovery of human norovirus 3C-like protease inhibitors","authors":"Jingxu Guo , Alice Douangamath , Weixiao Song , Alun R. Coker , A.W. Edith Chan , Steve P. Wood , Jonathan B. Cooper , Efrat Resnick , Nir London , Frank von Delft","doi":"10.1016/j.yjsbx.2020.100031","DOIUrl":"https://doi.org/10.1016/j.yjsbx.2020.100031","url":null,"abstract":"<div><p>Outbreaks of human epidemic nonbacterial gastroenteritis are mainly caused by noroviruses. Viral replication requires a 3C-like cysteine protease (3CL<sup>pro</sup>) which processes the 200 kDa viral polyprotein into six functional proteins. The 3CL<sup>pro</sup> has attracted much interest due to its potential as a target for antiviral drugs. A system for growing high-quality crystals of native Southampton norovirus 3CL<sup>pro</sup> (SV3CP) has been established, allowing the ligand-free crystal structure to be determined to 1.3 Å in a tetrameric state. This also allowed crystal-based fragment screening to be performed with various compound libraries, ultimately to guide drug discovery for SV3CP. A total of 19 fragments were found to bind to the protease out of the 844 which were screened. Two of the hits were located at the active site of SV3CP and showed good inhibitory activity in kinetic assays. Another 5 were found at the enzyme’s putative RNA-binding site and a further 11 were located in the symmetric central cavity of the tetramer.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":"4 ","pages":"Article 100031"},"PeriodicalIF":2.9,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.yjsbx.2020.100031","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72076019","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: 2

Measurement of local resolution in electron tomography 电子断层扫描局部分辨率的测量

IF 2.9

Journal of Structural Biology: X Pub Date : 2020-01-01 DOI: 10.1016/j.yjsbx.2019.100016

J.L. Vilas , J. Oton , C. Messaoudi , R. Melero , P. Conesa , E. Ramirez-Aportela , J. Mota , M. Martinez , A. Jimenez , R. Marabini , J.M. Carazo , J. Vargas , C.O.S. Sorzano

{"title":"Measurement of local resolution in electron tomography","authors":"J.L. Vilas , J. Oton , C. Messaoudi , R. Melero , P. Conesa , E. Ramirez-Aportela , J. Mota , M. Martinez , A. Jimenez , R. Marabini , J.M. Carazo , J. Vargas , C.O.S. Sorzano","doi":"10.1016/j.yjsbx.2019.100016","DOIUrl":"10.1016/j.yjsbx.2019.100016","url":null,"abstract":"<div><p>Resolution (global and local) is one of the most reported metrics of quality measurement in Single Particle Analysis (SPA). However, in electron tomography, the situation is different and its computation is not straightforward. Typically, resolution estimation is global and, therefore, reduces the assessment of a whole tomogram to a single number. However, it is known that tomogram quality is spatially variant. Still, up to our knowledge, a method to estimate local quality metrics in tomography is lacking. This work introduces <em>MonoTomo</em>, a method developed to estimate locally in a tomogram the highest reliable frequency component, expressed as a form of local resolution. The fundamentals lie in a local analysis of the density map via monogenic signals, which, in analogy to <em>MonoRes</em>, allows for local estimations. Results with experimental data show that the local resolution range that MonoTomo casts agrees with reported resolution values for experimental data sets, with the advantage of providing a local estimation. A range of applications of <em>MonoTomo</em> are suggested for further exploration.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":"4 ","pages":"Article 100016"},"PeriodicalIF":2.9,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.yjsbx.2019.100016","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38137262","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: 11

Small angle X-ray scattering and molecular dynamic simulations provide molecular insight for stability of recombinant human transferrin 小角度x射线散射和分子动力学模拟为重组人转铁蛋白的稳定性提供了分子视角

IF 2.9

Journal of Structural Biology: X Pub Date : 2020-01-01 DOI: 10.1016/j.yjsbx.2019.100017

Alina Kulakova , Sowmya Indrakumar , Pernille Sønderby , Lorenzo Gentiluomo , Werner Streicher , Dierk Roessner , Wolfgang Frieß , Günther H.J. Peters , Pernille Harris

{"title":"Small angle X-ray scattering and molecular dynamic simulations provide molecular insight for stability of recombinant human transferrin","authors":"Alina Kulakova , Sowmya Indrakumar , Pernille Sønderby , Lorenzo Gentiluomo , Werner Streicher , Dierk Roessner , Wolfgang Frieß , Günther H.J. Peters , Pernille Harris","doi":"10.1016/j.yjsbx.2019.100017","DOIUrl":"10.1016/j.yjsbx.2019.100017","url":null,"abstract":"<div><p>Transferrin is an attractive candidate for drug delivery due to its ability to cross the blood brain barrier. However, in order to be able to use it for therapeutic purposes, it is important to investigate how its stability depends on different formulation conditions. Combining high-throughput thermal and chemical denaturation studies with small angle X-ray scattering (SAXS) and molecular dynamics (MD) simulations, it was possible to connect the stability of transferrin with its conformational changes. Lowering pH induces opening of the transferrin N-lobe, which results in a negative effect on the stability. Presence of NaCl or arginine at low pH enhances the opening and has a negative impact on the overall protein stability.</p></div><div><h3>Statement of Significance</h3><p>Protein-based therapeutics have become an essential part of medical treatment. They are highly specific, have high affinity and fewer off-target effects. However, stabilization of proteins is critical, time-consuming, and expensive, and it is not yet possible to predict the behavior of proteins under different conditions. The current work is focused on a molecular understanding of the stability of human serum transferrin; a protein which is abundant in blood serum, may pass the blood brain barrier and therefore with high potential in drug delivery. Combination of high throughput unfolding techniques and structural studies, using small angle X-ray scattering and molecular dynamic simulations, allows us to understand the behavior of transferrin on a molecular level.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":"4 ","pages":"Article 100017"},"PeriodicalIF":2.9,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.yjsbx.2019.100017","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38137264","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: 10