Channels (Austin, Tex.)最新文献

{"title":"Regulatory mechanisms of mitochondrial BK_Ca channels.","authors":"Ana L González-Cota, Carmen Santana-Calvo, Rocío Servín-Vences, Gerardo Orta, Enrique Balderas","doi":"10.1080/19336950.2021.1919463","DOIUrl":"10.1080/19336950.2021.1919463","url":null,"abstract":"<p><p>The mitochondrial BK_Ca channel (mitoBK_Ca) is a splice variant of plasma membrane BK_Ca (Maxi-K, BK_Ca, Slo1, K_Ca1.1). While a high-resolution structure of mitoBK_Ca is not available yet, functional and structural studies of the plasma membrane BK_Ca have provided important clues on the gating of the channel by voltage and Ca²⁺, as well as the interaction with auxiliary subunits. To date, we know that the control of expression of mitoBK_Ca, targeting and voltage-sensitivity strongly depends on its association with its regulatory β1-subunit, which overall participate in the control of mitochondrial Ca²⁺-overload in cardiac myocytes. Moreover, novel regulatory mechanisms of mitoBK_Ca such as β-subunits and amyloid-β have recently been proposed. However, major basic questions including how the regulatory BK_Ca-β1-subunit reaches mitochondria and the mechanism through which amyloid-β impairs mitoBK_Ca channel function remain to be addressed.</p>","PeriodicalId":72555,"journal":{"name":"Channels (Austin, Tex.)","volume":" ","pages":"424-437"},"PeriodicalIF":0.0,"publicationDate":"2021-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8117780/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38954825","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}

{"title":"Changes in peripheral HCN2 channels during persistent inflammation.","authors":"L-A R Jansen, L A Forster, X L Smith, M Rubaharan, A Z Murphy, D J Baro","doi":"10.1080/19336950.2020.1870086","DOIUrl":"10.1080/19336950.2020.1870086","url":null,"abstract":"<p><p>Nociceptor sensitization following nerve injury or inflammation leads to chronic pain. An increase in the nociceptor hyperpolarization-activated current, I_h, is observed in many models of pathological pain. Pharmacological blockade of I_h prevents the mechanical and thermal hypersensitivity that occurs during pathological pain. Alterations in the Hyperpolarization-activated Cyclic Nucleotide-gated ion channel 2 (HCN2) mediate I_h-dependent thermal and mechanical hyperalgesia. Limited knowledge exists regarding the nature of these changes during chronic inflammatory pain. Modifications in HCN2 expression and post-translational SUMOylation have been observed in the Complete Freund's Adjuvant (CFA) model of chronic inflammatory pain. Intra-plantar injection of CFA into the rat hindpaw induces unilateral hyperalgesia that is sustained for up to 14 days following injection. The hindpaw is innervated by primary afferents in lumbar DRG, L4-6. Adjustments in HCN2 expression and SUMOylation have been well-documented for L5 DRG during the first 7 days of CFA-induced inflammation. Here, we examine bilateral L4 and L6 DRG at day 1 and day 3 post-CFA. Using L4 and L6 DRG cryosections, HCN2 expression and SUMOylation were measured with immunohistochemistry and proximity ligation assays, respectively. Our findings indicate that intra-plantar injection of CFA elicited a bilateral increase in HCN2 expression in L4 and L6 DRG at day 1, but not day 3, and enhanced HCN2 SUMOylation in ipsilateral L6 DRG at day 1 and day 3. Changes in HCN2 expression and SUMOylation were transient over this time course. Our study suggests that HCN2 is regulated by multiple mechanisms during CFA-induced inflammation.</p>","PeriodicalId":72555,"journal":{"name":"Channels (Austin, Tex.)","volume":" ","pages":"165-179"},"PeriodicalIF":0.0,"publicationDate":"2021-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/e0/c6/KCHL_15_1870086.PMC7808421.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38801496","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}

{"title":"Bibliometric analysis of nicotinic acetylcholine receptors channel research (2000-2020).","authors":"Xueping Zhu, Yan Zhou, Guozhen Yuan, Jingjing Shi, Shuai Shi, Limei Zhang, Ruoning Chai, Yihang Du, Chenglin Duan, Yuanhui Hu","doi":"10.1080/19336950.2021.1882113","DOIUrl":"10.1080/19336950.2021.1882113","url":null,"abstract":"<p><p>To explore the research status, hotspots, and trends in research on nicotinic acetylcholine receptor (nAChR) channel. The Web of Science core collection database from 2000 to 2020 was used as the data source. The visual analysis software VOSviewer1.6.16 and Citespace5.7 R3 were used to visualize the studies of the nAChR channel. The national/institutional distribution, journal distribution, authors, and related research were discussed. A total of 5,794 articles were obtained. The USA and the Utah System of Higher Education were the most productive country and institution for nAChR channel research. <i>Journal of Biological Chemistry</i> was the most productive journal (212) and the most productive researcher was McIntosh, J. Michael. The first highly co-cited article was \"Refined structure of the nicotinic acetylcholine receptor at 4A resolution.\" The most researched area was neurosciences neurology. The hot spots of nAChR channel research were \"subunit and structure of nAChR,\" \"activation/agonist of nAChR channel,\" and \"Changes in nAChRs With Alzheimer's Disease.\" The top three research frontiers of nAChR channel research were \"neuropathic pain,\" \"neuroinflammation,\" and \"α7 nACHR.\" The study provides a perspective to visualize and analyze hotspots and emerging trends in the nAChR channel.</p>","PeriodicalId":72555,"journal":{"name":"Channels (Austin, Tex.)","volume":" ","pages":"298-309"},"PeriodicalIF":0.0,"publicationDate":"2021-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7901545/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25392010","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}

{"title":"Molecular mechanisms of activation and regulation of ANO1-Encoded Ca²⁺-Activated Cl^- channels.","authors":"M B Hawn,&nbsp;E Akin,&nbsp;H C Hartzell,&nbsp;I A Greenwood,&nbsp;N Leblanc","doi":"10.1080/19336950.2021.1975411","DOIUrl":"10.1080/19336950.2021.1975411","url":null,"abstract":"<p><p>Ca²⁺-activated Cl^- channels (CaCCs) perform a multitude of functions including the control of cell excitability, regulation of cell volume and ionic homeostasis, exocrine and endocrine secretion, fertilization, amplification of olfactory sensory function, and control of smooth muscle cell contractility. CaCCs are the translated products of two members (ANO1 and ANO2, also known as TMEM16A and TMEM16B) of the Anoctamin family of genes comprising ten paralogs. This review focuses on recent progress in understanding the molecular mechanisms involved in the regulation of ANO1 by cytoplasmic Ca²⁺, post-translational modifications, and how the channel protein interacts with membrane lipids and protein partners. After first reviewing the basic properties of native CaCCs, we then present a brief historical perspective highlighting controversies about their molecular identity in native cells. This is followed by a summary of the fundamental biophysical and structural properties of ANO1. We specifically address whether the channel is directly activated by internal Ca²⁺ or indirectly through the intervention of the Ca²⁺-binding protein Calmodulin (CaM), and the structural domains responsible for Ca²⁺- and voltage-dependent gating. We then review the regulation of ANO1 by internal ATP, Calmodulin-dependent protein kinase II-(CaMKII)-mediated phosphorylation and phosphatase activity, membrane lipids such as the phospholipid phosphatidyl-(4,5)-bisphosphate (PIP₂), free fatty acids and cholesterol, and the cytoskeleton. The article ends with a survey of physical and functional interactions of ANO1 with other membrane proteins such as CLCA1/2, inositol trisphosphate and ryanodine receptors in the endoplasmic reticulum, several members of the TRP channel family, and the ancillary Κ⁺ channel β subunits KCNE1/5.</p>","PeriodicalId":72555,"journal":{"name":"Channels (Austin, Tex.)","volume":" ","pages":"569-603"},"PeriodicalIF":0.0,"publicationDate":"2021-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8480199/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39390343","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}

{"title":"Acid-sensing ion channel 3: An analgesic target.","authors":"Jasdip Singh Dulai, Ewan St John Smith, Taufiq Rahman","doi":"10.1080/19336950.2020.1852831","DOIUrl":"10.1080/19336950.2020.1852831","url":null,"abstract":"<p><p>Acid-sensing ion channel 3 (ASIC3) belongs to the epithelial sodium channel/degenerin (ENaC/DEG) superfamily. There are 7 different ASIC subunits encoded by 5 different genes. Most ASIC subunits form trimeric ion channels that upon activation by extracellular protons mediate a transient inward current inducing cellular excitability. ASIC subunits exhibit differential tissue expression and biophysical properties, and the ability of subunits to form homo- and heteromeric trimers further increases the complexity of currents measured and their pharmacological properties. ASIC3 is of particular interest, not only because it exhibits high expression in sensory neurones, but also because upon activation it does not fully inactivate: a transient current is followed by a sustained current that persists during a period of extracellular acidity, i.e. ASIC3 can encode prolonged acidosis as a nociceptive signal. Furthermore, certain mediators sensitize ASIC3 enabling smaller proton concentrations to activate it and other mediators can directly activate the channel at neutral pH. Moreover, there is a plethora of evidence using transgenic mouse models and pharmacology, which supports ASIC3 as being a potential target for development of analgesics. This review will focus on current understanding of ASIC3 function to provide an overview of how ASIC3 contributes to physiology and pathophysiology, examining the mechanisms by which it can be modulated, and highlighting gaps in current understanding and future research directions.</p>","PeriodicalId":72555,"journal":{"name":"Channels (Austin, Tex.)","volume":" ","pages":"94-127"},"PeriodicalIF":0.0,"publicationDate":"2021-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7801124/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38321787","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}

{"title":"Comparison of quinazoline and benzoylpyrazoline chemotypes targeting the CaVα-β interaction as antagonists of the N-type CaV2.2 channel.","authors":"Dongzhi Ran, Kimberly Gomez, Aubin Moutal, Marcel Patek, Samantha Perez-Miller, Rajesh Khanna","doi":"10.1080/19336950.2020.1863595","DOIUrl":"10.1080/19336950.2020.1863595","url":null,"abstract":"<p><p>Structural studies with an α subunit fragment of voltage-gated calcium (CaV) channels in complex with the CaVβ subunits revealed a high homology between the various CaVα-β subunits, predicting that targeting of this interface would result in nonselective compounds. Despite this likelihood, my laboratory initiated a rational structure-based screening campaign focusing on \"hot spots\" on the alpha interacting domain (AID) of the CaVβ2a subunits and identified the small molecule 2-(3,5-dimethylisoxazol-4-yl)-N-((4-((3-phenylpropyl)amino)quinazolin-2-yl)methyl)acetamide ( <b><i>IPPQ</i></b> ) which selectively targeted the interface between the N-type calcium (CaV2.2) channel and CaVβ. <b><i>IPPQ</i></b> (i) specifically bound to CaVβ2a; (ii) inhibited CaVβ2 's interaction with CaV.2-AID; (iii) inhibited CaV2.2 currents in sensory neurons; (iv) inhibited pre-synaptic localization of CaV2.2 <i>in vivo</i>; and (v) inhibited spinal neurotransmission, which resulted in decreased neurotransmitter release. <b><i>IPPQ</i></b> was anti-nociceptive in naïve rats and reversed mechanical allodynia and thermal hyperalgesia in rodent models of acute, neuropathic, and genetic pain. In structure-activity relationship (SAR) studies focused on improving binding affinity of <b><i>IPPQ</i></b> , another compound (BTT-369), a benzoyl-3,4-dihydro-1'H,2 H-3,4'-bipyrazole class of compounds, was reported by Chen and colleagues, based on work conducted in my laboratory beginning in 2008. BTT-369 contains tetraaryldihydrobipyrazole scaffold - a chemotype featuring phenyl groups known to be significantly metabolized, lower the systemic half-life, and increase the potential for toxicity. Furthermore, the benzoylpyrazoline skeleton in BTT-369 is patented across multiple therapeutic indications. Prior to embarking on an extensive optimization campaign of <b><i>IPPQ</i></b> , we performed a head-to-head comparison of the two compounds. We conclude that <b><i>IPPQ</i></b> is superior to BTT-369 for on-target efficacy, setting the stage for SAR studies to improve on <b><i>IPPQ</i></b> for the development of novel pain therapeutics.</p>","PeriodicalId":72555,"journal":{"name":"Channels (Austin, Tex.)","volume":" ","pages":"128-135"},"PeriodicalIF":0.0,"publicationDate":"2021-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7808423/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38797802","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}

{"title":"A bibliometric analysis and review of recent researches on Piezo (2010-2020).","authors":"Lifu Wang, Xuening Liu, Kun Zhang, Zhongcheng Liu, Qiong Yi, Jin Jiang, Yayi Xia","doi":"10.1080/19336950.2021.1893453","DOIUrl":"10.1080/19336950.2021.1893453","url":null,"abstract":"","PeriodicalId":72555,"journal":{"name":"Channels (Austin, Tex.)","volume":" ","pages":"310-321"},"PeriodicalIF":0.0,"publicationDate":"2021-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7971259/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25480654","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}

{"title":"Mechanosensory and mechanotransductive processes mediated by ion channels in articular chondrocytes: Potential therapeutic targets for osteoarthritis.","authors":"Kun Zhang, Lifu Wang, Zhongcheng Liu, Bin Geng, Yuanjun Teng, Xuening Liu, Qiong Yi, Dechen Yu, Xiangyi Chen, Dacheng Zhao, Yayi Xia","doi":"10.1080/19336950.2021.1903184","DOIUrl":"10.1080/19336950.2021.1903184","url":null,"abstract":"<p><p>Articular cartilage consists of an extracellular matrix including many proteins as well as embedded chondrocytes. Articular cartilage formation and function are influenced by mechanical forces. Hind limb unloading or simulated microgravity causes articular cartilage loss, suggesting the importance of the healthy mechanical environment in articular cartilage homeostasis and implying a significant role of appropriate mechanical stimulation in articular cartilage degeneration. Mechanosensitive ion channels participate in regulating the metabolism of articular chondrocytes, including matrix protein production and extracellular matrix synthesis. Mechanical stimuli, including fluid shear stress, stretch, compression and cell swelling and decreased mechanical conditions (such as simulated microgravity) can alter the membrane potential and regulate the metabolism of articular chondrocytes via transmembrane ion channel-induced ionic fluxes. This process includes Ca²⁺ influx and the resulting mobilization of Ca²⁺ that is due to massive released Ca²⁺ from stores, intracellular cation efflux and extracellular cation influx. This review brings together published information on mechanosensitive ion channels, such as stretch-activated channels (SACs), voltage-gated Ca²⁺ channels (VGCCs), large conductance Ca²⁺-activated K⁺ channels (BK_Ca channels), Ca²⁺-activated K⁺ channels (SK_Ca channels), voltage-activated H⁺ channels (VAHCs), acid sensing ion channels (ASICs), transient receptor potential (TRP) family channels, and piezo1/2 channels. Data based on epithelial sodium channels (ENaCs), purinergic receptors and N-methyl-d-aspartate (NMDA) receptors are also included. These channels mediate mechanoelectrical physiological processes essential for converting physical force signals into biological signals. The primary channel-mediated effects and signaling pathways regulated by these mechanosensitive ion channels can influence the progression of osteoarthritis during the mechanosensory and mechanoadaptive process of articular chondrocytes.</p>","PeriodicalId":72555,"journal":{"name":"Channels (Austin, Tex.)","volume":" ","pages":"339-359"},"PeriodicalIF":0.0,"publicationDate":"2021-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8018402/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25524407","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}

{"title":"Specific protein kinase C isoform exerts chronic inhibition on the slowly activating delayed-rectifier potassium current by affecting channel trafficking.","authors":"Xiangbo Gou, Tingting Hu, Yu Gou, Chaoqi Li, Ming Yi, Mengran Jia","doi":"10.1080/19336950.2021.1882112","DOIUrl":"10.1080/19336950.2021.1882112","url":null,"abstract":"<p><p>The slowly activating delayed rectifier K⁺ current (<i>I</i>_Ks) plays a key role in the repolarization of ventricular action potential in the human heart and is formed by the pore-forming α-subunit encoded by KCNQ1 (Kv7.1) and β-subunit encoded by KCNE1. Evidence suggested that <i>I</i>_Ks was regulated through protein kinase C (PKC) pathway, but the mechanism is controversial. This study was designed to identify the specific PKC isoform involved in the long-term regulation of <i>I</i>_Ks current. The <i>I</i>_Ks current was recorded using whole-cell patch-clamp technique in human embryonic kidney (HEK) 293B cell co-transfected with human KCNQ1/KCNE1 genes. The results revealed that both chronic activation of Ang II and PMA reduced the <i>I</i>_Ks current in a long-term regulation (about 24 hours). Further evidence showed that PKCε knockdown by siRNA antagonized the AngII-induced chronic inhibition on the <i>I</i>_Ks current, whereas knockdown of cPKC (PKCα and PKCβ) attenuated the inhibition effect of PMA on the current. Moreover, the forward transport inhibition of the channel with brefeldin A alleviated the Ang II-induced chronic inhibition on <i>I</i>_Ks current, while the channel endocytosis inhibition with dynasore alleviated both Ang II and PMA-induced chronic inhibition on <i>I</i>_Ks current. The above results showed that PKCε activation promoted the channel endocytosis and inhibited the channel forward transport to the plasma membrane, while cPKC activation only promoted the channel endocytosis, which both down regulated the channel current.</p>","PeriodicalId":72555,"journal":{"name":"Channels (Austin, Tex.)","volume":" ","pages":"262-272"},"PeriodicalIF":0.0,"publicationDate":"2021-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7872027/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25329371","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}

{"title":"Epigenetic control of ion channel expression and cell-specific splicing in nociceptors: Chronic pain mechanisms and potential therapeutic targets.","authors":"Diane Lipscombe, E Javier Lopez-Soto","doi":"10.1080/19336950.2020.1860383","DOIUrl":"10.1080/19336950.2020.1860383","url":null,"abstract":"<p><p>Ion channels underlie all forms for electrical signaling including the transmission of information about harmful events. Voltage-gated calcium ion channels have dual function, they support electrical signaling as well as intracellular calcium signaling through excitation-dependent calcium entry across the plasma membrane. Mechanisms that regulate ion channel forms and actions are essential for myriad cell functions and these are targeted by drugs and therapeutics. When disrupted, the cellular mechanisms that control ion channel activity can contribute to disease pathophysiology. For example, alternative pre-mRNA splicing is a major step in defining the precise composition of the transcriptome across different cell types from early cellular differentiation to programmed apoptosis. An estimated 30% of disease-causing mutations are associated with altered alternative splicing, and mis-splicing is a feature of numerous highly prevalent diseases including neurodegenerative, cancer, and chronic pain. Here we discuss the important role of epigenetic regulation of gene expression and cell-specific alternative splicing of calcium ion channels in nociceptors, with emphasis on how these processes are disrupted in chronic pain, the potential therapeutic benefit of correcting or compensating for aberrant ion channel splicing in chronic pain.</p>","PeriodicalId":72555,"journal":{"name":"Channels (Austin, Tex.)","volume":" ","pages":"156-164"},"PeriodicalIF":0.0,"publicationDate":"2021-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7808434/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38715587","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}