The membrane plays an important role in the structure and function of membrane proteins. We studied the influence of the lipid environment on the photocycle of the membrane protein bacteriorhodopsin (BR) with time-resolved step-scan FTIR spectroscopy. Proton transfer dynamics was monitored with microsecond time resolution for BR embedded in the native purple membrane as well as reconstituted into DOPC liposomes. We observed altered protonation dynamics of the Schiff base and the primary proton acceptor Asp85, revealing a faster rise as well as decay of the M state for BR surrounded by DOPC lipids. The purple membrane consists of a lipid composition that adapts better to the protein shape resulting in a stronger protein- membrane interaction as compared to the uniform DOPC lipid environment. Conformational dynamics and the correlated protonation dynamics are affected by the altered protein-membrane interaction explaining the faster photoreaction of BR in DOPC liposomes. Here we demonstrate the high sensitivity of the proton transfer dynamics to the lipid environment of BR.
{"title":"Impact of the lipid environment on the protonation dynamics of bacteriorhodopsin studied with time-resolved step-scan FTIR spectroscopy","authors":"Michael Jawurek, C. Glaubitz, K. Hauser","doi":"10.3233/BSI-160135","DOIUrl":"https://doi.org/10.3233/BSI-160135","url":null,"abstract":"The membrane plays an important role in the structure and function of membrane proteins. We studied the influence of the lipid environment on the photocycle of the membrane protein bacteriorhodopsin (BR) with time-resolved step-scan FTIR spectroscopy. Proton transfer dynamics was monitored with microsecond time resolution for BR embedded in the native purple membrane as well as reconstituted into DOPC liposomes. We observed altered protonation dynamics of the Schiff base and the primary proton acceptor Asp85, revealing a faster rise as well as decay of the M state for BR surrounded by DOPC lipids. The purple membrane consists of a lipid composition that adapts better to the protein shape resulting in a stronger protein- membrane interaction as compared to the uniform DOPC lipid environment. Conformational dynamics and the correlated protonation dynamics are affected by the altered protein-membrane interaction explaining the faster photoreaction of BR in DOPC liposomes. Here we demonstrate the high sensitivity of the proton transfer dynamics to the lipid environment of BR.","PeriodicalId":44239,"journal":{"name":"Biomedical Spectroscopy and Imaging","volume":"94 1","pages":"167-174"},"PeriodicalIF":0.0,"publicationDate":"2016-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3233/BSI-160135","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"69856631","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Fil: Barrantes, Francisco Jose. Pontificia Universidad Catolica Argentina "Santa Maria de los Buenos Aires". Instituto de Investigaciones Biomedicas. Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Houssay. Instituto de Investigaciones Biomedicas; Argentina
线程:Barrantes, Francisco Jose。阿根廷教皇天主教大学“布宜诺斯艾利斯的圣玛丽亚”。生物医学研究所。国家科学技术研究委员会。豪赛行政协调办公室。生物医学研究所;阿根廷
{"title":"Cholesterol and nicotinic acetylcholine receptor: An intimate nanometer-scale spatial relationship spanning the billion year time-scale","authors":"F. Barrantes","doi":"10.3233/BSI-160158","DOIUrl":"https://doi.org/10.3233/BSI-160158","url":null,"abstract":"Fil: Barrantes, Francisco Jose. Pontificia Universidad Catolica Argentina \"Santa Maria de los Buenos Aires\". Instituto de Investigaciones Biomedicas. Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Houssay. Instituto de Investigaciones Biomedicas; Argentina","PeriodicalId":44239,"journal":{"name":"Biomedical Spectroscopy and Imaging","volume":"34 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2016-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3233/BSI-160158","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"69856733","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
We have compiled a list of the 100 most cited articles in cholesterol research to assess research trends over the last 10 and 100 years to mark the 200th anniversary of the naming of cholesterol as part of the special issue of Biomedical Spectroscopy and Imaging.
{"title":"The top 100 cited cholesterol papers","authors":"Aaron A. Sorensen, D. Weedon","doi":"10.3233/BSI-160160","DOIUrl":"https://doi.org/10.3233/BSI-160160","url":null,"abstract":"We have compiled a list of the 100 most cited articles in cholesterol research to assess research trends over the last 10 and 100 years to mark the 200th anniversary of the naming of cholesterol as part of the special issue of Biomedical Spectroscopy and Imaging.","PeriodicalId":44239,"journal":{"name":"Biomedical Spectroscopy and Imaging","volume":"5 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2016-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3233/BSI-160160","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"69856821","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"FTIR imaging of MCF-7 colonies and their vicinity in Matrigel-embedded 3D cultures","authors":"M. Smolina, E. Goormaghtigh","doi":"10.3233/BSI-160139","DOIUrl":"https://doi.org/10.3233/BSI-160139","url":null,"abstract":"","PeriodicalId":44239,"journal":{"name":"Biomedical Spectroscopy and Imaging","volume":"5 1","pages":"155-166"},"PeriodicalIF":0.0,"publicationDate":"2016-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3233/BSI-160139","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"69856484","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Voiding dysfunction occurs due to the interplay of anatomic, physiologic and functional elements. Hence, integration of new imaging and spectroscopy modalities offers the potential for improving patient assessment by enabling the causal structural defects, formal staging of pelvic floor dysfunction and underlying physiologic mechanisms to be better defined. The purpose of this review is to outline the limitations of current imaging, and highlight the advantages of newer technologies in the evaluation of patients with voiding dysfunction due to loss of structural integrity of the pelvic floor. The everyday action of voiding belies the complex interplay of neural control of the voiding cycle, precise function of healthy organ systems and hemodynamic changes in the microcirculation required for the bladder to fill and empty normally. Brain mediated control initiates voluntary voiding, and integrity of the spinal cord is required to transmit neural signaling to the bladder. A spino-bulbo-spinal reflex is integral to voluntary voiding while urine storage is dependent on lumbosacral spinal reflexes (27). The bladder microcirculation is uniquely adapted to maintain perfusion as the organ's size and wall thickness alter as it fills and empties, and to preferentially perfuse the detrusor muscle prior to bladder contraction. The structure of the pelvic floor is integral to continence; with incontinence in various forms a consequence of the effects of damage, structural weakness or organ prolapse. Urinary incontinence due to loss of pelvic floor integrity is a complex condition. With aging and the effects of illness and injury the normal supportive function of the pelvic floor muscles, ligaments and fascia becomes compromised. Progressive reduction or traumatic loss of soft tissue support results in pelvic organ prolapse (POP), which is a prevalent and debilitating disorder (25). POP is part of the spectrum of abnormalities occurring with pelvic floor dysfunction (35). POP is defined as abnormal symptomatic displacement of the pelvic organs from their normal anatomic position; herniation of some or all of the pelvic viscera occurs, including the urethra, bladder, vaginal vault, cervix, small bowel,
{"title":"Integration of spectroscopy and imaging to optimize evaluation of voiding dysfunction","authors":"L. Stothers, A. Macnab","doi":"10.3233/BSI-160149","DOIUrl":"https://doi.org/10.3233/BSI-160149","url":null,"abstract":"Voiding dysfunction occurs due to the interplay of anatomic, physiologic and functional elements. Hence, integration of new imaging and spectroscopy modalities offers the potential for improving patient assessment by enabling the causal structural defects, formal staging of pelvic floor dysfunction and underlying physiologic mechanisms to be better defined. The purpose of this review is to outline the limitations of current imaging, and highlight the advantages of newer technologies in the evaluation of patients with voiding dysfunction due to loss of structural integrity of the pelvic floor. The everyday action of voiding belies the complex interplay of neural control of the voiding cycle, precise function of healthy organ systems and hemodynamic changes in the microcirculation required for the bladder to fill and empty normally. Brain mediated control initiates voluntary voiding, and integrity of the spinal cord is required to transmit neural signaling to the bladder. A spino-bulbo-spinal reflex is integral to voluntary voiding while urine storage is dependent on lumbosacral spinal reflexes (27). The bladder microcirculation is uniquely adapted to maintain perfusion as the organ's size and wall thickness alter as it fills and empties, and to preferentially perfuse the detrusor muscle prior to bladder contraction. The structure of the pelvic floor is integral to continence; with incontinence in various forms a consequence of the effects of damage, structural weakness or organ prolapse. Urinary incontinence due to loss of pelvic floor integrity is a complex condition. With aging and the effects of illness and injury the normal supportive function of the pelvic floor muscles, ligaments and fascia becomes compromised. Progressive reduction or traumatic loss of soft tissue support results in pelvic organ prolapse (POP), which is a prevalent and debilitating disorder (25). POP is part of the spectrum of abnormalities occurring with pelvic floor dysfunction (35). POP is defined as abnormal symptomatic displacement of the pelvic organs from their normal anatomic position; herniation of some or all of the pelvic viscera occurs, including the urethra, bladder, vaginal vault, cervix, small bowel,","PeriodicalId":44239,"journal":{"name":"Biomedical Spectroscopy and Imaging","volume":"5 1","pages":"283-294"},"PeriodicalIF":0.0,"publicationDate":"2016-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3233/BSI-160149","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"69856515","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
M. Malferrari, F. Francia, A. Mezzetti, G. Venturoli
{"title":"Kinetic effects in dehydration, rehydration, and isotopic exchange of bacterial photosynthetic reaction centers","authors":"M. Malferrari, F. Francia, A. Mezzetti, G. Venturoli","doi":"10.3233/BSI-160136","DOIUrl":"https://doi.org/10.3233/BSI-160136","url":null,"abstract":"","PeriodicalId":44239,"journal":{"name":"Biomedical Spectroscopy and Imaging","volume":"5 1","pages":"185-196"},"PeriodicalIF":0.0,"publicationDate":"2016-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3233/BSI-160136","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"69856693","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
A. Torreggiani, G. Navarra, A. Tinti, M. Foggia, V. Militello
BACKGROUND: Metal ions are implicated in protein aggregation processes of several neurodegenerative pathologies, where the protein deposition occurs, and in the biotechnology field like the food technology where many processes in food manufacturing are based on thermal treatments. OBJECTIVE: The influence of Cu 2+ or Zn 2+ ions on the thermal aggregation process of Bovine β-lactoglobulin (BLG) and Bovine Serum Albumin (BSA), two protein models, was studied with the aim of delineating the role of these ions in the protein aggregation kinetics and to clarify the related molecular mechanisms. METHODS: The protein structure changes were monitored by Raman spectroscopy, whereas the aggregate growth was followed by Dynamic Light Scattering measurements. RESULTS: Both metal ions are able to favour the BLG aggregation, whereas only Zn 2+ ions have a promoter effect on the thermal aggregation of BSA. The reason of this different behaviour is that the BLG aggregation evolution is manly affected by the redistribution of charges, whereas that of BSA by the metal coordination binding which depends on metal. CONCLUSIONS: Raman spectroscopy, combined with dynamic light scattering experiments, was very useful in identifying the role played by Cu 2+ and Zn 2+ on the aggregation pathways of BLG and BSA. The results provide evidence for the role of histidine residues both in the redistribution of charges and in the two modes of metal binding that take place in BLG- and BSA-containing systems, respectively.
{"title":"Chemical and physical characterization of thermal aggregation of model proteins modulated by zinc(II) and copper(II) ions","authors":"A. Torreggiani, G. Navarra, A. Tinti, M. Foggia, V. Militello","doi":"10.3233/BSI-160145","DOIUrl":"https://doi.org/10.3233/BSI-160145","url":null,"abstract":"BACKGROUND: Metal ions are implicated in protein aggregation processes of several neurodegenerative pathologies, where the protein deposition occurs, and in the biotechnology field like the food technology where many processes in food manufacturing are based on thermal treatments. OBJECTIVE: The influence of Cu 2+ or Zn 2+ ions on the thermal aggregation process of Bovine β-lactoglobulin (BLG) and Bovine Serum Albumin (BSA), two protein models, was studied with the aim of delineating the role of these ions in the protein aggregation kinetics and to clarify the related molecular mechanisms. METHODS: The protein structure changes were monitored by Raman spectroscopy, whereas the aggregate growth was followed by Dynamic Light Scattering measurements. RESULTS: Both metal ions are able to favour the BLG aggregation, whereas only Zn 2+ ions have a promoter effect on the thermal aggregation of BSA. The reason of this different behaviour is that the BLG aggregation evolution is manly affected by the redistribution of charges, whereas that of BSA by the metal coordination binding which depends on metal. CONCLUSIONS: Raman spectroscopy, combined with dynamic light scattering experiments, was very useful in identifying the role played by Cu 2+ and Zn 2+ on the aggregation pathways of BLG and BSA. The results provide evidence for the role of histidine residues both in the redistribution of charges and in the two modes of metal binding that take place in BLG- and BSA-containing systems, respectively.","PeriodicalId":44239,"journal":{"name":"Biomedical Spectroscopy and Imaging","volume":"5 1","pages":"197-205"},"PeriodicalIF":0.0,"publicationDate":"2016-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3233/BSI-160145","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"69856716","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Photosystem II (PSII) in plants and cyanobacteria performs light-driven water oxidation to obtain electrons necessary for CO2 fixation. In PSII, a series of electron transfer reactions take place from the Mn4CaO5 cluster, the catalytic site of water oxidation, to a plastoquinone molecule via several redox cofactors. Light-induced Fourier transform infrared (FTIR) difference spectroscopy has been extensively used to investigate the structures and reactions of the redox cofactors in PSII. Recently, FTIR spectroelectrochemistry combined with the light-induced difference technique was applied to study the mechanism of electrontransfer regulation in PSII involving the quinone electron acceptors, QA and QB, and the non-heme iron that bridges them. In this mini-review, this combined FTIR method is introduced, and obtained results about the redox reactions of the non-heme iron and QB, involving the long-range interaction of the Mn4CaO5 cluster with the electron-acceptor side, are summarized.
{"title":"FTIR spectroelectrochemistry combined with a light-induced difference technique: Application to the iron-quinone electron acceptor in photosystem II","authors":"Yuki Kato, T. Noguchi","doi":"10.3233/BSI-160146","DOIUrl":"https://doi.org/10.3233/BSI-160146","url":null,"abstract":"Photosystem II (PSII) in plants and cyanobacteria performs light-driven water oxidation to obtain electrons necessary for CO2 fixation. In PSII, a series of electron transfer reactions take place from the Mn4CaO5 cluster, the catalytic site of water oxidation, to a plastoquinone molecule via several redox cofactors. Light-induced Fourier transform infrared (FTIR) difference spectroscopy has been extensively used to investigate the structures and reactions of the redox cofactors in PSII. Recently, FTIR spectroelectrochemistry combined with the light-induced difference technique was applied to study the mechanism of electrontransfer regulation in PSII involving the quinone electron acceptors, QA and QB, and the non-heme iron that bridges them. In this mini-review, this combined FTIR method is introduced, and obtained results about the redox reactions of the non-heme iron and QB, involving the long-range interaction of the Mn4CaO5 cluster with the electron-acceptor side, are summarized.","PeriodicalId":44239,"journal":{"name":"Biomedical Spectroscopy and Imaging","volume":"5 1","pages":"269-282"},"PeriodicalIF":0.0,"publicationDate":"2016-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3233/BSI-160146","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"69856789","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Henry Mantsch (see Fig. 1) was born in Romania in 1935. He studied chemistry at the Cluj-Napoca University from 1953 till 1958. Subsequently, he obtained his PhD degree in Physical Chemistry in 1964 from the Institute of Chemistry of the Romanian Academy of Sciences. His PhD thesis focused on infrared spectroscopy. Henry moved to the Technical University in Munich as Humboldt Research Fellow for two years (1966–1967). There he secured a German Dr. rer. nat. habil. (DSc). Henry migrated to Canada in 1968 to work with Norman Jones at the National Research Council (NRC) in Ottawa. The
Henry Mantsch(见图1)1935年出生于罗马尼亚。1953年至1958年，他在克卢日-纳波卡大学学习化学。随后，他于1964年在罗马尼亚科学院化学研究所获得物理化学博士学位。他的博士论文研究的是红外光谱学。亨利搬到慕尼黑工业大学担任洪堡研究员两年(1966-1967)。在那里，他找到了一位德国博士。nat. habil。(DSc)。亨利于1968年移居加拿大，在渥太华的国家研究委员会(NRC)与诺曼·琼斯(Norman Jones)一起工作。的
{"title":"Henry Horst Mantsch–A visionary biomedical spectroscopist and a true interdisciplinary professional","authors":"P. Haris","doi":"10.3233/BSI-150125","DOIUrl":"https://doi.org/10.3233/BSI-150125","url":null,"abstract":"Henry Mantsch (see Fig. 1) was born in Romania in 1935. He studied chemistry at the Cluj-Napoca University from 1953 till 1958. Subsequently, he obtained his PhD degree in Physical Chemistry in 1964 from the Institute of Chemistry of the Romanian Academy of Sciences. His PhD thesis focused on infrared spectroscopy. Henry moved to the Technical University in Munich as Humboldt Research Fellow for two years (1966–1967). There he secured a German Dr. rer. nat. habil. (DSc). Henry migrated to Canada in 1968 to work with Norman Jones at the National Research Council (NRC) in Ottawa. The","PeriodicalId":44239,"journal":{"name":"Biomedical Spectroscopy and Imaging","volume":"4 1","pages":"311-314"},"PeriodicalIF":0.0,"publicationDate":"2015-10-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3233/BSI-150125","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"69856170","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
When my colleague Parvez Haris asked me to write a historical review on the evolution of biomedical vibrational spectroscopy I consented, but now I need to clarify what this review is about and what it is not. It is my personal belief that biomedical vibrational spectroscopy has yet to reach its full potential and therefore I will not restrict myself to recounting its past history but will look ahead to its future and where it may still be evolving. Accordingly, my review will comprise two parts. As yours truly has now joined the league of octogenarians, in the first part I plan to share with the readers my personal recollections of the very early days of vibrational bio-spectroscopy which I was privileged to witness and be part of. In the second part I intend to peer into the crystal ball and speculate on new applications in the medical sciences, envisioning vibrational spectroscopy as a tool for the exploration of the human mind to probe psychosomatic diseases and emotional disorders.
{"title":"The evolution of biomedical vibrational spectroscopy: A personal perspective","authors":"H. Mantsch","doi":"10.3233/BSI-150118","DOIUrl":"https://doi.org/10.3233/BSI-150118","url":null,"abstract":"When my colleague Parvez Haris asked me to write a historical review on the evolution of biomedical vibrational spectroscopy I consented, but now I need to clarify what this review is about and what it is not. It is my personal belief that biomedical vibrational spectroscopy has yet to reach its full potential and therefore I will not restrict myself to recounting its past history but will look ahead to its future and where it may still be evolving. Accordingly, my review will comprise two parts. As yours truly has now joined the league of octogenarians, in the first part I plan to share with the readers my personal recollections of the very early days of vibrational bio-spectroscopy which I was privileged to witness and be part of. In the second part I intend to peer into the crystal ball and speculate on new applications in the medical sciences, envisioning vibrational spectroscopy as a tool for the exploration of the human mind to probe psychosomatic diseases and emotional disorders.","PeriodicalId":44239,"journal":{"name":"Biomedical Spectroscopy and Imaging","volume":"4 1","pages":"315-329"},"PeriodicalIF":0.0,"publicationDate":"2015-10-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3233/BSI-150118","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"69856336","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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