Matrix Biology Plus最新文献

{"title":"Corrigendum to “Extracellular matrix remodeling in calcific aortic valve disease: Localized enrichment of type III collagen and LTBP-4” [Matrix Biol Plus 30 (2026) 100194]","authors":"Reiko Kemmochi , Haruko Miyazaki , Yuki Taga , Naoki Takahashi , Takafumi Watanabe , Kentaro Ikemura , Takako Sasaki , Kazunori Mizuno , Satoshi Hirohata , Mitsuaki Matsumoto , Toshitaka Oohashi","doi":"10.1016/j.mbplus.2026.100196","DOIUrl":"10.1016/j.mbplus.2026.100196","url":null,"abstract":"","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"30 ","pages":"Article 100196"},"PeriodicalIF":0.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148184178","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":"Revealing sex-specific changes across protein structure in the aging bone extracellular matrix","authors":"Jacob Tudor ,&nbsp;Alexander Eckersley ,&nbsp;Michael Buckley","doi":"10.1016/j.mbplus.2025.100189","DOIUrl":"10.1016/j.mbplus.2025.100189","url":null,"abstract":"<div><div>The process of aging is an integral but complex component of life that has been intensely studied for decades, from the molecular level to whole organisms. At the tissue level, bone is one of the most difficult to study due to its composite nature of inorganic and organic phases, but advancements in proteomics are enhancing our understanding of the latter, improving our understanding of skeletal aging through identifying temporal changes across the bone proteome. The relative longevity of extracellular matrix (ECM) proteins can make them more susceptible to accumulating damage modifications over time. In addition, their informational density, including their 2D and 3D structure, protein folding, post translational modifications and proteomic composition, as well as their functional importance, has made them a target of interest in the study of aging and medical conditions such as osteoporosis and arthritis. ECM proteins are also increasingly utilised in forensic science for determining biological sex/age because of their longevity. Following recent developments in peptide location fingerprinting methods that improve capabilities of identifying regional changes in protein structure, this study aimed to identify age-associated regional changes along protein structures in <em>Rattus norvegicus</em> from whole limb LC-MC/MS data. Regional changes in protein structure were identified in a variety of collagenous and non-collagenous ECM proteins, providing evidence for increased remodeling in juvenile rats and a reduced ability in adult rats, alongside damage accumulation in the adult ECM. This research highlights the importance of fibrillar collagen remodeling but is also indicative of potential new roles for osteopontin, thrombin, apolipoproteins and wider ECM regulators such as cartilage oligomeric matrix protein. This demonstrates, in this case, the utility of peptide location fingerprinting as a screening tool to identify biomarker candidates of bone aging between juvenile and adult rats.</div></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"29 ","pages":"Article 100189"},"PeriodicalIF":0.0,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145926747","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":"P-LM421E8, the heparan sulfate chain-conjugated laminin-421-E8 fragment, drives differentiation of human induced pluripotent stem cells into hematopoietic progenitor cells comparable to basic fibroblast growth factor in a chemically defined system","authors":"Naoto Ninomiya ,&nbsp;Kaoru Sasaki ,&nbsp;Ryosuke Katori ,&nbsp;Yasuhiro Shimizu ,&nbsp;Kazumasa Fujita ,&nbsp;Yukimasa Taniguchi ,&nbsp;Taiko Kunieda ,&nbsp;Kouichi Tamura ,&nbsp;Masashi Yamada ,&nbsp;Kiyotoshi Sekiguchi ,&nbsp;Hironobu Kimura","doi":"10.1016/j.mbplus.2025.100188","DOIUrl":"10.1016/j.mbplus.2025.100188","url":null,"abstract":"<div><div>Human induced pluripotent stem cells (hiPSCs) are a promising source for cell-based and regenerative therapies. In this study, we developed and optimized a chemically defined differentiation protocol to generate hematopoietic progenitor cells (HPCs) from hiPSCs. We demonstrated that basic fibroblast growth factor (bFGF) plays a crucial role in enhancing HPC differentiation, particularly when applied during both the mesoderm (ME) and hematopoietic endothelial (HE) induction stages. Additionally, we explored the use of P-LM421E8, a recombinant fusion protein of laminin421-E8 fragment with domain 1 (D1) of perlecan possessing heparan sulfate (HS) chains. Our findings indicate that P-LM421E8 effectively supports HPC differentiation, generating stable CD34-high/CD117⁺ populations comparable to those produced with bFGF treatment. Furthermore, we observed that HPCs generated on P‑LM421E8‑coated surfaces exhibited superior natural killer (NK) cell differentiation potential. Although both P-LM421E8 and bFGF supported HPC differentiation, no significant additive effects were observed when used together. This suggests that P-LM421E8 can effectively support HPC differentiation without the need for exogenous bFGF, possibly through enhanced interaction with endogenous FGFs. The structural properties of P-LM421E8, which facilitate retention and presentation of FGFs via HS chains on its D1, may contribute to its effectiveness in promoting HPC development. Our findings establish P‑LM421E8 as a potent matrix for HPC differentiation and highlight its promise for refining hematopoietic protocols and advancing cell‑based immunotherapies.</div></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"29 ","pages":"Article 100188"},"PeriodicalIF":0.0,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145738941","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":"Human gingival fibroblast-mediated remodeling of three-dimensional fibrin hydrogels","authors":"Merve Ceylan ,&nbsp;Marja L. Laine ,&nbsp;Behrouz Zandieh Doulabi ,&nbsp;Hans J.A.M. Korfage ,&nbsp;René J.B. Dijkstra ,&nbsp;Teun J. de Vries ,&nbsp;Ton Schoenmaker","doi":"10.1016/j.mbplus.2026.100191","DOIUrl":"10.1016/j.mbplus.2026.100191","url":null,"abstract":"<div><div>The extracellular matrix (ECM) critically regulates fibroblast behavior during tissue repair and regeneration. However, how culture dimensionality influences fibroblast-mediated ECM remodeling remains unclear. This study investigated the effects of three-dimensional (3D) fibrin hydrogels on the phenotype and remodeling activity of primary human gingival fibroblasts (GFs) compared to conventional two-dimensional (2D) monolayer cultures. Live/dead staining confirmed high GF viability in both conditions, with elongated and branched cell morphologies in 3D fibrin hydrogels, contrasting with spindle-shaped cells in 2D monolayers. Hematoxylin and Eosin, and Masson’s Trichrome staining revealed progressive fibrin degradation and <em>de novo</em> collagen deposition over 21 days of culturing. Gene expression analysis showed that while <em>FN1</em>, <em>COL1A1</em>, and <em>COL3A1</em> levels remained relatively stable, <em>TGFB1</em> expression increased significantly from day 7 to day 14 in 3D hydrogels (<em>p</em> &lt; 0.05) and was higher than in 2D cultures at day 21 (<em>p</em> &lt; 0.05). This coincided with a marked upregulation of <em>ACTA2</em> (<em>p</em> &lt; 0.01), indicating myofibroblast-like differentiation. MMP-2 activity increased significantly over time in both 2D and 3D cultures (<em>p</em> &lt; 0.01 and <em>p</em> &lt; 0.001, respectively). In contrast, <em>PLAU</em> and <em>PLAT</em> expression decreased significantly at days 14 and 21 (<em>p</em> &lt; 0.001 and <em>p</em> &lt; 0.05, respectively), reflecting a temporal shift from fibrinolytic to collagenolytic remodeling. Despite active remodeling, mechanical testing showed no significant changes in hydrogel stiffness or relaxation between day 1 and day 7, or between cell-seeded and acellular gels (<em>p</em> &gt; 0.05), likely due to the small contractile forces generated by the cells relative to the gel’s bulk modulus. Together, these findings demonstrate that 3D fibrin hydrogels provide a biologically active and physiologically relevant microenvironment that supports fibroblast-mediated ECM remodeling, offering a biomimetic model for investigating the mechanobiology of periodontal and <em>peri</em>-implant soft tissue regeneration.</div></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"29 ","pages":"Article 100191"},"PeriodicalIF":0.0,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146229804","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":"Regional FDL tendon properties are regulated by biglycan in a collagen VI-independent manner","authors":"R.J. Leiphart,&nbsp;S.N. Weiss,&nbsp;N.A. Dyment,&nbsp;L.J. Soslowsky","doi":"10.1016/j.mbplus.2026.100190","DOIUrl":"10.1016/j.mbplus.2026.100190","url":null,"abstract":"<div><div>Healthy tendon is associated with organized and aligned extracellular matrix (ECM) that becomes disorganized with disease, yet the mechanisms and pathogenesis of tendon disease remain poorly understood. Tendons that “wrap-around” joints, such as the flexor digitorum longus (FDL) tendon, contain a unique ECM that shares similarities with diseased tendons, which can be leveraged to study tendon cell biology across distinct loading environments. The pericellular matrix (PCM) is a critical matrix structure that is understudied in tendon and is likely involved in tendon mechanosensation and homeostasis. Two components of the tendon PCM, biglycan and collagen VI, are known regulators of tendon function and are implicated in tendon disease. Given the implication of PCM molecules in regulating tendon properties, this work sought to define the regional development of a murine wrap-around tendon, how biglycan influences these regional properties, and the extent to which these mechanisms involve collagen VI. Gene expression and histological analyses demonstrated regional divergence in FDL tendon properties by P14. While biglycan knockout did not result in broad disruptions to gene expression or the behavior of <em>Scx</em>+ or <em>Col6a1</em>+ cells, several genes were dysregulated with biglycan deficiency. These changes corresponded with inferior mechanical properties in biglycan-deficient tendons. This work defines the development of regional FDL tendon properties and demonstrates that biglycan knockout impacts these regional properties through a collagen VI-independent mechanism. Results from this work provide understanding of biglycan regulation in tendon and lay the foundation for future work researching tendon mechanosensitive mechanisms.</div></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"29 ","pages":"Article 100190"},"PeriodicalIF":0.0,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146229758","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":"Loss of fibronectin fiber tension is inherent to ECM remodeling in human myocarditis and post-inflammatory fibrosis","authors":"Krishna Chander Sridhar ,&nbsp;Julia Mehl ,&nbsp;Karin Klingel ,&nbsp;Mario Thiele ,&nbsp;Sophie Van Linthout ,&nbsp;Carsten Tschöpe ,&nbsp;Georg N Duda ,&nbsp;Viola Vogel","doi":"10.1016/j.mbplus.2025.100182","DOIUrl":"10.1016/j.mbplus.2025.100182","url":null,"abstract":"<div><h3>Background</h3><div>Viral myocarditis (MC) is associated with extracellular matrix (ECM) remodeling and involves excessive deposition of collagen and other ECM proteins by cardiac fibroblasts, potentially leading to scarring and ECM stiffening, which may subsequently contribute to impaired cardiac functions. Clarifying whether changes in ECM fiber tension are detectable during either the acute or scarring phase could provide a novel, mechanistically relevant mechanobiological signature.</div></div><div><h3>Objectives</h3><div>Our goal was to ask whether ECM mechano-markers can be identified in the myocardium, beyond excessive collagen fiber deposition, that are associated with the acute infection or the pathological scarring of the human heart, and how this might be associated with the infiltration of macrophages.</div></div><div><h3>Methods</h3><div>Left-ventricular (LV) endomyocardial biopsies were obtained from patients (N = 39) with acute myocarditis MC (N = 21) including COVID-19 (N = 4) patients suspected with myocarditis MC and/or impaired LV function, dilated cardiomyopathy (N = 6), inflammatory dilated cardiomyopathy (N = 12) to specify diagnosis and treatment options. Endomyocardial biopsies were analyzed for viral genomes, immune cells infiltration and ECM remodeling. Fibronectin fiber tension was assessed using the fibronectin-binding tension-sensor (FnBPA5), while collagen fiber deposits were visualized using second harmonic generation (SHG) microscopy.</div></div><div><h3>Results</h3><div>While fibronectin fibers were tensed in healthy hearts, histological staining with our novel tension probe FnBPA5 showed that fibronectin fibers had lost their tension in distinct loci in all patient groups. In the acute inflammatory phase (MC), loci with untensed fibronectin fibers were found in close proximity to infiltrated macrophages. In already dilated hearts, biopsies which presented low densities of infiltrated macrophages, thick collagen I/III fiber bundles as visualized by SHG were found in proximity to untensed fibronectin fibers and myofibroblasts, which together are indicative of fibrotic ECM niches where the inflammation has subsided. Comparison of clinical diagnostic and experimental histological data showed clear correlations between altered ECM niche properties and cardiac function deterioration.</div></div><div><h3>Conclusions</h3><div>Our data suggest that relaxed fibronectin fibers are a recurrent feature of myocarditis and associate with measures of cardiac dysfunction. These findings suggest that fibronectin fiber tension might be a mechanobiological signature that warrants validation in larger, longitudinal cohorts and evaluation of in-vivo measurability.</div></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"28 ","pages":"Article 100182"},"PeriodicalIF":0.0,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145229686","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":"Generation of a conditional Adamts6 mouse allele reveals roles in lung maturation in addition to cardiac and musculoskeletal development","authors":"Jessica M. Sirek ,&nbsp;Elizabeth H. Rush ,&nbsp;Aditi Darodkar ,&nbsp;Suneel S. Apte ,&nbsp;Timothy J. Mead","doi":"10.1016/j.mbplus.2025.100186","DOIUrl":"10.1016/j.mbplus.2025.100186","url":null,"abstract":"<div><div>Prior analysis of mouse embryos homozygous for a point mutation (p.Ser149Arg) that abrogated secretion of the protease, ADAMTS6, showed that it is essential for cardiovascular and limb development. Because <em>Adamts6</em>^S149R/S149R mice do not survive past birth, it is currently not feasible to investigate ADAMTS6 in specific cellular lineages postnatally. Therefore, we generated a conditional allele using CRISPR-Cas9-mediated genome editing to insert unidirectional loxP sites flanking the first coding exon in <em>Adamts6</em>, resulting in a frameshift mutation after loxP recombination. Mice homozygous for the unrecombined floxed allele (<em>Adamts6</em>^fl/fl) are viable, fertile, and without overt phenotype. <em>Adamts6</em>^del/del embryos, generated upon constitutive recombination induced by a <em>CMV</em>-Cre transgene, also do not survive past birth and have identical defects in the heart and limbs as <em>Adamts6</em>^S149R/S149R embryos, demonstrating efficient transgene recombination. In addition to previous defects in cardiovascular and limb development, <em>Adamts6</em>^del/del embryos have reduced airway branching, thereby identifying a role for ADAMTS6 in lung maturation. This newly generated <em>Adamts6</em>^fl allele makes feasible analysis of ADAMTS6 secreted by cells of different lineages and during specified temporal windows during developmental processes as well as in disease models.</div></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"28 ","pages":"Article 100186"},"PeriodicalIF":0.0,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145623743","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":"Corrigendum to “Tissue material properties, whole-bone morphology and mechanical behavior in the Fbn1C1041G/+ mouse model of Marfan Syndrome” [Matrix Biol. Plus 23 (2024) 100155]","authors":"Elizabeth A. Zimmermann ,&nbsp;Taylor DeVet ,&nbsp;Myriam Cilla ,&nbsp;Laia Albiol ,&nbsp;Kyle Kavaseri ,&nbsp;Christine Andrea ,&nbsp;Catherine Julien ,&nbsp;Kerstin Tiedemann ,&nbsp;Arash Panahifar ,&nbsp;Sima Alidokht ,&nbsp;Richard Chromik ,&nbsp;Svetlana V. Komarova ,&nbsp;Dieter P. Reinhardt ,&nbsp;Paul Zaslansky ,&nbsp;Bettina M. Willie","doi":"10.1016/j.mbplus.2025.100176","DOIUrl":"10.1016/j.mbplus.2025.100176","url":null,"abstract":"","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"28 ","pages":"Article 100176"},"PeriodicalIF":0.0,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145693603","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":"Retraction notice to “Deregulated expression of Elastin Microfibril Interfacer 2 (EMILIN2) in gastric cancer affects tumor growth and angiogenesis.” [Matrix Biol. Plus 6–7 (2020) 100029]","authors":"Eva Andreuzzi ,&nbsp;Albina Fejza ,&nbsp;Alessandra Capuano ,&nbsp;Evelina Poletto ,&nbsp;Eliana Pivetta ,&nbsp;Roberto Doliana ,&nbsp;Rosanna Pellicani ,&nbsp;Andrea Favero ,&nbsp;Stefania Maiero ,&nbsp;Mara Fornasarig ,&nbsp;Renato Cannizzaro ,&nbsp;Renato V. Iozzo ,&nbsp;Paola Spessotto ,&nbsp;Maurizio Mongiat","doi":"10.1016/j.mbplus.2025.100184","DOIUrl":"10.1016/j.mbplus.2025.100184","url":null,"abstract":"","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"28 ","pages":"Article 100184"},"PeriodicalIF":0.0,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145693602","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":"Evolutionary constraints on positional sequence, collective properties and sequence style of tropoelastin dictated by fundamental requirements for formation and function of the extracellular elastic matrix","authors":"Fred W. Keeley","doi":"10.1016/j.mbplus.2025.100183","DOIUrl":"10.1016/j.mbplus.2025.100183","url":null,"abstract":"<div><div>Elastin is the extracellular matrix protein responsible for properties of extension and energy-efficient elastic recoil in large blood vessels, lung parenchyma and other vertebrate tissues. Monomeric tropoelastin assembles by phase separation into an extended polymeric matrix covalently cross-linked through lysine residues, producing a robust biomaterial able to withstand hundreds of millions of cycles of extension and recoil. Elastin functions as an entropic elastomer, whose properties are the direct result of the inability of the protein to fold into a fixed, stable structure. Most investigations of how the unusual properties of polymeric elastin arise from the sequence of tropoelastin have utilized molecular biological/biophysical methodologies. This study takes an alternative approach, using a comprehensive, well-curated database of Amniote tropoelastin sequences to identify characteristics conserved through &gt;300 million years of evolution. Conserved characteristics included preservation of not only regions of positional sequence but also collective or compositional characteristics derived from but not strictly dependent on positional sequence. A plausible overall consensus sequence for Amniote tropoelastins allowed quantification of residue-by-residue, domain-by-domain and region-by-region levels of sequence conservation. Regions of low positional sequence conservation nevertheless maintained a recognizable sequence style characterized by tandem repeats and partial repeats of short, non-polar motifs. Motif analysis suggested hPGhGG, with numerous insertions and deletions, as the underlying repeating unit in all Amniote tropoelastins. The data identify significant evolutionary constraints dictated by fundamental requirements for formation and functionality of the extracellular elastin matrix, and suggest a rich source of evolutionarily permitted opportunities for modulating properties to meet specific species requirements.</div></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"28 ","pages":"Article 100183"},"PeriodicalIF":0.0,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145322329","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}