Archives of biochemistry and biophysics最新文献

{"title":"Microcrystallization and room-temperature serial crystallography structure of human cytochrome P450 3A4","authors":"Owens Uwangue ,&nbsp;Johan Glerup ,&nbsp;Andreas Dunge ,&nbsp;Monika Bjelcic ,&nbsp;Gabrielle Wehlander ,&nbsp;Gisela Brändén","doi":"10.1016/j.abb.2025.110419","DOIUrl":"10.1016/j.abb.2025.110419","url":null,"abstract":"<div><div>The cytochrome P450 family of enzymes are key players in the metabolism of foreign substances in the body, including pharmaceutical compounds, and therefore important to take into consideration during drug development. The main human isoform is CYP3A4, a highly flexible protein that can act on a diverse set of substances and that is inhibited by compounds varying greatly in size. To accompany the different ligands, substantial conformational changes occur that transform the active-site binding pocket between a collapsed form and various open states. A large body of biophysical data including high-resolution structures are available but there is still a lack of understanding of the dynamic properties of CYP3A4. Here, we present the first room-temperature structure of CYP3A4 solved by serial crystallography. The structure is overall very similar to structures solved at cryo-temperature of the un-bound form of the enzyme including the conformation of the active-site lid. We observe that loops are better defined at room-temperature despite the lower resolution of this structure. Based on an internal distance matrix analysis of a large set of CYP3A4 structures, we conclude that the crystal form rather than temperature is determining for how the structures cluster. Finally, a workflow for generating microcrystals suitable for fixed-target serial crystallography data collection is described. This work lays the foundation for future studies of ligand-induced dynamics and structural transitions during the catalytic reaction of CYP3A4.</div></div>","PeriodicalId":8174,"journal":{"name":"Archives of biochemistry and biophysics","volume":"769 ","pages":"Article 110419"},"PeriodicalIF":3.8,"publicationDate":"2025-04-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143823629","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A glibenclamide analog lacking the cyclohexylurea portion fails to block ischemic preconditioning-induced mitochondrial and cardiac protection against ischemia/reperfusion injury","authors":"Plínio Bezerra Palácio,&nbsp;Geovanna Carvalho de Freitas Soares,&nbsp;Heberty Tarso Facundo","doi":"10.1016/j.abb.2025.110418","DOIUrl":"10.1016/j.abb.2025.110418","url":null,"abstract":"<div><div>Despite significant research, there are no definitive therapies to prevent ischemia/reperfusion injury. During reperfusion, mitochondrial reactive oxygen species (ROS) cause cell damage. Ischemic preconditioning (IP), characterized by brief cycles of ischemia and reperfusion, activates mitochondrial ATP-sensitive potassium channels (mitoKATP) and provides cardioprotection. The aim of the present study is to investigate the impact of a truncated glibenclamide (lacking the cyclohexylurea portion - IMP-A) in ischemic preconditioning (IP)-mediated cardioprotection. Our study shows that IMP-A (2–5 μM) does not inhibit the protective effects of IP against ischemia/reperfusion damage in isolated rat hearts. In this context, IP hearts (with or without IMP-A) exhibited preserved cardiac function, as indicated by stable left ventricular developed pressure, maximal and minimal first derivatives, and rate-pressure product, along with a reduced infarct size following ischemia/reperfusion injury. Conversely, glibenclamide (2 μM - a well-characterized mitoKATP inhibitor) abolished the protective effects of IP against ischemia/reperfusion damage. Mitochondria isolated from reperfused IP hearts (treated or not with IMP-A) produced significantly lower levels of mitochondrial ROS and had lower susceptibility to Ca²⁺-induced swelling secondary to mitochondrial permeability transition pore (mPTP) opening. Additionally, IP hearts (treated or not with IMP-A) had preserved protein sulfhydryls. Glibenclamide elevated mitochondrial ROS production and negatively impacted mPTP and the sulfhydryl protection seen in IP hearts. Importantly, mitochondrial O₂ consumption was preserved in IP hearts (treated or not with IMP-A), and this preservation was disrupted by glibenclamide but not by IMP-A. These findings suggest that the cyclohexylurea group of glibenclamide is essential for its ability to block IP-mediated cardioprotection, providing valuable insights for developing novel therapeutic strategies.</div></div>","PeriodicalId":8174,"journal":{"name":"Archives of biochemistry and biophysics","volume":"769 ","pages":"Article 110418"},"PeriodicalIF":3.8,"publicationDate":"2025-04-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143829917","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Miltefosine and amphoterin B induce membrane rigidity in Leishmania amazonensis and Leishmania-infected macrophages","authors":"Ellyêssa Nascimento Borges ,&nbsp;Kleber Santiago Freitas e Silva ,&nbsp;Éder Jéferson Souza Cardoso ,&nbsp;Eliana Martins Lima ,&nbsp;Sebastião Antonio Mendanha ,&nbsp;Antonio Alonso","doi":"10.1016/j.abb.2025.110417","DOIUrl":"10.1016/j.abb.2025.110417","url":null,"abstract":"<div><div>Miltefosine (MTF) and amphotericin B (AmB), drugs approved for leishmaniasis treatment, induce membrane rigidity in <em>Leishmania amazonensis</em> at concentrations that inhibit parasite growth, as demonstrated through spin-probe electron paramagnetic resonance (EPR) spectroscopy. Notably, the rigidity induced by MTF is not due to its direct interaction with the membrane, as shorter incubation periods instead increase fluidity. However, measurements taken following short-term drug exposure reflect conditions before possible oxidative stress has fully developed. AmB causes membrane rigidity, but only at concentration 100 times higher than those causing rigidity after 24 h of exposure. In contrast, oxidative stress-induced membrane rigidity was not observed in macrophages, suggesting that nitric oxide production by these cells may mitigate oxidative damage. Both drugs, however, induced significant membrane rigidity in <em>Leishmania</em>-infected macrophages at concentrations slightly above the IC₅₀ for amastigotes. EPR data further suggest that oxidative processes can occur within the membranes of the macrophage-amastigote system even without drug exposure. This study also suggests that the primary mechanisms underlying the antileishmanial activity of these two membrane-active drugs are associated with their effects on the cell membrane. Membrane alterations likely lead to ionic imbalances, which may, in turn, disrupt mitochondrial membrane potential and thereby enhance reactive oxygen species (ROS) formation.</div></div>","PeriodicalId":8174,"journal":{"name":"Archives of biochemistry and biophysics","volume":"769 ","pages":"Article 110417"},"PeriodicalIF":3.8,"publicationDate":"2025-04-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143817716","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"E53, E96, D162, E247 and D322 in Ca2+-binding domains of annexin A2 are essential for regulating intracellular [Ca2+] and crystal adhesion to renal cells via ERK1/2 and JNK signaling pathways","authors":"Sunisa Yoodee,&nbsp;Thanyalak Malaitad,&nbsp;Sirikanya Plumworasawat,&nbsp;Visith Thongboonkerd","doi":"10.1016/j.abb.2025.110410","DOIUrl":"10.1016/j.abb.2025.110410","url":null,"abstract":"<div><div>Annexin A2 (ANXA2) is expressed inside the cytoplasm and on the surface of renal tubular epithelial cells (RTECs) and is documented as a calcium oxalate monohydrate (COM) crystal-binding protein. Nevertheless, its molecular mechanism involved in kidney stone disease (KSD) remains underinvestigated. Herein, we performed various molecular assays to unravel the roles of ANXA2 and core residues (E53, E96, D162, E247 and D322) in its Ca²⁺-binding domains in the stone formation mechanism, particularly at crystal-cell adhesion step and downstream signaling cascade. ANXA2 was up-regulated in apical membranes, not cytosol, of RTECs after COM crystal exposure. Neutralizing the surface expression of ANXA2 by a specific monoclonal antibody and silencing its expression by small interfering RNA (siRNA) significantly decreased COM crystal-cell adhesion. siRNA also suppressed the COM-induced up-regulation of phospho-ERK1/2 and phospho-JNK, but not that of phospho-p38. Overexpression of ANXA2 wild-type (WT), but not that of E53A, E96A, D162A, E247A and D322A mutants of its Ca²⁺-binding domains, significantly increased intracellular [Ca²⁺], COM-cell adhesion, and phospho-ERK1/2 level. Therefore, E53, E96, D162, E247 and D322 in the Ca²⁺-binding domains of annexin A2 are essential for regulating intracellular [Ca²⁺] and COM crystal-cell adhesion via ERK1/2 and JNK signaling pathways.</div></div>","PeriodicalId":8174,"journal":{"name":"Archives of biochemistry and biophysics","volume":"769 ","pages":"Article 110410"},"PeriodicalIF":3.8,"publicationDate":"2025-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143791015","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Redox regulation of cutaneous AMPs by ozone in tensioned skin models","authors":"John Ivarsson ,&nbsp;Erika Pambianchi ,&nbsp;Alessandra Pecorelli ,&nbsp;Yunsook Lim ,&nbsp;Giuseppe Valacchi","doi":"10.1016/j.abb.2025.110409","DOIUrl":"10.1016/j.abb.2025.110409","url":null,"abstract":"<div><div>Ozone-induced inflammation has been linked to the development of skin ailments including atopic dermatitis, acne vulgaris, eczema and psoriasis, mainly through a redox-inflammatory pathway. While ozone cannot penetrate the cutaneous layers, it is able to damage the skin through oxinflammatory reactions in the epidermis that lead to the generation of lipid-peroxides, aldehydes, and H₂O₂. When the production of these bioactive oxidative molecules overwhelms the cutaneous redox defenses, cutaneous damage incurs. Antimicrobial peptides (AMPs) are effector molecules that regulate a variety of cutaneous immune responses. Increased AMPs levels have also been detected in active lesions of inflammatory skin diseases. Our previous research has shown that exposure to either ozone induced the expression of cutaneous AMPs (LL-37, β-defensin 2, and β-defensin 3) levels in <em>ex vivo</em> skin explants, corroborating the hypothesis that ozone exposure might worsen inflammatory skin conditions via AMPs de-regulation. In the present work, to further assess the cutaneous AMPs responses in a more physiological setting, skin models cultured under physiological tension (TenBio) were expose to ozone. As a proof of concept, cutaneous models were pre-treated with a variety of redox inhibitors (catalase, deferoxamine (DFO) and VAS2870 (VAS)) before ozone exposure to better understand the involvement of a redox signaling. Our data demonstrates that even in the most realistic cutaneous <em>ex vivo</em> model, ozone induces LL-37, hBD2, and hBD3 protein levels through a redox mechanism. This study lays the basis to uncover the mechanisms of ozone dysregulation of cutaneous AMPs, a fundamental step to understanding the development/worsening of pollution-linked inflammatory skin conditions.</div></div>","PeriodicalId":8174,"journal":{"name":"Archives of biochemistry and biophysics","volume":"769 ","pages":"Article 110409"},"PeriodicalIF":3.8,"publicationDate":"2025-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143791022","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Lipid saturation modulates the interaction of anastrozole with biointerfaces","authors":"Guilherme Veronezi,&nbsp;Matheus E. Rosa,&nbsp;Jefferson Carnevalle Rodrigues,&nbsp;Luciano Caseli","doi":"10.1016/j.abb.2025.110408","DOIUrl":"10.1016/j.abb.2025.110408","url":null,"abstract":"<div><div>The interaction of anastrozole, an anticancer drug, with lipid biointerfaces was investigated using Langmuir monolayers of DPPS (saturated lipid) and POPS (unsaturated lipid) to model different membrane environments. Surface pressure-area isotherms revealed that anastrozole induced a slight condensation in DPPS monolayers, while significantly condensing POPS at higher surface pressures, indicating attractive interactions with the unsaturated lipid. The surface dilatational modulus remained largely unaffected for DPPS but decreased for POPS, highlighting a reduction in the surface elasticity. Brewster Angle Microscopy (BAM) images showed the formation of domains in anastrozole-POPS monolayers, whereas DPPS monolayers retained a homogeneous morphology. Infrared spectroscopy indicated that anastrozole increased the conformational order of DPPS alkyl chains while decreasing order in POPS, further supporting the lipid-specific effects of the drug. These findings suggest that lipid saturation plays a critical role in modulating drug-lipid interactions, with anastrozole exhibiting a higher affinity for unsaturated lipids, potentially influencing its bioavailability and mechanism of action at biomembrane interfaces. The results provide insights into the physicochemical behavior of anastrozole in lipid-rich environments, which may be relevant for drug delivery and therapeutic applications.</div></div>","PeriodicalId":8174,"journal":{"name":"Archives of biochemistry and biophysics","volume":"769 ","pages":"Article 110408"},"PeriodicalIF":3.8,"publicationDate":"2025-04-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143787405","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The role of lncRNAs in sepsis-induced acute lung injury: Molecular mechanisms and therapeutic potential","authors":"Huijuan Qi,&nbsp;Gu Ying,&nbsp;Wang Ling,&nbsp;Honggang Jia,&nbsp;Xinxiu Zhou,&nbsp;Xinyu Lin","doi":"10.1016/j.abb.2025.110407","DOIUrl":"10.1016/j.abb.2025.110407","url":null,"abstract":"<div><div>Sepsis, a life-threatening syndrome, results from a dysregulated immune and hemostatic response, contributing to acute lung injury (ALI) and its progression into acute respiratory distress syndrome (ARDS). The development of septic ALI is complex, involving excessive inflammatory mediator production that damages endothelial and epithelial cells, leading to vascular leakage, edema, and vasodilation—key factors in ALI pathogenesis. Long noncoding RNAs (lncRNAs), over 200 nucleotides in length, play critical roles in various biological processes, including sepsis regulation. They exhibit both promotive and inhibitory effects, influencing sepsis progression and resolution. Despite their significance, comprehensive reviews detailing lncRNA involvement in sepsis-induced ALI remain limited. This review aims to address this gap by summarizing the diverse functions of lncRNAs in septic ALI, emphasizing their potential in diagnosis and treatment. Furthermore, we will explore the molecular mechanisms underlying lncRNA involvement, particularly their miRNA-dependent regulatory pathways. Understanding these interactions may provide novel insights into therapeutic strategies for sepsis-induced ALI.</div></div>","PeriodicalId":8174,"journal":{"name":"Archives of biochemistry and biophysics","volume":"768 ","pages":"Article 110407"},"PeriodicalIF":3.8,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143778865","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Decreased levels of Prx1 are associated with proteasome impairment and mitochondrial dysfunction in the yeast Saccharomyces cerevisiae","authors":"Natália Mori Avellaneda Penatti ,&nbsp;Mário Henrique Barros ,&nbsp;Fernando Gomes ,&nbsp;Luis Eduardo Soares Netto ,&nbsp;Kamila de Jesus Maciel ,&nbsp;Vincent Louis Viala ,&nbsp;Ana Mara Viana ,&nbsp;Marilene Demasi","doi":"10.1016/j.abb.2025.110406","DOIUrl":"10.1016/j.abb.2025.110406","url":null,"abstract":"<div><div>In previous studies we reported the S-glutathionylation at Cys residues (C76 and C221) of the α5 subunit of the 20S catalytic unit of the yeast proteasome, later mutated to Ser residues. Notably, the strain with the α5-C76S mutation exhibited a reduced chronological life span when grown in glucose as the carbon source. In the present study, we aimed to explore the interplay between mitochondria and the proteasome, considering the α5-C76S-mutated strain as a model of proteasomal impairment. For this purpose, we focused on the growth of the C76S strain in glycerol/ethanol as the carbon source. C76S strain exhibited poor growth and morphological alterations under these conditions, while the proteasomal activity was significantly decreased. We observed decreased activity of the 30S and 26S complexes in the C76S strain, which were accompanied by increased pool of poly-ubiquitinylated proteins. Regarding mitochondrial function, O₂ consumption and the concentration of total cellular ATP were significantly increased in the C76S strain. However, levels of peroxiredoxin-1 (Prx1), an important mitochondrial Cys-based peroxidase, were reduced in the C76S strain. In parallel, H₂O₂ release by mitochondrial respiration was augmented as well as decreased GSH/GSSG ratios, an important parameter of oxidative stress. These findings suggest that, despite increased O₂ consumption and ATP production, the mitochondria from the C76S strain promotes an increased oxidative stress most probably due to decreased Prx1 levels. DNA fragmentation and increased cytoplasmic cytochrome C, two apoptotic markers, were observed in the C76S strain. To assess the role of Prx1 in the survival of the C76S strain, we overexpressed this peroxiredoxin in both wild type and C76S strains, which resulted in the partial recovery of the C76S strain phenotype and proteasome activity. The relationship between decreased Prx1 concentration and proteasome impairment remains under investigation.</div></div>","PeriodicalId":8174,"journal":{"name":"Archives of biochemistry and biophysics","volume":"768 ","pages":"Article 110406"},"PeriodicalIF":3.8,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143767882","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Tyrosinase inhibition by natural stilbenoid glycosides: Critical role of the vinyl moiety in piceid for melanogenesis suppression","authors":"Yilu Sun,&nbsp;Jia Zhao,&nbsp;Jianhui Rong","doi":"10.1016/j.abb.2025.110405","DOIUrl":"10.1016/j.abb.2025.110405","url":null,"abstract":"<div><div>Skin hyperpigmentation due to UV-induced tyrosinase activation and melanin overproduction is an ongoing challenge in cosmetic and dermatological applications. While resveratrol analogues show anti-melanogenic potential, the structure-activity relationships of their glycosylated derivatives remain underexplored. Here, we investigate how the vinyl moiety in the food-derived stilbenoid glycoside piceid (resveratrol-3-<em>O</em>-β-glucoside) affects tyrosinase inhibition. We reduced the vinyl moiety to yield dihydropiceid by catalytic hydrogenation and systematically assessed both compounds for anti-melanogenic effects. As results, piceid exhibited superior monophenolase inhibition over dihydropiceid in enzyme kinetics, while both compounds showed comparable diphenolase inhibition. Cellular assays revealed that piceid reduced melanin production by 59.2 % at 25 μM in α-MSH-stimulated B16F10 melanoma cells, whereas dihydropiceid showed weaker activity (&lt;25 % reduction). MolgpKa analysis indicated that the vinyl moiety lowered the 4′-OH pKa (9.7 vs. 9.9), while UV–vis spectroscopy validated that the vinyl moiety enhanced the copper chelation capacity of piceid (ΔOD: 0.459) over dihydropiceid (ΔOD: 0.233). Molecular docking revealed that 4′-OH in piceid closely coordinated the tyrosinase binuclear copper center, whereas molecular dynamics simulation validated that hydrogen bonding supports the binding of both compounds to tyrosinase. Collectively, this study establishes the vinyl moiety in dietary stilbenoids as a critical pharmacophore for tyrosinase inhibition and thereby provides a molecular basis for developing natural anti-hyperpigmentation functional foods or cosmeceuticals.</div></div>","PeriodicalId":8174,"journal":{"name":"Archives of biochemistry and biophysics","volume":"768 ","pages":"Article 110405"},"PeriodicalIF":3.8,"publicationDate":"2025-03-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143738932","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Corrigendum to “Cucurbitacin B inhibits gastric cancer progression by suppressing STAT3 activity” [Archiv. Biochem. Biophys. 684 (2020) 108314]","authors":"Jiaixin Xu ,&nbsp;Yunhe Chen ,&nbsp;Rui Yang ,&nbsp;Tong Zhou ,&nbsp;Wei Ke ,&nbsp;Yuan Si ,&nbsp;Shusheng Yang ,&nbsp;Te Zhang ,&nbsp;Xuewen Liu ,&nbsp;Liang Zhang ,&nbsp;Ke Xiang ,&nbsp;Yang Guo ,&nbsp;Ying Liu","doi":"10.1016/j.abb.2025.110401","DOIUrl":"10.1016/j.abb.2025.110401","url":null,"abstract":"","PeriodicalId":8174,"journal":{"name":"Archives of biochemistry and biophysics","volume":"768 ","pages":"Article 110401"},"PeriodicalIF":3.8,"publicationDate":"2025-03-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143750855","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}