Molecular Biology of the Cell最新文献_第4页

EB-SUN, a new microtubule plus-end tracking protein in Drosophila. EB-SUN--果蝇中一种新的微管加端追踪蛋白

IF 3.1 3区生物学

Molecular Biology of the Cell Pub Date : 2024-12-01 Epub Date: 2024-10-30 DOI: 10.1091/mbc.E24-09-0402

Sun K Kim, Stephen L Rogers, Wen Lu, Brad S Lee, Vladimir I Gelfand

{"title":"EB-SUN, a new microtubule plus-end tracking protein in Drosophila.","authors":"Sun K Kim, Stephen L Rogers, Wen Lu, Brad S Lee, Vladimir I Gelfand","doi":"10.1091/mbc.E24-09-0402","DOIUrl":"10.1091/mbc.E24-09-0402","url":null,"abstract":"Microtubule (MT) regulation is essential for oocyte development. In Drosophila, MT stability, polarity, abundance, and orientation undergo dynamic changes across developmental stages. In our effort to identify novel microtubule-associated proteins that regulate MTs in the Drosophila ovary, we identified a previously uncharacterized gene, CG18190, which encodes a novel MT end-binding (EB) protein, which we propose to name EB-SUN. We show that EB-SUN colocalizes with EB1 at growing MT plus-ends in Drosophila S2 cells. Tissue-specific and developmental expression profiles from Paralog Explorer reveal that EB-SUN is predominantly expressed in the ovary and early embryos, while EB1 is ubiquitously expressed. Furthermore, as early as oocyte determination, EB-SUN comets are highly concentrated in oocytes during oogenesis. EB-SUN knockout (KO) results in decreased MT density at the onset of mid-oogenesis (stage 7) and delays oocyte growth during late mid-oogenesis (stage 9). Combining EB-SUN KO with EB1 knockdown (KD) in germ cells significantly further reduces MT density at stage 7. Hatching assays of single protein depletion reveal distinct roles for EB-SUN and EB1 in early embryogenesis, likely due to differences in their expression and binding partners. Notably, all eggs from EB-SUN KO/EB1 KD females fail to hatch, suggesting partial redundancy between these proteins.","PeriodicalId":18735,"journal":{"name":"Molecular Biology of the Cell","volume":" ","pages":"ar147"},"PeriodicalIF":3.1,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142546408","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}

引用次数: 0

After their membrane assembly, Sec18 (NSF) and Sec17 (SNAP) promote membrane fusion. 在膜组装后，Sec18（NSF）和 Sec17（SNAP）会促进膜融合。

IF 3.1 3区生物学

Molecular Biology of the Cell Pub Date : 2024-12-01 Epub Date: 2024-10-30 DOI: 10.1091/mbc.E24-10-0439

Hongki Song, Karina Lopes, Amy Orr, William Wickner

{"title":"After their membrane assembly, Sec18 (NSF) and Sec17 (SNAP) promote membrane fusion.","authors":"Hongki Song, Karina Lopes, Amy Orr, William Wickner","doi":"10.1091/mbc.E24-10-0439","DOIUrl":"10.1091/mbc.E24-10-0439","url":null,"abstract":"The energy that drives membrane fusion can come from either complete SNARE zippering, from Sec17 and Sec18, or both. Sec17 and Sec18 initially form a complex which binds membranes. Sec17, Sec18, and the apolarity of a loop on the N-domain of Sec17 are required for their interdependent membrane association. To determine whether Sec18 and the Sec17 loop apolarity are still required for fusion after their membrane arrival, a hydrophobic transmembrane (TM) anchor was affixed to the N-terminus of Sec17, forming TM-Sec17. Fusion without energy from complete SNARE zippering requires Sec18 as well as either Sec17 or TM-Sec17. Even without the need for membrane targeting, the TM-Sec17 apolar loop strongly stimulates Sec17/18-driven fusion. Thus, Sec18 and the Sec17 apolar loop are first required for membrane targeting, and once bound, drive rapid fusion. Each of these variables-the absence or presence of Sec17, its N-loop apolarity, addition or omission of Sec18, and unimpeded or diminished energy from SNARE zippering-has almost no effect on the amount of trans-SNARE complex, but instead regulates the capacity of docked membranes to fuse.","PeriodicalId":18735,"journal":{"name":"Molecular Biology of the Cell","volume":" ","pages":"ar150"},"PeriodicalIF":3.1,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142546406","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}

引用次数: 0

Regulating transport efficiency through the nuclear pore complex: The role of binding affinity with FG-Nups. 通过核孔复合体调节运输效率：与 FG-Nups 结合亲和力的作用。

IF 4.3 3区生物学

Molecular Biology of the Cell Pub Date : 2024-12-01 Epub Date: 2024-10-30 DOI: 10.1091/mbc.E24-05-0224

Atsushi Matsuda, Mohammad R K Mofrad

{"title":"Regulating transport efficiency through the nuclear pore complex: The role of binding affinity with FG-Nups.","authors":"Atsushi Matsuda, Mohammad R K Mofrad","doi":"10.1091/mbc.E24-05-0224","DOIUrl":"10.1091/mbc.E24-05-0224","url":null,"abstract":"Macromolecules are transported through the nuclear pore complex (NPC) via a series of transient binding and unbinding events with FG-Nups, which are intrinsically disordered proteins anchored to the pore's inner wall. Prior studies suggest that the weak and transient nature of this binding is crucial for maintaining the transported molecules' diffusivity. In this study, we explored the relationship between binding kinetics and transport efficiency using Brownian dynamics simulations. Our results indicate that the duration of binding is a critical factor in regulating transport efficiency. Specifically, excessively short binding durations insufficiently facilitate transport, while overly long durations impede molecular movement. We calculated the optimal binding duration for efficient molecular transport and found that it aligns with other theoretical predictions. Additionally, the calculated value is comparable to experimental measurements of the association timescale between nuclear transport receptors and FG-Nups at a single binding site. Our study provides a quantitative framework that bridges local molecular interactions with overall transport dynamics through the NPC, offering valuable insights into the mechanisms governing selective molecular transport.","PeriodicalId":18735,"journal":{"name":"Molecular Biology of the Cell","volume":" ","pages":"ar149"},"PeriodicalIF":4.3,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142546409","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}

引用次数: 0

PunctaFinder: An algorithm for automated spot detection in fluorescence microscopy images. PunctaFinder：荧光显微镜图像中斑点自动检测算法。

IF 3.1 3区生物学

Molecular Biology of the Cell Pub Date : 2024-12-01 Epub Date: 2024-11-13 DOI: 10.1091/mbc.E24-06-0254

Hanna M Terpstra, Rubén Gómez-Sánchez, Annemiek C Veldsink, Tegan A Otto, Liesbeth M Veenhoff, Matthias Heinemann

{"title":"PunctaFinder: An algorithm for automated spot detection in fluorescence microscopy images.","authors":"Hanna M Terpstra, Rubén Gómez-Sánchez, Annemiek C Veldsink, Tegan A Otto, Liesbeth M Veenhoff, Matthias Heinemann","doi":"10.1091/mbc.E24-06-0254","DOIUrl":"10.1091/mbc.E24-06-0254","url":null,"abstract":"Fluorescence microscopy has revolutionized biological research by enabling the visualization of subcellular structures at high resolution. With the increasing complexity and volume of microscopy data, there is a growing need for automated image analysis to ensure efficient and consistent interpretation. In this study, we introduce PunctaFinder, a novel Python-based algorithm designed to detect puncta, small bright spots, in raw fluorescence microscopy images without image denoising or signal enhancement steps. Furthermore, unlike other available spot detectors, PunctaFinder not only detects puncta, but also defines the cytoplasmic region, making it a valuable tool to quantify target molecule localization in cellular contexts. PunctaFinder is a widely applicable punctum detector and size estimator, as evidenced by its successful detection of Atg9-positive vesicles, lipid droplets, aggregates of a destabilized luciferase mutant, and the nuclear pore complex. Notably, PunctaFinder excels in detecting puncta in images with a relatively low resolution and signal-to-noise ratio, demonstrating its capability to identify dim puncta and puncta of dynamic target molecules. PunctaFinder reliably detects puncta in fluorescence microscopy images where automated analysis was not possible before, providing researchers with an efficient and robust method for punctum quantification in fluorescence microscopy images.","PeriodicalId":18735,"journal":{"name":"Molecular Biology of the Cell","volume":" ","pages":"mr9"},"PeriodicalIF":3.1,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142624080","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}

引用次数: 0

AI: A transformative opportunity in cell biology.

IF 3.1 3区生物学

Molecular Biology of the Cell Pub Date : 2024-12-01 DOI: 10.1091/mbc.E24-09-0415

Ambrose Carr, Jonah Cool, Theofanis Karaletsos, Donghui Li, Alan R Lowe, Stephani Otte, Sandra L Schmid

引用次数: 0

Significantly reduced, but balanced, rates of mitochondrial fission and fusion are sufficient to maintain the integrity of yeast mitochondrial DNA. 线粒体裂变和融合的速率显著降低但保持平衡，足以维持酵母线粒体 DNA 的完整性。

IF 3.1 3区生物学

Molecular Biology of the Cell Pub Date : 2024-12-01 Epub Date: 2024-11-13 DOI: 10.1091/mbc.E24-07-0306

Brett T Wisniewski, Jason C Casler, Laura L Lackner

{"title":"Significantly reduced, but balanced, rates of mitochondrial fission and fusion are sufficient to maintain the integrity of yeast mitochondrial DNA.","authors":"Brett T Wisniewski, Jason C Casler, Laura L Lackner","doi":"10.1091/mbc.E24-07-0306","DOIUrl":"10.1091/mbc.E24-07-0306","url":null,"abstract":"Mitochondria exist as dynamic tubular networks and the morphology of these networks impacts organelle function and cell health. Mitochondrial morphology is maintained in part by the opposing activities of mitochondrial fission and fusion. Mitochondrial fission and fusion are also required to maintain mitochondrial DNA (mtDNA) integrity. In Saccharomyces cerevisiae, the simultaneous inhibition of mitochondrial fission and fusion results in increased mtDNA mutation and the consequent loss of respiratory competence. The mechanism by which fission and fusion maintain mtDNA integrity is not fully understood. Previous work demonstrates that mtDNA is spatially linked to mitochondrial fission sites. Here, we extend this finding using live-cell imaging to localize mtDNA to mitochondrial fusion sites. While mtDNA is present at sites of mitochondrial fission and fusion, mitochondrial fission and fusion rates are not altered in cells lacking mtDNA. Using alleles that alter mitochondrial fission and fusion rates, we find that mtDNA integrity can be maintained in cells with significantly reduced, but balanced, rates of fission and fusion. In addition, we find that increasing mtDNA copy number reduces the loss of respiratory competence in double mitochondrial fission-fusion mutants. Our findings add novel insights into the relationship between mitochondrial dynamics and mtDNA integrity.","PeriodicalId":18735,"journal":{"name":"Molecular Biology of the Cell","volume":" ","pages":"br25"},"PeriodicalIF":3.1,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142624082","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}

引用次数: 0

The TOG5 domain of CKAP5 is required to interact with F-actin and promote microtubule advancement in neurons. CKAP5的TOG5结构域需要与F-肌动蛋白相互作用，并促进神经元中微管的前进。

IF 3.1 3区生物学

Molecular Biology of the Cell Pub Date : 2024-12-01 Epub Date: 2024-11-06 DOI: 10.1091/mbc.E24-05-0202

Garrett M Cammarata, Burcu Erdogan, Jan Sabo, Yusuf Kayaer, Michaela Dujava Zdimalova, Filip Engström, Urvika Gupta, Jasming Senel, Tara O'Brien, Chiedza Sibanda, Akanksha Thawani, Eric S Folker, Marcus Braun, Zdenek Lansky, Laura A Lowery

{"title":"The TOG5 domain of CKAP5 is required to interact with F-actin and promote microtubule advancement in neurons.","authors":"Garrett M Cammarata, Burcu Erdogan, Jan Sabo, Yusuf Kayaer, Michaela Dujava Zdimalova, Filip Engström, Urvika Gupta, Jasming Senel, Tara O'Brien, Chiedza Sibanda, Akanksha Thawani, Eric S Folker, Marcus Braun, Zdenek Lansky, Laura A Lowery","doi":"10.1091/mbc.E24-05-0202","DOIUrl":"10.1091/mbc.E24-05-0202","url":null,"abstract":"Microtubule (MT) and F-actin cytoskeletal cross-talk and organization are important aspects of axon guidance mechanisms, but how associated proteins facilitate this function remains largely unknown. While the MT-associated protein, CKAP5 (XMAP215/ch-TOG), has been best characterized as a MT polymerase, we have recently highlighted a novel role for CKAP5 in facilitating interactions between MT and F-actin in vitro and in embryonic Xenopus laevis neuronal growth cones. However, the mechanism by which it does so is unclear. Here, using in vitro reconstitution assays coupled with total internal reflection fluorescence microscopy, we report that the TOG5 domain of CKAP5 is necessary for its ability to bind to and bundle actin filaments, as well as to cross-link MTs and F-actin in vitro. Additionally, we show that this novel MT/F-actin cross-linking function of CKAP5 is possible even in MT polymerase-incompetent mutants of CKAP5 in vivo. Indeed, CKAP5 requires both MT and F-actin binding, but not MT polymerization, to promote MT-F-actin alignment in growth cones and axon outgrowth. Taken together, our findings provide mechanistic insights into how MT populations penetrate the growth cone periphery through CKAP5-facilitated interaction with F-actin during axon outgrowth and guidance.","PeriodicalId":18735,"journal":{"name":"Molecular Biology of the Cell","volume":" ","pages":"br24"},"PeriodicalIF":3.1,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142591312","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}

引用次数: 0

The transmembrane domain of the desmosomal cadherin desmoglein-1 governs lipid raft association to promote desmosome adhesive strength. 脱丝体粘附蛋白 desmoglein-1 的跨膜结构域控制着脂质筏的结合，以促进脱丝体的粘附强度。

IF 3.1 3区生物学

Molecular Biology of the Cell Pub Date : 2024-12-01 Epub Date: 2024-11-06 DOI: 10.1091/mbc.E24-05-0200

Stephanie E Zimmer, William Giang, Ilya Levental, Andrew P Kowalczyk

{"title":"The transmembrane domain of the desmosomal cadherin desmoglein-1 governs lipid raft association to promote desmosome adhesive strength.","authors":"Stephanie E Zimmer, William Giang, Ilya Levental, Andrew P Kowalczyk","doi":"10.1091/mbc.E24-05-0200","DOIUrl":"10.1091/mbc.E24-05-0200","url":null,"abstract":"Cholesterol- and sphingolipid-enriched domains called lipid rafts are hypothesized to selectively coordinate protein complex assembly within the plasma membrane to regulate cellular functions. Desmosomes are mechanically resilient adhesive junctions that associate with lipid raft membrane domains, yet the mechanisms directing raft association of the desmosomal proteins, particularly the transmembrane desmosomal cadherins, are poorly understood. We identified the desmoglein-1 (DSG1) transmembrane domain (TMD) as a key determinant of desmoglein lipid raft association and designed a panel of DSG1TMD variants to assess the contribution of TMD physicochemical properties (length, bulkiness, and palmitoylation) to DSG1 lipid raft association. Sucrose gradient fractionations revealed that TMD length and bulkiness, but not palmitoylation, govern DSG1 lipid raft association. Further, DSG1 raft association determines plakoglobin recruitment to raft domains. Super-resolution imaging and functional assays uncovered a strong relationship between the efficiency of DSG1TMD lipid raft association and the formation of morphologically and functionally robust desmosomes. Lipid raft association regulated both desmosome assembly dynamics and DSG1 cell surface stability, indicating that DSG1 lipid raft association is required for both desmosome formation and maintenance. These studies identify the biophysical properties of desmoglein transmembrane domains as key determinants of lipid raft association and desmosome adhesive function.","PeriodicalId":18735,"journal":{"name":"Molecular Biology of the Cell","volume":" ","pages":"ar152"},"PeriodicalIF":3.1,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142591315","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}

引用次数: 0

Diffusion within the synaptonemal complex can account for signal transduction along meiotic chromosomes. 突触复合体内部的扩散可以解释减数分裂染色体上的信号转导。

IF 3.1 3区生物学

Molecular Biology of the Cell Pub Date : 2024-12-01 Epub Date: 2024-10-30 DOI: 10.1091/mbc.E24-05-0225

Lexy von Diezmann, Chloe Bristow, Ofer Rog

{"title":"Diffusion within the synaptonemal complex can account for signal transduction along meiotic chromosomes.","authors":"Lexy von Diezmann, Chloe Bristow, Ofer Rog","doi":"10.1091/mbc.E24-05-0225","DOIUrl":"10.1091/mbc.E24-05-0225","url":null,"abstract":"Meiotic chromosomes efficiently transduce information along their length to regulate the distribution of genetic exchanges (crossovers). However, the mode of signal transduction remains unknown. A conserved protein interface called the synaptonemal complex forms between the parental chromosomes. The synaptonemal complex exhibits liquid-like behaviors, suggesting that the diffusion of signaling molecules along its length could coordinate crossover formation. Here, we directly test the feasibility of such a mechanism by tracking a component of the synaptonemal complex (SYP-3) and a conserved regulator of exchanges (ZHP-3) in live Caenorhabditis elegans gonads. While we find that both proteins diffuse within the synaptonemal complex, ZHP-3 diffuses 4- and 9-fold faster than SYP-3 before and after crossover designation, respectively. We use these measurements to parameterize a physical model for signal transduction. We find that ZHP-3, but not SYP-3, can explore the lengths of chromosomes on the time scale of crossover designation, consistent with a role in the spatial regulation of exchanges. Given the conservation of ZHP-3 paralogues across eukaryotes, we propose that diffusion along the synaptonemal complex may be a conserved mechanism of meiotic regulation. More broadly, our work explores how diffusion compartmentalized by condensates could regulate crucial chromosomal functions.","PeriodicalId":18735,"journal":{"name":"Molecular Biology of the Cell","volume":" ","pages":"ar148"},"PeriodicalIF":3.1,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142546407","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}

引用次数: 0

GpsB interacts with FtsZ in multiple species and may serve as an accessory Z-ring anchor. 在多个物种中，GpsB 与 FtsZ 相互作用，可能充当 Z 环的辅助锚。

IF 3.1 3区生物学

Molecular Biology of the Cell Pub Date : 2024-11-27 DOI: 10.1091/mbc.E24-07-0302

Dipanwita Bhattacharya, Asher King, Lily McKnight, Pilar Horigian, Prahathees J Eswara

{"title":"GpsB interacts with FtsZ in multiple species and may serve as an accessory Z-ring anchor.","authors":"Dipanwita Bhattacharya, Asher King, Lily McKnight, Pilar Horigian, Prahathees J Eswara","doi":"10.1091/mbc.E24-07-0302","DOIUrl":"https://doi.org/10.1091/mbc.E24-07-0302","url":null,"abstract":"Bacterial cytokinesis commences when a tubulin-like GTPase, FtsZ, forms a Z-ring to mark the division site. Synchronized movement of Z-ring filaments and peptidoglycan synthesis along the axis of division generates a division septum to separate the daughter cells. Thus, FtsZ needs to be linked to the peptidoglycan synthesis machinery. GpsB is a highly conserved protein among species of the Firmicutes phylum known to regulate peptidoglycan synthesis. Previously, we showed that GpsB directly binds to FtsZ by recognizing a signature sequence in its C-terminal tail (CTT) region. As the GpsB recognition sequence is also present in Bacillus subtilis, we speculated that GpsB may interact with FtsZ in this organism. Earlier reports revealed that disruption of gpsB and ftsA or gpsB and ezrA is deleterious. Given that both FtsA and EzrA also target the CTT of FtsZ for interaction, we hypothesized that in the absence of other FtsZ partners, GpsB-FtsZ interaction may become apparent. Our data confirms that is the case, and reveal that GpsB interacts with FtsZ in multiple species and stimulates the GTPase activity of the latter. Moreover, it appears that GpsB may serve as an accessory Z-ring anchor such as when FtsA, one of the main anchors, is absent.","PeriodicalId":18735,"journal":{"name":"Molecular Biology of the Cell","volume":" ","pages":"mbcE24070302"},"PeriodicalIF":3.1,"publicationDate":"2024-11-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142739887","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}

引用次数: 0