Pub Date : 2025-08-16DOI: 10.1016/j.sbi.2025.103137
Rui João Loureiro, Satyabrata Maiti, Kuntal Mondal, Sunandan Mukherjee, Janusz M. Bujnicki
RNA and RNA–protein (RNP) complexes are central to many cellular processes, but the determination of their structures remains challenging due to RNA flexibility and interaction diversity. This review highlights recent computational advances, particularly from the past two years, in predicting and analyzing RNA and RNP structures. We discuss template-based modeling, docking, molecular simulations, and deep learning approaches, with an emphasis on emerging hybrid methods that integrate these strategies. Special attention is given to tools for modeling conformational heterogeneity, folding pathways, and dynamic binding. We also outline machine learning and simulation techniques for ensemble prediction and explore future directions including quantum-enhanced modeling. Together, these developments are enabling more accurate and scalable modeling of both the static and dynamic aspects of RNA and RNP complexes.
{"title":"Modeling flexible RNA 3D structures and RNA-protein complexes","authors":"Rui João Loureiro, Satyabrata Maiti, Kuntal Mondal, Sunandan Mukherjee, Janusz M. Bujnicki","doi":"10.1016/j.sbi.2025.103137","DOIUrl":"10.1016/j.sbi.2025.103137","url":null,"abstract":"<div><div>RNA and RNA–protein (RNP) complexes are central to many cellular processes, but the determination of their structures remains challenging due to RNA flexibility and interaction diversity. This review highlights recent computational advances, particularly from the past two years, in predicting and analyzing RNA and RNP structures. We discuss template-based modeling, docking, molecular simulations, and deep learning approaches, with an emphasis on emerging hybrid methods that integrate these strategies. Special attention is given to tools for modeling conformational heterogeneity, folding pathways, and dynamic binding. We also outline machine learning and simulation techniques for ensemble prediction and explore future directions including quantum-enhanced modeling. Together, these developments are enabling more accurate and scalable modeling of both the static and dynamic aspects of RNA and RNP complexes.</div></div>","PeriodicalId":10887,"journal":{"name":"Current opinion in structural biology","volume":"94 ","pages":"Article 103137"},"PeriodicalIF":6.1,"publicationDate":"2025-08-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144852624","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-08-14DOI: 10.1016/j.sbi.2025.103133
Liming Qiu , Xiaoqin Zou
RNA aptamers possess a remarkable ability to selectively target a diverse spectrum of biomolecules with exceptional affinity and specificity. Their distinctive physical and chemical attributes have driven extensive research into their therapeutic, diagnostic, and analytical applications. However, experimental approaches alone are insufficient to meet the growing demand. As a result, accurate and efficient computational methods are playing an increasingly vital role in RNA aptamer sequence design and structural modeling. Recent breakthroughs in biomolecular structure prediction, particularly through deep learning, have further spurred the development of innovative algorithms. In this review, we summarize current computational models for RNA aptamer structure prediction and design, highlighting recent advances in the field.
{"title":"Advances in Protein-RNA aptamer recognition and modeling: Current trends and future perspectives","authors":"Liming Qiu , Xiaoqin Zou","doi":"10.1016/j.sbi.2025.103133","DOIUrl":"10.1016/j.sbi.2025.103133","url":null,"abstract":"<div><div>RNA aptamers possess a remarkable ability to selectively target a diverse spectrum of biomolecules with exceptional affinity and specificity. Their distinctive physical and chemical attributes have driven extensive research into their therapeutic, diagnostic, and analytical applications. However, experimental approaches alone are insufficient to meet the growing demand. As a result, accurate and efficient computational methods are playing an increasingly vital role in RNA aptamer sequence design and structural modeling. Recent breakthroughs in biomolecular structure prediction, particularly through deep learning, have further spurred the development of innovative algorithms. In this review, we summarize current computational models for RNA aptamer structure prediction and design, highlighting recent advances in the field.</div></div>","PeriodicalId":10887,"journal":{"name":"Current opinion in structural biology","volume":"94 ","pages":"Article 103133"},"PeriodicalIF":6.1,"publicationDate":"2025-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144830604","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-08-14DOI: 10.1016/j.sbi.2025.103135
Alfie-Louise R. Brownless , Dariia Yehorova , Colin L. Welsh , Shina Caroline Lynn Kamerlin
The advent of AlphaFold and consumer large language models have elicited unprecedented development of artificial intelligence (AI). AI has had substantial impact in every area of research, including in molecular biology. This is principally in thanks to contributions to the Protein Data Bank and various genome sequence databases, providing an astronomical amount of data for model training. These databases contain evolutionary information explicitly and implicitly, allowing accurate predictions and deep insights into biological questions. Here, we describe recent state-of-the-art applications of AI that exploit evolutionary relationships. This includes structure prediction and design, conformational ensemble generation, and functional site identification. We present a brief snapshot of AI usage in studying protein structure and dynamics, a field that is advancing at breakneck speed.
{"title":"Generative AI techniques for conformational diversity and evolutionary adaptation of proteins","authors":"Alfie-Louise R. Brownless , Dariia Yehorova , Colin L. Welsh , Shina Caroline Lynn Kamerlin","doi":"10.1016/j.sbi.2025.103135","DOIUrl":"10.1016/j.sbi.2025.103135","url":null,"abstract":"<div><div>The advent of AlphaFold and consumer large language models have elicited unprecedented development of artificial intelligence (AI). AI has had substantial impact in every area of research, including in molecular biology. This is principally in thanks to contributions to the Protein Data Bank and various genome sequence databases, providing an astronomical amount of data for model training. These databases contain evolutionary information explicitly and implicitly, allowing accurate predictions and deep insights into biological questions. Here, we describe recent state-of-the-art applications of AI that exploit evolutionary relationships. This includes structure prediction and design, conformational ensemble generation, and functional site identification. We present a brief snapshot of AI usage in studying protein structure and dynamics, a field that is advancing at breakneck speed.</div></div>","PeriodicalId":10887,"journal":{"name":"Current opinion in structural biology","volume":"94 ","pages":"Article 103135"},"PeriodicalIF":6.1,"publicationDate":"2025-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144840958","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Enzymes are inherently dynamic entities, with their functions intricately governed by the interplay between conformational dynamics - ranging from local residue fluctuations to global motions - and biochemical activity. Deciphering how such dynamics coordinate higher-order cooperativity across multiple timescales to drive catalysis remains a fundamental challenge. This mini-review highlights the role of large-scale, collective motions involving domain-level displacements and hinge-based rearrangements, which not only facilitate substrate recognition, transformation, and release, but also emerge from and propagate through multidirectional allosteric interactions. Such dynamic mechanochemical coupling reflects evolutionary memory and provides a blueprint for enzyme design innovations.
{"title":"Global dynamics behind enzyme catalysis, evolution, and design","authors":"Burcu Aykac Fas , Zeynep Erge Akbas Buz , Turkan Haliloglu","doi":"10.1016/j.sbi.2025.103131","DOIUrl":"10.1016/j.sbi.2025.103131","url":null,"abstract":"<div><div>Enzymes are inherently dynamic entities, with their functions intricately governed by the interplay between conformational dynamics - ranging from local residue fluctuations to global motions - and biochemical activity. Deciphering how such dynamics coordinate higher-order cooperativity across multiple timescales to drive catalysis remains a fundamental challenge. This mini-review highlights the role of large-scale, collective motions involving domain-level displacements and hinge-based rearrangements, which not only facilitate substrate recognition, transformation, and release, but also emerge from and propagate through multidirectional allosteric interactions. Such dynamic mechanochemical coupling reflects evolutionary memory and provides a blueprint for enzyme design innovations.</div></div>","PeriodicalId":10887,"journal":{"name":"Current opinion in structural biology","volume":"94 ","pages":"Article 103131"},"PeriodicalIF":6.1,"publicationDate":"2025-08-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144813912","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-08-06DOI: 10.1016/j.sbi.2025.103130
Weihua Qiu , Youzhong Guo
The native cell membrane nanoparticles (NCMN) system utilizes membrane-active polymers specifically designed and optimized to extract and stabilize membrane proteins in the form of NCMN particlesfor biochemical and biophysical characterization. The NCMN system is a genuine and advanced detergent-free approach inspired by the membrane activity of the styrene–maleic acid copolymers (SMA), distinguishing it from the nanodisc technology, Salipro technology, and Peptidisc technology. This review introduces the current advancements in the NCMN system, including the development of NCMN polymers, the application of the NCMN system for single-particle cryo-EM analysis, and the functional characterization of membrane proteins.
{"title":"Advances in native cell membrane nanoparticles system","authors":"Weihua Qiu , Youzhong Guo","doi":"10.1016/j.sbi.2025.103130","DOIUrl":"10.1016/j.sbi.2025.103130","url":null,"abstract":"<div><div>The native cell membrane nanoparticles (NCMN) system utilizes membrane-active polymers specifically designed and optimized to extract and stabilize membrane proteins in the form of NCMN particlesfor biochemical and biophysical characterization. The NCMN system is a genuine and advanced detergent-free approach inspired by the membrane activity of the styrene–maleic acid copolymers (SMA), distinguishing it from the nanodisc technology, Salipro technology, and Peptidisc technology. This review introduces the current advancements in the NCMN system, including the development of NCMN polymers, the application of the NCMN system for single-particle cryo-EM analysis, and the functional characterization of membrane proteins.</div></div>","PeriodicalId":10887,"journal":{"name":"Current opinion in structural biology","volume":"94 ","pages":"Article 103130"},"PeriodicalIF":6.1,"publicationDate":"2025-08-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144781331","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-08-05DOI: 10.1016/j.sbi.2025.103122
Nancy M. Elbaz, Mahmoud L. Nasr
The stabilization of HIV-1 gp160 trimers (Env) within phospholipid bilayer nanodiscs has provided critical structural insights into the membrane-proximal external region (MPER) and the broader dynamics of gp160. Cryo-EM and molecular simulations reveal that the membrane context preserves the MPER architecture and captures spontaneous trimer asymmetry, as well as ectodomain tilting. These dynamic properties expose vulnerable epitopes that are targeted by broadly neutralizing antibodies (bnAbs). Studies using nanodiscs have highlighted how interactions with the membrane affect the structure of gp160, the accessibility of epitopes, and the mechanisms of neutralization, providing important insights for immunogen design. Unlike soluble SOSIP and IDL constructs, full-length nanodisc-embedded gp160 maintains its native stability, flexibility, and the complete set of neutralization epitopes, suggesting that membrane-mimicking platforms are essential for the rational design of next-generation HIV vaccines targeting conserved regions, such as the MPER.
{"title":"HIV-1 gp160 in nanodiscs: Unravelling structures and guiding vaccine design","authors":"Nancy M. Elbaz, Mahmoud L. Nasr","doi":"10.1016/j.sbi.2025.103122","DOIUrl":"10.1016/j.sbi.2025.103122","url":null,"abstract":"<div><div>The stabilization of HIV-1 gp160 trimers (Env) within phospholipid bilayer nanodiscs has provided critical structural insights into the membrane-proximal external region (MPER) and the broader dynamics of gp160. Cryo-EM and molecular simulations reveal that the membrane context preserves the MPER architecture and captures spontaneous trimer asymmetry, as well as ectodomain tilting. These dynamic properties expose vulnerable epitopes that are targeted by broadly neutralizing antibodies (bnAbs). Studies using nanodiscs have highlighted how interactions with the membrane affect the structure of gp160, the accessibility of epitopes, and the mechanisms of neutralization, providing important insights for immunogen design. Unlike soluble SOSIP and IDL constructs, full-length nanodisc-embedded gp160 maintains its native stability, flexibility, and the complete set of neutralization epitopes, suggesting that membrane-mimicking platforms are essential for the rational design of next-generation HIV vaccines targeting conserved regions, such as the MPER.</div></div>","PeriodicalId":10887,"journal":{"name":"Current opinion in structural biology","volume":"94 ","pages":"Article 103122"},"PeriodicalIF":6.1,"publicationDate":"2025-08-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144772465","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-08-05DOI: 10.1016/j.sbi.2025.103127
R. Gonzalo Parra , Diego U. Ferreiro
The controlled dissipation of chemical potentials is the fundamental way cells make a living. Enzyme-mediated catalysis allows the various transformations to proceed at biologically relevant rates with remarkable precision and efficiency. Theory, experiments, and computational studies coincide to show that local frustration is a useful concept to relate protein dynamics with catalytic power. Local frustration gives rise to the asperities of the energy landscapes that can harness the thermal fluctuations to guide the functional protein motions. We review here recent advances into these relationships from various fields of protein science. The biologically relevant dynamics is tuned by the evolution of protein sequences that modulate local frustration patterns to near-optimal values.
{"title":"Frustration, dynamics, and catalysis","authors":"R. Gonzalo Parra , Diego U. Ferreiro","doi":"10.1016/j.sbi.2025.103127","DOIUrl":"10.1016/j.sbi.2025.103127","url":null,"abstract":"<div><div>The controlled dissipation of chemical potentials is the fundamental way cells make a living. Enzyme-mediated catalysis allows the various transformations to proceed at biologically relevant rates with remarkable precision and efficiency. Theory, experiments, and computational studies coincide to show that local frustration is a useful concept to relate protein dynamics with catalytic power. Local frustration gives rise to the asperities of the energy landscapes that can harness the thermal fluctuations to guide the functional protein motions. We review here recent advances into these relationships from various fields of protein science. The biologically relevant dynamics is tuned by the evolution of protein sequences that modulate local frustration patterns to near-optimal values.</div></div>","PeriodicalId":10887,"journal":{"name":"Current opinion in structural biology","volume":"94 ","pages":"Article 103127"},"PeriodicalIF":6.1,"publicationDate":"2025-08-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144772464","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-08-05DOI: 10.1016/j.sbi.2025.103126
Tanaya Basu Roy , Mana Heidari , Nikolay V. Dokholyan
Optogenetically regulated enzymes offer unprecedented spatiotemporal control over protein activity, intermolecular interactions, and intracellular signaling. Many design strategies have been developed for their fabrication based on the principles of intrinsic allostery, oligomerization or ‘split’ status, intracellular compartmentalization, and steric hindrance. In addition to employing photosensory domains as part of the traditional optogenetic toolset, the specificity of effector domains has also been leveraged for endogenous applications. Here, we discuss the dynamics of light activation while providing a bird's eye view of the crafting approaches, targets, and impact of optogenetic enzymes in orchestrating cellular functions, as well as the bottlenecks and an outlook into the future.
{"title":"Optogenetic enzymes: A deep dive into design and impact","authors":"Tanaya Basu Roy , Mana Heidari , Nikolay V. Dokholyan","doi":"10.1016/j.sbi.2025.103126","DOIUrl":"10.1016/j.sbi.2025.103126","url":null,"abstract":"<div><div>Optogenetically regulated enzymes offer unprecedented spatiotemporal control over protein activity, intermolecular interactions, and intracellular signaling. Many design strategies have been developed for their fabrication based on the principles of intrinsic allostery, oligomerization or ‘split’ status, intracellular compartmentalization, and steric hindrance. In addition to employing photosensory domains as part of the traditional optogenetic toolset, the specificity of effector domains has also been leveraged for endogenous applications. Here, we discuss the dynamics of light activation while providing a bird's eye view of the crafting approaches, targets, and impact of optogenetic enzymes in orchestrating cellular functions, as well as the bottlenecks and an outlook into the future.</div></div>","PeriodicalId":10887,"journal":{"name":"Current opinion in structural biology","volume":"94 ","pages":"Article 103126"},"PeriodicalIF":6.1,"publicationDate":"2025-08-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144781330","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-08-04DOI: 10.1016/j.sbi.2025.103125
Virgil A. Woods , Shivani Sharma , Alexis M. Lemberikman , Daniel A. Keedy
Protein tyrosine phosphatases (PTPs) are a family of enzymes that play critical roles in intracellular signaling and regulation. PTPs are conformationally dynamic, exhibiting motions of catalytic loops and additional regions of the structurally conserved catalytic domain. However, many questions remain about how dynamics contribute to catalysis and allostery in PTPs, how these behaviors vary among evolutionarily divergent PTP family members, and how mutations and ligands reshape dynamics to modulate PTP function. Recently, our understanding in these areas has expanded significantly, thanks to novel applications of existing methods and emergence of new approaches in structural biology and biophysics. Here we review exciting advances in this realm from the last few years. We organize our commentary both by experimental and computational methodologies, including solution techniques, avant-garde crystallography, molecular dynamics simulations, and bioinformatics, and also by scientific focus, including regulatory mechanisms, mutations and protein engineering, and small-molecule ligands such as allosteric modulators.
{"title":"Orchestrating function: Concerted dynamics, allostery, and catalysis in protein tyrosine phosphatases","authors":"Virgil A. Woods , Shivani Sharma , Alexis M. Lemberikman , Daniel A. Keedy","doi":"10.1016/j.sbi.2025.103125","DOIUrl":"10.1016/j.sbi.2025.103125","url":null,"abstract":"<div><div>Protein tyrosine phosphatases (PTPs) are a family of enzymes that play critical roles in intracellular signaling and regulation. PTPs are conformationally dynamic, exhibiting motions of catalytic loops and additional regions of the structurally conserved catalytic domain. However, many questions remain about how dynamics contribute to catalysis and allostery in PTPs, how these behaviors vary among evolutionarily divergent PTP family members, and how mutations and ligands reshape dynamics to modulate PTP function. Recently, our understanding in these areas has expanded significantly, thanks to novel applications of existing methods and emergence of new approaches in structural biology and biophysics. Here we review exciting advances in this realm from the last few years. We organize our commentary both by experimental and computational methodologies, including solution techniques, avant-garde crystallography, molecular dynamics simulations, and bioinformatics, and also by scientific focus, including regulatory mechanisms, mutations and protein engineering, and small-molecule ligands such as allosteric modulators.</div></div>","PeriodicalId":10887,"journal":{"name":"Current opinion in structural biology","volume":"94 ","pages":"Article 103125"},"PeriodicalIF":6.1,"publicationDate":"2025-08-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144768528","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-07-31DOI: 10.1016/j.sbi.2025.103128
Anand Srivastava
Since the publication of the first papers in the early 1990s, molecular simulation as a reliable biophysical tool in the area of membrane biophysics has come a long way. Advances in simulation algorithms, coupled with exascale computing have pushed the size and time scales of biomolecular membrane simulations to scales where connections to experiments are made with higher fidelity. When integrated with experimental data in a theoretically well-grounded manner, current biomolecular simulations are providing indispensable insights that cannot be obtained through experiments alone. Here, I summarize some recent developments where simulations have allowed a deeper understanding in membrane spatiotemporal organization. I also discuss the need for transformative method developments to meet recent breakthroughs in experimental measurements at molecular scales.
{"title":"Emerging paradigms in the lateral and transverse organization in biological membrane and their functional implications: Connecting the dots with biomolecular simulations","authors":"Anand Srivastava","doi":"10.1016/j.sbi.2025.103128","DOIUrl":"10.1016/j.sbi.2025.103128","url":null,"abstract":"<div><div>Since the publication of the first papers in the early 1990s, molecular simulation as a reliable biophysical tool in the area of membrane biophysics has come a long way. Advances in simulation algorithms, coupled with exascale computing have pushed the size and time scales of biomolecular membrane simulations to scales where connections to experiments are made with higher fidelity. When integrated with experimental data in a theoretically well-grounded manner, current biomolecular simulations are providing indispensable insights that cannot be obtained through experiments alone. Here, I summarize some recent developments where simulations have allowed a deeper understanding in membrane spatiotemporal organization. I also discuss the need for transformative method developments to meet recent breakthroughs in experimental measurements at molecular scales.</div></div>","PeriodicalId":10887,"journal":{"name":"Current opinion in structural biology","volume":"94 ","pages":"Article 103128"},"PeriodicalIF":6.1,"publicationDate":"2025-07-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144739059","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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