Biochimica et biophysica acta. Proteins and proteomics最新文献

{"title":"Green tea polyphenol EGCG acts differentially on end-stage amyloid polymorphs of α-synuclein formed in different polyol osmolytes","authors":"Santosh Devi ,&nbsp;Dushyant K. Garg ,&nbsp;Rajiv Bhat","doi":"10.1016/j.bbapap.2025.141073","DOIUrl":"10.1016/j.bbapap.2025.141073","url":null,"abstract":"<div><div>Synucleinopathies are heterogenous group of disorders characterized by α-synuclein amyloid aggregates in the nervous system. Different synucleinopathy clinical subtypes are encoded by structurally diverse α-synuclein amyloid polymorphs referred to as ‘strains’. The underlying structural differences between polymorphs can potentially hamper the drug design against synucleinopathies. Polyphenolic compounds like EGCG have shown promise in inhibiting and remodeling of α-synuclein amyloid aggregates, but their effects on different polymorphs are not well-studied. The cellular environment is one factor contributing to the heterogeneity in the amyloid landscape. Herein, we generated diverse polymorphs of α-synuclein by fine-tuning its aggregation using different polyol osmolytes, varying in their physicochemical properties. These osmolytes act as globular protein stabilizers and conformational modulators of intrinsically disordered proteins. While the buffer control α-synuclein aggregates were evenly dispersed, the polyol-induced aggregate solutions contained a heterogeneous mixture of <em>co</em>-existing polymorphs, as evidenced by AFM and TEM measurements. The polyol-induced aggregated solutions consisted of a mixture of both fibrillar and nonfibrillar cross-β-rich species. Using various spectroscopic tools, we observed differences in the structures of osmolyte-induced polymorphic aggregates. We incubated these aggregates with EGCG and observed its disparate action over polymorphs wherein the treated species were either disintegrated or structurally altered. Contrary to previous reports, all EGCG-treated polymorphs were β-sheet-rich and seeding-competent. Our findings are relevant in assessing the efficacy of polyphenolic compounds on diverse aggregate strains encoding different proteinopathy variants. The formation of β-sheet-rich species in our study also engenders a more critical examination of EGCG's mode of action on diverse classes of amyloids.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1873 4","pages":"Article 141073"},"PeriodicalIF":2.5,"publicationDate":"2025-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143794633","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Crystal structure of thymidine kinase from the multi-drug resistant col strain of Staphylococcus aureus","authors":"Anam Ashraf ,&nbsp;Ravi Kant Pal ,&nbsp;Md. Imtaiyaz Hassan","doi":"10.1016/j.bbapap.2025.141071","DOIUrl":"10.1016/j.bbapap.2025.141071","url":null,"abstract":"<div><div>Thymidine kinase (TK) is a key enzyme in the salvage pathway of thymidine that produces thymidine monophosphate. TK enzyme activity is tightly coupled to the cell cycle, exhibiting marked fluctuations in expression and activity. We report the crystal structure of TK from the <em>Staphylococcus aureus col</em> strain (Sa-TK), which has emerged as a promising therapeutic target. The overall structure of Sa-TK closely resembles that of human TK. The lasso region in the structure shows an open conformation due to the absence of a natural substrate. The phosphate donor site is bound with sulfate ions from the crystallization conditions. The P-loop is visible, but the complete P-β hairpin cannot be traced due to the flexibility of this region. Sa-TK assembles as a tetramer with unique inter-subunit interactions involving salt bridges between charged residues. Glu136 and Arg184, as well as Arg154 and Glu102 from each of the subunits, have β-sheet interactions that form salt bridges. The catalytically active site residue Glu89 is conserved, which is essential for enzyme activity. Sa-TK lacks a longer C-terminal sequence involved in mitotic regulation through proteolytic degradation, a feature that is likely absent in Sa-TK. The crystal structure of Sa-TK offers detailed insights into its structural and functional properties, highlighting its conserved nature and emphasizing the challenge of developing selective inhibitors that do not affect host TK. This detailed structural information presents a valuable opportunity for the rational design of novel antibacterial agents specifically targeting Sa-TK, offering a promising avenue for combating <em>S. aureus</em> infections.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1873 4","pages":"Article 141071"},"PeriodicalIF":2.5,"publicationDate":"2025-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143785301","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"TMB Stab-pred: Predicting the stability of transmembrane β-barrel proteins using their sequence and structural signatures","authors":"P. Ramakrishna Reddy,&nbsp;A. Kulandaisamy,&nbsp;M. Michael Gromiha","doi":"10.1016/j.bbapap.2025.141070","DOIUrl":"10.1016/j.bbapap.2025.141070","url":null,"abstract":"<div><div>Understanding the folding and stability of transmembrane β-barrel proteins (TMBs) provides insights into their structural integrity, functional mechanisms, and implications for disease states. In this work, we have characterized the important features that influence the folding and stability of TMBs. Our results showed that lipid accessible surface area and transition energy are important for understanding the stability of TMBs. Further, this information was utilized to develop a linear regression-based method for predicting the stability of TMBs. Our method achieved a correlation and mean absolute error (MAE) of 0.96 and 0.94 kcal/mol on the jack-knife test. Moreover, we compared the stability of TMBs with globular all-β proteins and observed that long-range interactions and energetic properties are crucial for maintaining the stability of both β-barrel membrane and all-β globular proteins. On the other hand, side-chain – side-chain hydrogen bonds and lipid accessible surface area are specific to membrane proteins. These features are critical for membrane proteins because they influence a protein to embed within the membrane environment. Further, we have developed a web server, TMB Stab-pred for predicting the stability of TMBs, and it is accessible at <span><span>https://web.iitm.ac.in/bioinfo2/TMBB/index.html</span><svg><path></path></svg></span>.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1873 4","pages":"Article 141070"},"PeriodicalIF":2.5,"publicationDate":"2025-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143794638","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Synovial fluid glycoproteome profiling in knee osteoarthritis: Molecular insights into type 2 diabetes-associated biomarkers and therapeutic targets","authors":"Monidipa Konar ,&nbsp;Bhavneet Kaur ,&nbsp;Uttam Chand Saini ,&nbsp;Sanjay K. Bhadada ,&nbsp;Sadhna Sharma","doi":"10.1016/j.bbapap.2025.141067","DOIUrl":"10.1016/j.bbapap.2025.141067","url":null,"abstract":"<div><div>Type 2 diabetes mellitus (T2DM) and Osteoarthritis (OA) share common risk factors like age, obesity and hypertension. Currently, 52 % of diabetic patients suffer from arthritis. Diabetes facilitates OA by altering lipid metabolism, levels of adipokines &amp; cytokines, accumulation of advanced glycation end products, etc., which affects cartilage &amp; bone health. However, the molecular mechanisms of the association of OA with T2DM remain unexplored. Since diabetes greatly affects the glycosylation status of proteins, the present study focused on identifying glycoproteins that could serve as diagnostic and prognostic markers for identifying osteoarthritis in diabetic individuals by LC-MS/MS. Comparative proteomic analysis revealed 20 significantly altered glycoproteins; among them, thyroxine-binding globulin (THBG), alpha-1-antitrypsin (A1AT), fibrinogen gamma chain (FGG) and angiotensinogen (AGT) were further validated. THBG, A1AT and AGT showed promising potential to identify the comorbid condition in serum and synovial fluid, however, ROC analysis identified THBG as the best candidate glycoprotein marker. Upregulation of THBG in OADM disrupts the bone remodeling cycle, degrades insulin, and promotes the expression of GLUT-1 and MMP-9. Overall, THBG could also serve as a therapeutic target for reducing the progression of osteoarthritis and alleviating pain and bone stiffness associated with the disease.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1873 4","pages":"Article 141067"},"PeriodicalIF":2.5,"publicationDate":"2025-03-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143742091","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Efficient production of a novel recombinant fusion protein of EIEC effector IpaD and EGFP: Biophysical characterization and functional studies","authors":"Sudeshna Halder,&nbsp;Namita Jaiswal,&nbsp;Salari Charan Balajee,&nbsp;Nibedita Mahata","doi":"10.1016/j.bbapap.2025.141066","DOIUrl":"10.1016/j.bbapap.2025.141066","url":null,"abstract":"<div><div>The conserved invasion plasmid antigen D (IpaD) protein demonstrates broad protective capabilities against bacillary dysentery caused by Enteroinvasive <em>Escherichia coli</em> (EIEC) and <em>Shigella</em>. However, the instability of the IpaD protein at room temperature limits its therapeutic potential. The stabilization and efficient production of functional recombinant proteins remain critical challenges in therapeutic and vaccine development. This study presents a novel fluorescence fusion strategy for producing a stable IpaD-EGFP recombinant protein using a flexible linker (GGGGS)₃. The fusion technique enhances the expression level (∼53 %), solubility (∼77 %), and stability of the IpaD-EGFP fusion protein. Biophysical characterization studies suggest that the IpaD-EGFP fusion protein is stable at refrigerated temperatures for extended periods and up to 1 month at 25 °C. The IpaD-EGFP protein triggers apoptosis in Raw 267.4 cells through activation of caspases 3/7. The protein also induces antibody response in BALB/c mice indicating its immunogenicity. Together, these findings indicate that IpaD-EGFP generated in this study is a potential approach for the design and production of stable IpaD-based protein therapeutics, breaking the expensive “cold chain” of continuous refrigeration. Fusion approach significantly enhanced the solubility, yield, and stability of IpaD, while enabling efficient purification.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1873 4","pages":"Article 141066"},"PeriodicalIF":2.5,"publicationDate":"2025-03-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143630132","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Tracking heme biology with resonance Raman spectroscopy","authors":"Amanda Bartkowiak,&nbsp;Ewa Szczesny-Malysiak,&nbsp;Jakub Dybas","doi":"10.1016/j.bbapap.2025.141065","DOIUrl":"10.1016/j.bbapap.2025.141065","url":null,"abstract":"<div><div>Heme proteins are a large group of biomolecules with heme incorporated as a prosthetic group. Apart from cytochromes present in almost all cell types, many other specific heme proteins are expressed in different kinds of cells, e.g. hemoglobin in the erythrocytes, myoglobin (skeletal and vascular smooth muscle cells), cytoglobin (fibroblasts) and neuroglobin (neurons and retina). Among their wide and diverse biological functions, the most important is their unique ability to bind, store, and transport gaseous molecules, such as oxygen, carbon monoxide, and nitric oxide. Resonance Raman (RR) spectroscopy is an exceptional analytical tool that allows for qualitative and quantitative characterization of heme proteins in biological systems. Due to its high sensitivity, even subtle structural alterations of the heme group can be monitored and tracked during cellular processes. Resonance Raman excitation within the Soret absorption band (390–440 nm) provides rich information on the environment of heme's active site, allowing differentiation of the iron ion oxidation and spin states, and tracking the movement of the porphyrin ring plane in response to the changes in oxygenation status. Herein, we summarize and discuss recent developments in RR applications aimed to link the structure-function relationship of heme proteins within biological systems, connected, e.g., with the formation of hemoglobin (Hb) adducts (nitrosylhemoglobin, cyanhemoglobin, sulfhemoglobin), irreversible Hb alterations deteriorating oxygen binding and differentiation of heme proteins oxidation state within live cells in situ.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1873 3","pages":"Article 141065"},"PeriodicalIF":2.5,"publicationDate":"2025-02-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143497595","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"DSP-1, the major fibronectin type-II protein of donkey seminal plasma is a small heat-shock protein and exhibits chaperone-like activity against thermal and oxidative stress","authors":"Sk Alim ,&nbsp;Sudheer K. Cheppali ,&nbsp;Sonali S. Pawar,&nbsp;Musti J. Swamy","doi":"10.1016/j.bbapap.2025.141064","DOIUrl":"10.1016/j.bbapap.2025.141064","url":null,"abstract":"<div><div>Fibronectin type-II (FnII) proteins are major constituents in the seminal plasma of many mammals and play a crucial role in sperm capacitation. Additionally, the seminal FnII proteins from bull and horse exhibit chaperone-like activity (CLA), by acting as small heat shock proteins (<em>shsp</em>s). The present work demonstrates that the major FnII protein of donkey seminal plasma, DSP-1 exhibits CLA with broad specificity and protects various client proteins such as alcohol dehydrogenase, lactate dehydrogenase and enolase against thermal and oxidative stress. Binding of phosphorylcholine (PrC) – the head group moiety of choline phospholipids, which are the physiological ligands of DSP-1 – decreased the CLA whereas binding of 1,2-dioleoyl-<em>sn</em>-glycero-3-phospholcholine (DOPC) increased the CLA. Biophysical studies suggested that these contrasting effects on the CLA by phosphorylcholine and diacyl phosphatidylcholine could be attributed to changes in the surface hydrophobicity of DSP-1 upon binding to these ligands. Interestingly, binding of PrC reduced DSP-1 tetramers to monomers with lower surface hydrophobicity, whereas binding to DOPC liposomes increased its surface hydrophobicity. These results, which demonstrate that DSP-1 exhibits CLA and functions as a molecular chaperone, expand the family of mammalian seminal FnII proteins that function as <em>shsp</em>s.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1873 3","pages":"Article 141064"},"PeriodicalIF":2.5,"publicationDate":"2025-02-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143432278","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Participation of a cysteine tetrad in the recycling mechanism of methionine sulfoxide reductase A from radiation-tolerant Deinococcus bacteria","authors":"Pascal Rey ,&nbsp;Nicolas Rouhier ,&nbsp;Chloé Carassus ,&nbsp;Arjan de Groot ,&nbsp;Laurence Blanchard","doi":"10.1016/j.bbapap.2025.141063","DOIUrl":"10.1016/j.bbapap.2025.141063","url":null,"abstract":"<div><div>Methionine oxidation leads to the formation of methionine sulfoxide (MetO), which is reduced back to Met by methionine sulfoxide reductases (Msrs). The catalytic mechanism used by A-type Msr (MsrA) for MetO reduction requires a catalytic cysteine (Cys), which is converted to a sulfenic acid. In general, two resolving Cys are required for the regeneration of the catalytic Cys forming two consecutive disulfide bridges, the last one being efficiently reduced by thioredoxin (Trx). Here, we performed the biochemical characterization of MsrA from <em>Deinococcus deserti</em>. It possesses four Cys, two present in the active site motif (18 and 21) and two distal ones (53 and 163). We produced MsrA variants mutated for these cysteines and analyzed their capacity to reduce MetO in the presence of the NADPH-Trx reductase/Trx system, their ability to form heterodimers with Trxs, and their redox status after incubation with MetO. We show that all four Cys are involved in the regeneration process of enzyme activity by Trx. After MetO reduction by Cys18, a first disulfide bridge is formed with Cys21. A second disulfide involving Cys21 with either Cys53 or Cys163 is reduced by Trx, and a third Cys53-Cys163 disulfide can be formed and also reduced by Trx. These findings highlighting for the first time the involvement of a Cys tetrad in the catalytic and regeneration mechanisms for a MsrA are placed in a structural context by performing 3D modelling and discussed in relation to the known recycling mechanisms involving a Cys triad.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1873 3","pages":"Article 141063"},"PeriodicalIF":2.5,"publicationDate":"2025-02-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143389955","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Elucidation of cytotoxicity of α-Synuclein fibrils on immune cells","authors":"Mikhail Matveyenka ,&nbsp;Abid Ali ,&nbsp;Charles L. Mitchell ,&nbsp;Mikhail Sholukh ,&nbsp;Dmitry Kurouski","doi":"10.1016/j.bbapap.2024.141061","DOIUrl":"10.1016/j.bbapap.2024.141061","url":null,"abstract":"<div><div>Progressive aggregation of α-synuclein (α-Syn), a small cytosolic protein involved in cell vesicle trafficking, in the midbrain, hypothalamus, and thalamus is linked to Parkinson's disease (PD). Amyloid oligomers and fibrils formed as a result of such aggregation are highly toxic to neurons. However, it remains unclear whether amyloid-induced toxicity of neurons is the primary mechanism of the progressive neurodegeneration observed upon PD. In the current study, we investigated cytotoxicity exerted by α-Syn fibrils formed in the lipid-free environment, as well as in the presence of two phospholipids, on macrophages, dendritic cells, and microglia. We found that α-Syn fibrils are far more toxic to dendritic cells and microglia compared to neurons. We also observe low toxicity levels of such amyloids to macrophages. Real-time polymerase chain reaction (RT-PCR) results suggest that toxicity of amyloids aggregates is linked to the levels of autophagy in cells. These results suggest that a strong impairment of the immune system in the brain may be the first stop of neurodegenerative processes that are taking place upon the onset of PD.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1873 2","pages":"Article 141061"},"PeriodicalIF":2.5,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142852091","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Replacement of the essential catalytic aspartate with serine leads to an active form of copper-containing nitrite reductase from the denitrifier Sinorhizobium meliloti 2011","authors":"Lorieth A. Guevara Cuasapud ,&nbsp;Pablo J. González ,&nbsp;Félix M. Ferroni ,&nbsp;Andrea B. Duré ,&nbsp;Sergio D. Dalosto ,&nbsp;Maria G. Rivas ,&nbsp;Carlos D. Brondino","doi":"10.1016/j.bbapap.2024.141062","DOIUrl":"10.1016/j.bbapap.2024.141062","url":null,"abstract":"<div><div>We report the molecular, biochemical and spectroscopic characterization and computational calculations of a variant of the copper-containing nitrite reductase from the rhizobial microorganism <em>S. meliloti</em> (<em>Sm</em>NirK), in which the catalytic aspartate residue (Asp_CAT) has been replaced with serine (Ser_CAT, D134S) by site-directed mutagenesis. Like the wild-type enzyme, D134S is a homotrimer with the typical catalytic pocket of two-domain NirK containing two copper centers, one of type 1 (T1) and another of type 2 (T2). The T1 electron transfer center is similar to that of the wild-type enzyme but the electronic and covalent properties of T2 active site are altered by the mutation. As for the wild-type enzyme, the enzymatic activity of D134S is pH-dependent, i.e. it is higher at lower pH values, but the <em>k</em>_cat is an order of magnitude lower. EPR studies showed a decrease in <em>g</em>_‖ and an increase in <em>A</em>_‖ of D134S relative to wild-type enzyme. This indicates changes in the electronic and covalent properties of T2 upon mutation, which affects the reduction potential of T2 and the T1-T2 reduction potential gap. Taken together, this evidence points to the importance of the ligands of the second coordination sphere of T2 in controlling critical parameters in catalysis. The possibility that Asp_CAT/Ser_CAT is the switch that triggers T1 → T2 electron transfer upon T2 nitrite binding and the importance of His_CAT for the pH-dependent catalytic activity of NirK are discussed.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1873 2","pages":"Article 141062"},"PeriodicalIF":2.5,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142913782","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}