Protein Science最新文献_第4页

Methods for detecting, building, and improving tryptophan mannosylation in glycoprotein structures. 糖蛋白结构中色氨酸甘露糖基化的检测、建立和改进方法。

IF 4.5 3区生物学

Protein Science Pub Date : 2025-02-01 DOI: 10.1002/pro.70025

Lou Holland, Phuong Thao Pham, Haroldas Bagdonas, Jordan S Dialpuri, Lucy C Schofield, Jon Agirre

{"title":"Methods for detecting, building, and improving tryptophan mannosylation in glycoprotein structures.","authors":"Lou Holland, Phuong Thao Pham, Haroldas Bagdonas, Jordan S Dialpuri, Lucy C Schofield, Jon Agirre","doi":"10.1002/pro.70025","DOIUrl":"10.1002/pro.70025","url":null,"abstract":"Tryptophan mannosylation, the covalent addition of an α-ᴅ-mannose sugar to a tryptophan side chain, is a post-translational modification (PTM) that can affect protein stability, folding, and interactions. Compared to other forms of protein glycosylation, it is relatively uncommon but is affected by conformational anomalies and modeling errors similar to those seen in N- and O-glycans in the Protein Data Bank (PDB). In this work, we report methods for detecting, building, and improving mannose structures linked to tryptophans. These methods have been used to mine X-ray crystallographic and cryo-electron microscopy maps in the PDB looking for unmodeled mannosylation, resulting in a number of cases where the modification can be placed in the map with high confidence. Additionally, we address most conformational issues affecting this modification. Finally, the development of a structural template to recognize thrombospondin repeats (TSR) domains where tryptophan mannosylation occurs will allow for the mannosylation of candidate-predicted models, for example, those predicted with AlphaFold.","PeriodicalId":20761,"journal":{"name":"Protein Science","volume":"34 2","pages":"e70025"},"PeriodicalIF":4.5,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11751905/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143010472","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}

引用次数: 0

Accelerated amyloid fibril formation at the interface of liquid-liquid phase-separated droplets by depletion interactions.

IF 4.5 3区生物学

Protein Science Pub Date : 2025-02-01 DOI: 10.1002/pro.5163

Keiichi Yamaguchi, Joji Mima, Kichitaro Nakajima, Hiroki Sakuta, Kenichi Yoshikawa, Yuji Goto

{"title":"Accelerated amyloid fibril formation at the interface of liquid-liquid phase-separated droplets by depletion interactions.","authors":"Keiichi Yamaguchi, Joji Mima, Kichitaro Nakajima, Hiroki Sakuta, Kenichi Yoshikawa, Yuji Goto","doi":"10.1002/pro.5163","DOIUrl":"10.1002/pro.5163","url":null,"abstract":"Amyloid fibril formation of α-synuclein (αSN) is a hallmark of synucleinopathies. Although the previous studies have provided numerous insights into the molecular basis of αSN amyloid formation, it remains unclear how αSN self-assembles into amyloid fibrils in vivo. Here, we show that αSN amyloid formation is accelerated in the presence of two macromolecular crowders, polyethylene glycol (PEG) (MW: ~10,000) and dextran (DEX) (MW: ~500,000), with a maximum at approximately 7% (w/v) PEG and 7% (w/v) DEX. Under these conditions, the two crowders induce a two-phase separation of upper PEG and lower DEX phases with a small number of liquid droplets of DEX and PEG in PEG and DEX phases, respectively. Fluorescence microscope images revealed that the interfaces of DEX droplets in the upper PEG phase are the major sites of amyloid formation. We consider that the depletion interactions working in micro phase-segregated state with DEX and PEG systems causes αSN condensation at the interface between solute PEG and DEX droplets, resulting in accelerated amyloid formation. Ultrasonication further accelerated the amyloid formation in both DEX and PEG phases, confirming the droplet-dependent amyloid formation. Similar PEG/DEX-dependent accelerated amyloid formation was observed for amyloid β peptide. In contrast, amyloid formation of β2-microglobulin or hen egg white lysozyme with a native fold was suppressed in the PEG/DEX mixtures, suggesting that the depletion interactions work adversely depending on whether the protein is unfolded or folded.","PeriodicalId":20761,"journal":{"name":"Protein Science","volume":"34 2","pages":"e5163"},"PeriodicalIF":4.5,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11774873/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143060527","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}

引用次数: 0

Conformational dynamics in specialized C₂H₂ zinc finger domains enable zinc-responsive gene repression in S. pombe.

IF 4.5 3区生物学

Protein Science Pub Date : 2025-02-01 DOI: 10.1002/pro.70044

Vibhuti Wadhwa, Cameron Jamshidi, Kye Stachowski, Amanda J Bird, Mark P Foster

{"title":"Conformational dynamics in specialized C2H2 zinc finger domains enable zinc-responsive gene repression in S. pombe.","authors":"Vibhuti Wadhwa, Cameron Jamshidi, Kye Stachowski, Amanda J Bird, Mark P Foster","doi":"10.1002/pro.70044","DOIUrl":"10.1002/pro.70044","url":null,"abstract":"Loz1 is a zinc-responsive transcription factor in fission yeast that maintains cellular zinc homeostasis by repressing the expression of genes required for zinc uptake in high zinc conditions. Previous deletion analysis of Loz1 found a region containing two tandem C2H2 zinc-fingers and an upstream \"accessory domain\" rich in histidine, lysine, and arginine residues to be sufficient for zinc-dependent DNA binding and gene repression. Here we report unexpected biophysical properties of this pair of seemingly classical C2H2 zinc fingers. Isothermal titration calorimetry and NMR spectroscopy reveal two distinct zinc binding events localized to the zinc fingers. NMR spectra reveal complex dynamic behavior in this zinc-responsive region spanning time scales from fast 10-12-10-10 to slow >100 s. Slow exchange due to cis-trans isomerization of the TGERP linker results in the doubling of many signals in the protein. Conformational exchange on the 10-3 s timescale throughout the first zinc finger distinguishes it from the second and is linked to a weaker affinity for zinc. These findings reveal a mechanism of zinc sensing by Loz1 and illuminate how the protein's rough free-energy landscape enables zinc sensing, DNA binding and regulated gene expression.","PeriodicalId":20761,"journal":{"name":"Protein Science","volume":"34 2","pages":"e70044"},"PeriodicalIF":4.5,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11761706/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143047685","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}

引用次数: 0

Insights into the flexibility of the domain-linking loop in actinobacterial coproheme decarboxylase through structures and molecular dynamics simulations.

IF 4.5 3区生物学

Protein Science Pub Date : 2025-02-01 DOI: 10.1002/pro.70027

Gaurav Patil, Diego Javier Alonso de Armiño, Yirui Guo, Paul G Furtmüller, Dominika Borek, Dario A Estrin, Stefan Hofbauer

{"title":"Insights into the flexibility of the domain-linking loop in actinobacterial coproheme decarboxylase through structures and molecular dynamics simulations.","authors":"Gaurav Patil, Diego Javier Alonso de Armiño, Yirui Guo, Paul G Furtmüller, Dominika Borek, Dario A Estrin, Stefan Hofbauer","doi":"10.1002/pro.70027","DOIUrl":"10.1002/pro.70027","url":null,"abstract":"Prokaryotic heme biosynthesis in Gram-positive bacteria follows the coproporphyrin-dependent heme biosynthesis pathway. The last step in this pathway is catalyzed by the enzyme coproheme decarboxylase, which oxidatively transforms two propionate groups into vinyl groups yielding heme b. The catalytic reaction cycle of coproheme decarboxylases exhibits four different states: the apo-form, the substrate (coproheme)-bound form, a transient three-propionate intermediate form (monovinyl, monopropionate deuteroheme; MMD), and the product (heme b)-bound form. In this study, we used cryogenic electron microscopy single-particle reconstruction (cryo-EM SPR) to characterize structurally the apo and heme b-bound forms of actinobacterial coproheme decarboxylase from Corynebacterium diphtheriae. The flexible loop that connects the N-terminal and the C-terminal ferredoxin domains of coproheme decarboxylases plays an important role in interactions between the enzyme and porphyrin molecule. To understand the role of this flexible loop, we performed molecular dynamics simulations on the apo and heme b coproheme decarboxylase from Corynebacterium diphtheriae. Our results are discussed in the context of the published structural information on coproheme-bound and MMD-bound coproheme decarboxylase and with respect to the reaction mechanism. Having structural information of all four enzymatically relevant states helps in understanding structural restraints with a functional impact.","PeriodicalId":20761,"journal":{"name":"Protein Science","volume":"34 2","pages":"e70027"},"PeriodicalIF":4.5,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11761711/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143047691","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}

引用次数: 0

AggNet: Advancing protein aggregation analysis through deep learning and protein language model. AggNet：通过深度学习和蛋白质语言模型推进蛋白质聚集分析。

IF 4.5 3区生物学

Protein Science Pub Date : 2025-02-01 DOI: 10.1002/pro.70031

Wenjia He, Xiaopeng Xu, Haoyang Li, Juexiao Zhou, Xin Gao

{"title":"AggNet: Advancing protein aggregation analysis through deep learning and protein language model.","authors":"Wenjia He, Xiaopeng Xu, Haoyang Li, Juexiao Zhou, Xin Gao","doi":"10.1002/pro.70031","DOIUrl":"10.1002/pro.70031","url":null,"abstract":"Protein aggregation is critical to various biological and pathological processes. Besides, it is also an important property in biotherapeutic development. However, experimental methods to profile protein aggregation are costly and labor-intensive, driving the need for more efficient computational alternatives. In this study, we introduce \"AggNet,\" a novel deep learning framework based on the protein language model ESM2 and AlphaFold2, which utilizes physicochemical, evolutionary, and structural information to discriminate amyloid and non-amyloid peptides and identify aggregation-prone regions (APRs) in diverse proteins. Benchmark comparisons show that AggNet outperforms existing methods and achieves state-of-the-art performance on protein aggregation prediction. Also, the predictive ability of AggNet is stable across proteins with different secondary structures. Feature analysis and visualizations prove that the model effectively captures peptides' physicochemical properties effectively, thereby offering enhanced interpretability. Further validation through a case study on MEDI1912 confirms AggNet's practical utility in analyzing protein aggregation and guiding mutation for aggregation mitigation. This study enhances computational tools for predicting protein aggregation and highlights the potential of AggNet in protein engineering. Finally, to improve the accessibility of AggNet, the source code can be accessed at: https://github.com/Hill-Wenka/AggNet.","PeriodicalId":20761,"journal":{"name":"Protein Science","volume":"34 2","pages":"e70031"},"PeriodicalIF":4.5,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11751882/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143010356","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}

引用次数: 0

Loop engineering of enzymes to control their immobilization and ultimately fabricate more efficient heterogeneous biocatalysts. 酶的环工程，以控制其固定化和最终制造更有效的多相生物催化剂。

IF 4.5 3区生物学

Protein Science Pub Date : 2025-02-01 DOI: 10.1002/pro.70040

Nicoll Zeballos, Irene Ginés-Alcober, Javier Macías-León, Daniel Andrés-Sanz, Andrés Manuel González-Ramírez, Mercedes Sánchez-Costa, Pedro Merino, Ramón Hurtado-Guerrero, Fernando López-Gallego

{"title":"Loop engineering of enzymes to control their immobilization and ultimately fabricate more efficient heterogeneous biocatalysts.","authors":"Nicoll Zeballos, Irene Ginés-Alcober, Javier Macías-León, Daniel Andrés-Sanz, Andrés Manuel González-Ramírez, Mercedes Sánchez-Costa, Pedro Merino, Ramón Hurtado-Guerrero, Fernando López-Gallego","doi":"10.1002/pro.70040","DOIUrl":"10.1002/pro.70040","url":null,"abstract":"Enzyme immobilization is indispensable for enhancing enzyme performance in various industrial applications. Typically, enzymes require specific spatial arrangements for optimal functionality, underscoring the importance of correct orientation. Despite well-known N- or C-terminus tailoring techniques, alternatives for achieving orientation control are limited. Here, we propose a novel approach that tailors the enzyme surface with engineered His-rich loops. To that aim, we first solve the X-ray crystal structure of a hexameric alcohol dehydrogenase from Thermus thermophilus HB27 (TtHBDH) (PDB: 9FBD). Guided by this 3D structure, we engineer the enzyme surface with a new loop enriched with six His residues to control enzyme orientation. Molecular dynamics simulations reveal that the engineered loop's imidazole rings have greater solvent accessibility than those in native His residues, allowing for more efficient enzyme immobilization on certain metal chelate-functionalized carriers. Using carriers functionalized with iron (III)-catechol, the apparent Vmax of the immobilized loop variant doubles the immobilized His-tagged one, and vice versa when both variants are immobilized on carriers functionalized with copper (II)-imidodiacetic acid. His-tagged and loop-engineered TtHBDH show high operational stability reaching 100% bioconversion after 10 reaction cycles, yet the loop variant is faster than the His-tagged one.","PeriodicalId":20761,"journal":{"name":"Protein Science","volume":"34 2","pages":"e70040"},"PeriodicalIF":4.5,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11751856/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143010467","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}

引用次数: 0

Applicability of AlphaFold2 in the modeling of dimeric, trimeric, and tetrameric coiled-coil domains. AlphaFold2 在二聚体、三聚体和四聚体线圈结构域建模中的适用性。

IF 4.5 3区生物学

Protein Science Pub Date : 2025-01-01 DOI: 10.1002/pro.5244

Rafal Madaj, Mikel Martinez-Goikoetxea, Kamil Kaminski, Jan Ludwiczak, Stanislaw Dunin-Horkawicz

{"title":"Applicability of AlphaFold2 in the modeling of dimeric, trimeric, and tetrameric coiled-coil domains.","authors":"Rafal Madaj, Mikel Martinez-Goikoetxea, Kamil Kaminski, Jan Ludwiczak, Stanislaw Dunin-Horkawicz","doi":"10.1002/pro.5244","DOIUrl":"10.1002/pro.5244","url":null,"abstract":"Coiled coils are a common protein structural motif involved in cellular functions ranging from mediating protein-protein interactions to facilitating processes such as signal transduction or regulation of gene expression. They are formed by two or more alpha helices that wind around a central axis to form a buried hydrophobic core. Various forms of coiled-coil bundles have been reported, each characterized by the number, orientation, and degree of winding of the constituent helices. This variability is underpinned by short sequence repeats that form coiled coils and whose properties determine both their overall topology and the local geometry of the hydrophobic core. The strikingly repetitive sequence has enabled the development of accurate sequence-based coiled-coil prediction methods; however, the modeling of coiled-coil domains remains a challenging task. In this work, we evaluated the accuracy of AlphaFold2 in modeling coiled-coil domains, both in modeling local geometry and in predicting global topological properties. Furthermore, we show that the prediction of the oligomeric state of coiled-coil bundles can be achieved by using the internal representations of AlphaFold2, with a performance better than any previous state-of-the-art method (code available at https://github.com/labstructbioinf/dc2_oligo).","PeriodicalId":20761,"journal":{"name":"Protein Science","volume":"34 1","pages":"e5244"},"PeriodicalIF":4.5,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11651203/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142839011","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}

引用次数: 0

Allosteric regulation of the tyrosine phosphatase PTP1B by a protein-protein interaction. 蛋白-蛋白相互作用对酪氨酸磷酸酶PTP1B的变构调节。

IF 4.5 3区生物学

Protein Science Pub Date : 2025-01-01 DOI: 10.1002/pro.70016

Cassandra A Chartier, Virgil A Woods, Yunyao Xu, Anne E van Vlimmeren, Andrew C Johns, Marko Jovanovic, Ann E McDermott, Daniel A Keedy, Neel H Shah

{"title":"Allosteric regulation of the tyrosine phosphatase PTP1B by a protein-protein interaction.","authors":"Cassandra A Chartier, Virgil A Woods, Yunyao Xu, Anne E van Vlimmeren, Andrew C Johns, Marko Jovanovic, Ann E McDermott, Daniel A Keedy, Neel H Shah","doi":"10.1002/pro.70016","DOIUrl":"10.1002/pro.70016","url":null,"abstract":"The rapid identification of protein-protein interactions has been significantly enabled by mass spectrometry (MS) proteomics-based methods, including affinity purification-MS, crosslinking-MS, and proximity-labeling proteomics. While these methods can reveal networks of interacting proteins, they cannot reveal how specific protein-protein interactions alter protein function or cell signaling. For instance, when two proteins interact, there can be emergent signaling processes driven purely by the individual activities of those proteins being co-localized. Alternatively, protein-protein interactions can allosterically regulate function, enhancing or suppressing activity in response to binding. In this work, we investigate the interaction between the tyrosine phosphatase PTP1B and the adaptor protein Grb2, which have been annotated as binding partners in a number of proteomics studies. This interaction has been postulated to co-localize PTP1B with its substrate IRS-1 by forming a ternary complex, thereby enhancing the dephosphorylation of IRS-1 to suppress insulin signaling. Here, we report that Grb2 binding to PTP1B also allosterically enhances PTP1B catalytic activity. We show that this interaction is dependent on the proline-rich region of PTP1B, which interacts with the C-terminal SH3 domain of Grb2. Using NMR spectroscopy and hydrogen-deuterium exchange mass spectrometry (HDX-MS) we show that Grb2 binding alters PTP1B structure and/or dynamics. Finally, we use MS proteomics to identify other interactors of the PTP1B proline-rich region that may also regulate PTP1B function similarly to Grb2. This work presents one of the first examples of a protein allosterically regulating the enzymatic activity of PTP1B and lays the foundation for discovering new mechanisms of PTP1B regulation in cell signaling.","PeriodicalId":20761,"journal":{"name":"Protein Science","volume":"34 1","pages":"e70016"},"PeriodicalIF":4.5,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11670308/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142897217","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}

引用次数: 0

The structural influence of the oncogenic driver mutation N642H in the STAT5B SH2 domain. STAT5B SH2结构域中致癌驱动突变N642H的结构影响。

IF 4.5 3区生物学

Protein Science Pub Date : 2025-01-01 DOI: 10.1002/pro.70022

Liam Haas-Neill, Deniz Meneksedag-Erol, Ayesha Chaudhry, Masha Novoselova, Qirat F Ashraf, Elvin D de Araujo, Derek J Wilson, Sarah Rauscher

{"title":"The structural influence of the oncogenic driver mutation N642H in the STAT5B SH2 domain.","authors":"Liam Haas-Neill, Deniz Meneksedag-Erol, Ayesha Chaudhry, Masha Novoselova, Qirat F Ashraf, Elvin D de Araujo, Derek J Wilson, Sarah Rauscher","doi":"10.1002/pro.70022","DOIUrl":"10.1002/pro.70022","url":null,"abstract":"The point mutation N642H of the signal transducer and activator of transcription 5B (STAT5B) protein is associated with aggressive and drug-resistant forms of leukemia. This mutation is thought to promote cancer due to hyperactivation of STAT5B caused by increased stability of the active, parallel dimer state. However, the molecular mechanism leading to this stabilization is not well understood as there is currently no structure of the parallel dimer. To investigate the mutation's mechanism of action, we conducted extensive all-atom molecular dynamics simulations of multiple oligomeric forms of both STAT5B and STAT5BN642H, including a model for the parallel dimer. The N642H mutation directly affects the hydrogen bonding network within the phosphotyrosine (pY)-binding pocket of the parallel dimer, enhancing the pY-binding interaction. The simulations indicate that apo STAT5B is highly flexible, exploring a diverse conformational space. In contrast, apo STAT5BN642H accesses two distinct conformational states, one of which resembles the conformation of the parallel dimer. The simulation predictions of the effects of the mutation on structure and dynamics are supported by the results of hydrogen-deuterium exchange (HDX) mass spectrometry measurements carried out on STAT5B and STAT5BN642H in which a phosphopeptide was used to mimic the effects of parallel dimerization on the SH2 domain. The molecular-level information uncovered in this work contributes to our understanding of STAT5B hyperactivation by the N642H mutation and could help pave the way for novel therapeutic strategies targeting this mutation.","PeriodicalId":20761,"journal":{"name":"Protein Science","volume":"34 1","pages":"e70022"},"PeriodicalIF":4.5,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11670306/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142896822","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}

引用次数: 0

The role of amphipathic and cationic helical peptides in Parkinson's disease. 两亲性和阳离子螺旋肽在帕金森病中的作用。

IF 4.5 3区生物学

Protein Science Pub Date : 2025-01-01 DOI: 10.1002/pro.70020

Carlos Pintado-Grima, Salvador Ventura

引用次数: 0