Journal of Inorganic Biochemistry最新文献_第2页

Regulation of ferryl reactivity by the cytochrome P450 decarboxylase OleT 细胞色素P450脱羧酶OleT对铁基反应性的调控

IF 3.8 2区化学

Journal of Inorganic Biochemistry Pub Date : 2025-04-04 DOI: 10.1016/j.jinorgbio.2025.112912

Hannah E. Gering , Olivia M. Manley , Alexis J. Holwerda , Job L. Grant , Steven C. Ratigan , Thomas M. Makris

{"title":"Regulation of ferryl reactivity by the cytochrome P450 decarboxylase OleT","authors":"Hannah E. Gering , Olivia M. Manley , Alexis J. Holwerda , Job L. Grant , Steven C. Ratigan , Thomas M. Makris","doi":"10.1016/j.jinorgbio.2025.112912","DOIUrl":"10.1016/j.jinorgbio.2025.112912","url":null,"abstract":"<div><div>The cytochrome P450 OleT catalyzes the decarboxylation of long-chain fatty acid substrates to produce terminal alkenes using hydrogen peroxide as a co-substrate. The facile activation of peroxide to form Compound I in the first step of the reaction, and subsequent C<img>C bond cleavage mediated by Compound II, provides a unique opportunity to visualize both ferryl intermediates using transient kinetic approaches. Analysis of the Arrhenius behavior yields activation barriers of ∼6 kcal/mol and ∼ 18 kcal/mol for the decay of Compound I and Compound II respectively. The influence of the secondary coordination sphere, probed through site-directed mutagenesis approaches, suggests that restriction of the donor-acceptor distance contributes to the reactivity of Compound I. The reactivity of Compound II was further probed using kinetic solvent isotope effect approaches, confirming that the large barrier owes to a proton-gated mechanism in the decarboxylation reaction coordinate. Hydrogen-bonding to an active-site histidine (H85) in the distal pocket plays a key role in this process.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"270 ","pages":"Article 112912"},"PeriodicalIF":3.8,"publicationDate":"2025-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143824267","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

A highly positively charged Ru(II) complex with photo-labile ligands for selective and efficient photo-inactivation of intracellular Staphylococcus aureus 带有光敏配体的高正电荷 Ru(II) 复合物可选择性地高效光灭活细胞内的金黄色葡萄球菌

IF 3.8 2区化学

Journal of Inorganic Biochemistry Pub Date : 2025-04-04 DOI: 10.1016/j.jinorgbio.2025.112908

Yunli Xu , Xuwen Da , Yao Jian , Wanpeng Zhou , Aifeng Wu , Yao Wu , Yatong Peng , Xiulian Liu , Yu Shi , Xuesong Wang , Qianxiong Zhou

{"title":"A highly positively charged Ru(II) complex with photo-labile ligands for selective and efficient photo-inactivation of intracellular Staphylococcus aureus","authors":"Yunli Xu , Xuwen Da , Yao Jian , Wanpeng Zhou , Aifeng Wu , Yao Wu , Yatong Peng , Xiulian Liu , Yu Shi , Xuesong Wang , Qianxiong Zhou","doi":"10.1016/j.jinorgbio.2025.112908","DOIUrl":"10.1016/j.jinorgbio.2025.112908","url":null,"abstract":"<div><div>Due to the protection afforded by host cells, intracellular <em>Staphylococcus aureus</em> (<em>S. aureus</em>), particularly methicillin-resistant <em>S. aureus</em> (MRSA), poses a significantly greater challenge to eliminate compared to the extracellular counterparts. It is highly desirable to develop novel antibacterial agents which are capable of selectively and efficiently eradicating intracellular bacteria, including drug-resistant strains, while being less prone to induce bacterial resistance. In this work, two Ru(II) complexes (Ru1 and Ru2) with photo-labile ligands were designed and synthesized. Both Ru1 and Ru2 could covalently bind to DNA after photo-induced ligand dissociation. Compared to Ru1, the incorporation of a triphenylamine group adorned with two positively charged cationic pyridine units significantly boosts the DNA binding constant, bacterial binding/uptake level, and subsequently, the antibacterial activity of Ru2. Ru2 could selectively photo-inactivate intracellular <em>S. aureus</em> and MRSA, being more efficient than vancomycin both <em>in vitro</em> and <em>in vivo</em>. Interestingly, after 20 days' treatment at sublethal concentrations, <em>S. aureus</em> cells exhibited no obvious drug resistance towards Ru2 upon irradiation. Such appealing results may provide new sights for developing novel antibacterial agents against intractable intracellular pathogens and also prevalent drug resistance.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"268 ","pages":"Article 112908"},"PeriodicalIF":3.8,"publicationDate":"2025-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143800406","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Intrinsically photoluminescent hydrogels to measure peptides‑copper binding affinities 内在光致发光水凝胶测量肽-铜结合亲和力

IF 3.8 2区化学

Journal of Inorganic Biochemistry Pub Date : 2025-04-04 DOI: 10.1016/j.jinorgbio.2025.112914

Alessia Distefano , Paolo Corsaro , Nunzio Tuccitto , Francesca Laneri , Olivier Monasson , Elisa Peroni , Giuseppe Grasso

{"title":"Intrinsically photoluminescent hydrogels to measure peptides‑copper binding affinities","authors":"Alessia Distefano , Paolo Corsaro , Nunzio Tuccitto , Francesca Laneri , Olivier Monasson , Elisa Peroni , Giuseppe Grasso","doi":"10.1016/j.jinorgbio.2025.112914","DOIUrl":"10.1016/j.jinorgbio.2025.112914","url":null,"abstract":"<div><div>NH<sub>2</sub> decorated intrinsically photoluminescent hydrogels (IPH-NH<sub>2</sub>) were functionalized with the addition of various peptides via EDC/NHS coupling method. These peptidic devices bind copper with binding affinities depending on surface functionalization. Particularly, fluorescence analysis of copper titrations, alongside the determination of quenching efficiency and lifetime measurements, allowed to assess binding constants and to elucidate the underlying binding mechanism. Various peptides, having the same copper binding amino acidic residues (GHK) but different chain lengths, were tested and it was found that increasing the distance of the GHK sequence from the IPH-NH<sub>2</sub> surface resulted in a decrease in the binding constant, as well as a reduction in quenching efficiency, whereas the binding mechanism remained unchanged as indicated by lifetime measurements. This method not only provides binding constants for peptides immobilized on biosensor surfaces or pre-fabricated devices without altering their structure, but also contributes to the optimization of biosensor design, tailoring it to its intended application.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"268 ","pages":"Article 112914"},"PeriodicalIF":3.8,"publicationDate":"2025-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143791270","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Recent advances in Schiff bases and Cu(II) complexes: Applications in fluorescence imaging and anticancer therapy (2020–2024) 希夫碱和Cu（II）配合物在荧光成像和抗癌治疗中的应用（2020-2024）

IF 3.8 2区化学

Journal of Inorganic Biochemistry Pub Date : 2025-04-03 DOI: 10.1016/j.jinorgbio.2025.112909

Alaa Shafie , Amal Adnan Ashour

{"title":"Recent advances in Schiff bases and Cu(II) complexes: Applications in fluorescence imaging and anticancer therapy (2020–2024)","authors":"Alaa Shafie , Amal Adnan Ashour","doi":"10.1016/j.jinorgbio.2025.112909","DOIUrl":"10.1016/j.jinorgbio.2025.112909","url":null,"abstract":"<div><div>Schiff base derivatives have garnered significant attention for their bioimaging and anticancer potentials. In the realm of bioimaging, Schiff base derivatives have shown exceptional capabilities in detecting various metal ions, due to their strong binding affinities and fluorescence properties. Moreover, the potential Schiff bases and their Cu(II) complexes as anticancer agents is being actively explored, with studies demonstrating their ability to induce apoptosis and inhibit cell proliferation in various cancer cell lines. This review article provides a comprehensive overview of recent advancements in the field of cell imaging utilizing Schiff base derivatives for the recognition of Cu<sup>2+</sup> in living cells and organisms. From 2022 to 2024, significant progress has been made in understanding the applications of Schiff bases in cell imaging techniques, ranging from fluorescence microscopy to molecular imaging modalities. Additionally, article has focused on leveraging the unique properties of Schiff base Cu(II) complexes to expand the anticancer efficacy. The article offering insights into the mechanisms underlying enhanced anticancer activity and the development of novel anticancer agents.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"268 ","pages":"Article 112909"},"PeriodicalIF":3.8,"publicationDate":"2025-04-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143785777","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Repaglinide platinum(IV) conjugates: Enhancing p53 signaling for antitumor and antimetastatic efficacy 瑞格列奈铂（IV）偶联物：增强p53信号传导抗肿瘤和抗转移疗效

IF 3.8 2区化学

Journal of Inorganic Biochemistry Pub Date : 2025-04-03 DOI: 10.1016/j.jinorgbio.2025.112910

Suying Li , Zhifang Liu , Yan Chen , Shuaiqi Feng , Hengye Chen , Yanna Zhao , Yanqin He , Qingpeng Wang

{"title":"Repaglinide platinum(IV) conjugates: Enhancing p53 signaling for antitumor and antimetastatic efficacy","authors":"Suying Li , Zhifang Liu , Yan Chen , Shuaiqi Feng , Hengye Chen , Yanna Zhao , Yanqin He , Qingpeng Wang","doi":"10.1016/j.jinorgbio.2025.112910","DOIUrl":"10.1016/j.jinorgbio.2025.112910","url":null,"abstract":"<div><div>The tumor suppressor p53 plays multiple roles at the crossroads of suppressing tumor development and metastasis. Here, a series of Repaglinide platinum(IV) conjugates promoting the p53 pathway were designed and prepared, which displayed potent antiproliferative and antimetastatic activities both <em>in vitro</em> and <em>in vivo</em>. Mechanistically, the expression of p53 was upregulated by the synergistic functions of the platinum core through causing severe DNA damage, and the RPG ligand <em>via</em> stimulating the lumican/p53/p21 pathway. The mitochondria-mediated apoptosis was initiated, involving the Bcl-2/Bax/caspase pathway. Pro-death autophagy was initiated with the upregulation of LC3II and down regulation of p62. Additionally, angiogenesis was suppressed by reversing tumor inflammation through the inhibition of key enzymes COX-2, MMP9, and VEGFA. Furthermore, antitumor immunity was enhanced by blocking the immune checkpoint PD-L1, which led to an increased presence of CD3<sup>+</sup> and CD8<sup>+</sup> T-cells within the tumor microenvironment.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"268 ","pages":"Article 112910"},"PeriodicalIF":3.8,"publicationDate":"2025-04-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143791269","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Unraveling the unfolding mechanism of pseudoazurin: Insights into stabilizing cupredoxin fold as a common domain of Cu-containing proteins 揭示伪azurin的展开机制：铜氧还蛋白折叠作为含铜蛋白的共同结构域的稳定见解

IF 3.8 2区化学

Journal of Inorganic Biochemistry Pub Date : 2025-04-02 DOI: 10.1016/j.jinorgbio.2025.112907

Takahide Yamaguchi , Attila Taborosi , Kiyokazu Tsugane , Kathleen Wood , Andrew E. Whitten , Seiji Mori , Takamitsu Kohzuma

{"title":"Unraveling the unfolding mechanism of pseudoazurin: Insights into stabilizing cupredoxin fold as a common domain of Cu-containing proteins","authors":"Takahide Yamaguchi , Attila Taborosi , Kiyokazu Tsugane , Kathleen Wood , Andrew E. Whitten , Seiji Mori , Takamitsu Kohzuma","doi":"10.1016/j.jinorgbio.2025.112907","DOIUrl":"10.1016/j.jinorgbio.2025.112907","url":null,"abstract":"<div><div>Understanding protein unfolding mechanisms is crucial for comprehending protein-folding related diseases, developing diagnostic methods, and designing proteins with desired stability for medicinal or industrial applications. However, investigating structures at atomic resolution is often difficult due to the flexibility and transiency of unfolding intermediate states. Pseudoazurin (PAz) is a well-characterized simple cupredoxin composed of a small polypeptide (124 amino acids) and a single metal cofactor (Cu<sup>2+</sup>), making it suitable to study the unfolding mechanism. In this study, combining the merits of structure determination by small-angle neutron scattering (SANS) and molecular dynamics (MD) simulations enabled us to access the details of the unfolding mechanism. The unfolding of PAz proceeds through a two-step mechanism involving the “native”, “open-domain”, and “random-coil” states. Several amino acid residues at the vicinity of Cu<sup>2+</sup> ion are involved in the structural transitions, where the interactions among these residues are important in controlling the stability of PAz. These findings may be applicable to stabilizing metalloproteins with cupredoxin domain structures.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"268 ","pages":"Article 112907"},"PeriodicalIF":3.8,"publicationDate":"2025-04-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143791271","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Rationalizing the structural basis of organic-platinum hybrid complexes binding towards quadruplex-duplex hybrids through all-atom simulations 通过全原子模拟，理顺了有机-铂杂化配合物向四双杂化结合的结构基础

IF 3.8 2区化学

Journal of Inorganic Biochemistry Pub Date : 2025-04-01 DOI: 10.1016/j.jinorgbio.2025.112904

Salvatore Muscarella, Irene Treccarichi, Luisa D'Anna, Angelo Spinello

{"title":"Rationalizing the structural basis of organic-platinum hybrid complexes binding towards quadruplex-duplex hybrids through all-atom simulations","authors":"Salvatore Muscarella, Irene Treccarichi, Luisa D'Anna, Angelo Spinello","doi":"10.1016/j.jinorgbio.2025.112904","DOIUrl":"10.1016/j.jinorgbio.2025.112904","url":null,"abstract":"<div><div>Guanine-rich sequences containing complementary base pairs can fold into non-canonical quadruplex-duplex hybrid (QDH) conformations. These structures possess unique structural features, leading to the presence of a peculiar binding pocket that can be distinguished from a canonical double helix or a G-quadruplex (G4) structure. Recently, two organic-metal hybrid platinum complexes, able to selectively and strongly recognize a particular type of QDH with a lateral duplex stem-loop, were reported in the literature. However, solution structures are not available for all the investigated compounds, leaving unanswered questions on the structural traits underlying the different binding affinity of these complexes. In this work, we address this gap using all-atom simulations to unravel the key features driving the high selectivity of these organic‑platinum hybrid complexes at an atomistic level. In particular, their binding affinity depends on a delicate balance between the extended π-π stacking interactions performed in the G4-duplex binding pocket and the capacity to form stable hydrogen bonds with the surrounding nucleobases. Thus, our findings provide essential insights to guide the rational design of novel compounds that selectively target QDH structures.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"268 ","pages":"Article 112904"},"PeriodicalIF":3.8,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143785778","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Bioinspired copper(II) complexes catalyzed oxidative coupling of aminophenols with broader substrate scope 生物激发铜（II）配合物催化氨基酚的氧化偶联具有更广泛的底物范围

IF 3.8 2区化学

Journal of Inorganic Biochemistry Pub Date : 2025-03-28 DOI: 10.1016/j.jinorgbio.2025.112906

Thasnim P Mohammed , Marappan Velusamy , Muniyandi Sankaralingam

{"title":"Bioinspired copper(II) complexes catalyzed oxidative coupling of aminophenols with broader substrate scope","authors":"Thasnim P Mohammed , Marappan Velusamy , Muniyandi Sankaralingam","doi":"10.1016/j.jinorgbio.2025.112906","DOIUrl":"10.1016/j.jinorgbio.2025.112906","url":null,"abstract":"<div><div>The strategic selection of ligand systems in metal complexes has demonstrated a profound impact on the efficiency and specificity of biomimetic reactions. In this work, we introduce a series of aminoquinoline-based copper(II) complexes (<strong>1</strong>–<strong>4</strong>) distinguished by systematic variation in terminal amine substituents: di-<em>n</em>-methyl (<strong>L1</strong>(H)), di-<em>n</em>-ethyl (<strong>L2</strong>(H)), di-<em>n</em>-propyl (<strong>L3</strong>(H)), and di-<em>n</em>-butyl (<strong>L4</strong>(H)). These complexes are synthesized, characterized, and evaluated as the catalyst for the oxidative coupling of different aminophenol derivatives. Remarkably, complex <strong>1</strong>, featuring a methyl substituent, exhibited unparalleled catalytic performance, achieving an 86 % (<em>K</em><sub>cat</sub> - 9.7 × 10<sup>4</sup> h<sup>−1</sup>) conversion of <em>o</em>-aminophenol to the desired product, 2-amino-phenoxazin-3-one, alongside water and hydrogen peroxide as byproducts. Notably, complex <strong>1</strong> demonstrated exceptional versatility, extending its catalytic activity to other substrates with remarkable activity. Mechanistic investigations, supported by mass-spectrometric analysis, revealed the formation of a complex-substrate adduct with all substrates, enabling us to propose a detailed reaction pathway. The work highlights the benefits of ligand design in improving catalytic performance and sets a new standard for aminoquinoline-based copper(II) complexes in oxidative coupling reactions. To the best of our knowledge, this work is the first to report a wider substrate scope for PHS activity with copper(II) complexes.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"270 ","pages":"Article 112906"},"PeriodicalIF":3.8,"publicationDate":"2025-03-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143829668","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Ascorbic acid potentiates the formation of IgG-enriched protein aggregates in plasma in a Cu(II)-mediated manner 抗坏血酸以Cu（II）介导的方式增强血浆中igg富集蛋白聚集体的形成

IF 3.8 2区化学

Journal of Inorganic Biochemistry Pub Date : 2025-03-24 DOI: 10.1016/j.jinorgbio.2025.112905

Christian Saporito-Magriña , Lila Lopez-Montañana , María Laura Facio , Guadalupe Pagano , Topp Nicole , Ariana Danzi , Juan Ignacio Bellida , Agustín Silva , Matías Albizzati , Marisa Gabriela Repetto

{"title":"Ascorbic acid potentiates the formation of IgG-enriched protein aggregates in plasma in a Cu(II)-mediated manner","authors":"Christian Saporito-Magriña , Lila Lopez-Montañana , María Laura Facio , Guadalupe Pagano , Topp Nicole , Ariana Danzi , Juan Ignacio Bellida , Agustín Silva , Matías Albizzati , Marisa Gabriela Repetto","doi":"10.1016/j.jinorgbio.2025.112905","DOIUrl":"10.1016/j.jinorgbio.2025.112905","url":null,"abstract":"<div><div>Protein aggregates have been reported in disease but also in physiological contexts in tissues as well as circulating protein aggregates in the bloodstream. Free Cu(II) induces the aggregation of serum proteins and this metal yields highly oxidant species upon reaction with hydrogen peroxide and also reacts with ascorbic acid (AA). A broad population is exposed to high doses of AA as second line therapy for different pathologies or as nutritional supplementation. This study addresses the effect of AA on the formation of plasma protein aggregates, observed by optic density, protein quantification and electrophoresis (SDS-PAGE) that, contrary to hampering the Cu(II)-induced plasma protein aggregation, AA potentiates their formation. Free Cu(II) induces the formation of IgG-enriched plasma protein aggregates but the combination with AA potentiates the incorporation of gamma-globulin (IgG) whereas other proteins such as albumin become depleted. The potentiating effect of Cu(II) and AA was corroborated employing isolated IgG. This effect of AA on Cu(II)-induced protein aggregation is not reproduced with isolated albumin. Additionally, AA does not potentiate Fe(III)-mediated aggregation of IgG, albumin or human plasma. Finally, it was shown that in healthy subjects which were administered high doses of intravenous AA, the aggregates can be obtained from the centrifuged plasma after 30 min of the administration of the antioxidant. Aggregated IgG have been shown to activate Fc receptors, involved in oxidative burst and inflammatory processes observed in neutrophils. Thus, the effect of AA on the immune system could be linked to the accumulation of protein aggregates enriched in specific proteins.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"269 ","pages":"Article 112905"},"PeriodicalIF":3.8,"publicationDate":"2025-03-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143705198","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Coiled coils as ligands for inclusion in the inorganic chemist's toolbox – For advances in MRI contrast agent design 卷绕线圈作为无机化学家工具箱中内含物的配体。磁共振成像造影剂设计的进展。

IF 3.8 2区化学

Journal of Inorganic Biochemistry Pub Date : 2025-03-23 DOI: 10.1016/j.jinorgbio.2025.112903

Anna F.A. Peacock

引用次数: 0