Publications by authors named "Xiaoting Qiu"

The nonribosomal peptide synthetase (NRPS) is a highly precise molecular assembly machinery for synthesizing structurally diverse peptides, which have broad medicinal applications. Withinthe NRPS, the condensation (C) domain is a core catalytic domain responsible for the formation of amide bonds between individual monomer residues during peptide elongation. This review summarizes various aspects of the C domain, including its structural characteristics, catalytic mechanisms, substrate specificity, substrate gating function, and auxiliary functions.

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Article Synopsis
  • The study explored how Xinfeng capsule (XFC) affects the salivary gland's structure and function in a mouse model of primary Sjögren's syndrome (pSS).
  • During the experiment, researchers collected and analyzed salivary gland tissues to measure specific gene expressions before and after XFC treatment, focusing on genes like EGR1 and M3R.
  • Results showed that XFC significantly improved saliva production and reduced inflammation in the salivary glands, with EGR1 identified as a potential biomarker for future pSS treatments.
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Nonribosomal peptides (NRPs) are biosynthesized by nonribosomal peptide synthetases (NRPSs) and are widely distributed in both terrestrial and marine organisms. Many NRPs and their analogs are biologically active and serve as therapeutic agents. The adenylation (A) domain is a key catalytic domain that primarily controls the sequence of a product during the assembling of NRPs and thus plays a predominant role in the structural diversity of NRPs.

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Oleogels, characterized by their semisolid matrix formed from liquid oil structured by gelators, are emerging as a pivotal innovation in food formulation, primarily due to their capacity to enhance the nutritional profile of products by incorporating healthier fats. This review explored the integration of oleogels into diverse food matrices, examining their impact on texture, mouthfeel, and overall sensory characteristics. Through an extensive analysis of current research, this paper illustrates the versatility of oleogels created with a variety of structuring agents across different food applications.

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Purpose: The aim of the work was to analyze the metabolites of the intestinal microbiota from the patients with mild cognitive impairment (MCI) and progressive MCI due to Alzheimer's disease (AD).

Method: Two cohorts were established. The first one included 87 subjects with 30 healthy controls (NC), 22 patients with MCI due to AD, and 35 patients with AD.

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Neurodegenerative disorders represent a significant and growing global health challenge, necessitating continuous advancements in diagnostic tools for accurate and early detection. This work explores the recent progress in Magnetic Resonance Imaging (MRI) techniques and their application in the realm of neurodegenerative disorders. The introductory section provides a comprehensive overview of the study's background, significance, and objectives.

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Objective: Primary Sjögren's syndrome (pSS) is a intricate autoimmune disease mainly characterized of immune-mediated destruction of exocrine tissues, such as salivary and lacrimal glands, occurring dry mouth and eyes. Although some breakthroughs in understanding pSS have been uncovered, many questions remain about its pathogenesis, especially the internal relations between exocrine glands and secretions.

Method: Transcriptomic and proteomic analyses were conducted on salivary tissues and saliva in experimental Sjögren syndrome (ESS).

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tRNA methylations, including base modification and 2'--methylation of ribose moiety, play critical roles in the structural stabilization of tRNAs and the fidelity and efficiency of protein translation. These modifications are catalyzed by tRNA methyltransferases (TRMs). Some of the TRMs from yeast can fully function only by a single subunit.

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Aeruginosins, a family of nonribosomal linear tetrapeptides discovered from cyanobacteria and sponges, exhibit in vitro inhibitory activity on various types of serine proteases. This family is characterized by the existence of the 2-carboxy-6-hydroxy-octahydroindole (Choi) moiety occupied at the central position of the tetrapeptide. Aeruginosins have attracted much attention due to their special structures and unique bioactivities.

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  • Ferritin is a protein with a unique cage-like structure that stores iron and can also interact with other heavy metals, but research on these interactions is limited.
  • In a study on a marine invertebrate ferritin (DzFer), it was found to withstand extreme pH levels while binding to silver (Ag) and copper (Cu) ions.
  • Ag showed a preference for binding at specific sites, potentially interfering more with ferritin's iron storage function compared to Cu, offering new insights into heavy metal interactions within ferritin.
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Introduction: Mouse models are the basis for primary Sjögren's syndrome (pSS) research. However, the depth of comparisons between mice and humans in salivary gland (SG) immune cells remains limited.

Methods: The gene expression profiles of SGs from normal subjects and pSS patients were downloaded from the Gene Expression Comprehensive Database.

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  • - Ferritin, an essential iron storage protein, is studied in the context of the echinoderm Selenka, which has notable regenerative abilities, but its iron oxidation mechanism is not fully understood.
  • - Researchers created various mutant forms of ferritin (AjFER) and analyzed their structures and functions, revealing how mutations affected the protein's overall shape and iron processing capabilities.
  • - The study showed that changes in specific metal-binding sites in the ferritin mutants led to decreased iron oxidation rates and lower stability, indicating these sites are crucial for the protein's catalytic function and providing insights into ferritins in marine invertebrates.
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In addition to its role as an iron storage protein, ferritin can function as a major detoxification component in the innate immune defense, and Cu ions can also play crucial antibacterial roles in the blood clam, . However, the mechanism of interaction between iron and copper in recombinant ferritin (TgFer) remains to be investigated. In this study, we investigated the crystal structure of TgFer and examined the effects of Fe and Cu ions on the TgFer structure and catalytic activity.

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Ferritin is considered to be an ubiquitous and conserved iron-binding protein that plays a crucial role in iron storage, detoxification, and immune response. Although ferritin is of critical importance for almost all kingdoms of life, there is a lack of knowledge about its role in the marine invertebrate sea cucumber (Apostichopus japonicus). In this study, we characterized the first crystal structure of A.

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Head and neck squamous cell carcinoma (HNSCC) is the sixth most common cancer malignancy worldwide and is known to have poor prognosis. The pathogenesis behind the development of HNSCC is not fully understood. Modifications on RNA are involved in many pathophysiological processes, such as tumor development and inflammation.

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DNA 5-methylcytosine modification plays an important role in the regulation of a variety of biological functions in both prokaryotic and eukaryotic organisms. Previous studies show that DNA Cytosine-5-methylation is predominantly associated with restriction-modification system in bacteria. IPF4390 is deduced to be a putative type II DNA Cytosine-5 methyltransferase from a fresh water cyanobacterium, Microcystis aeruginosa.

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Article Synopsis
  • Marine invertebrates lack an adaptive immune system, and ferritin serves as a key intracellular iron-storage protein that aids innate immunity.
  • The study reveals the crystal structures of two new ferritins, Fer147 and PeFer, from the marine invertebrate P. esculenta, showcasing their unique 24-subunit cage-like structures.
  • Differences in the electrostatic potential of their channels indicate variations in metal ion movement and aggregation, providing a foundation for further research on iron-storage mechanisms in marine invertebrate ferritins.
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Ferritin is an important hub of iron metabolism because it stores iron during times of iron overload and releases iron during iron deficiency. Here, we present the first crystal structure of ferritin from the marine invertebrate Dendrorhynchus zhejiangensis with a 2.3 Å resolution.

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The 2-carboxy-6-hydroxyoctahydroindole (Choi) moiety is an essential residue for the antithrombotic activities of aeruginosins, which are a class of cyanobacterial derived bioactive linear tetrapeptides. Biosynthetic pathway of Choi is still elusive. AerF was suggested to be involved in the biosynthesis of Choi, and can be assigned to the short-chain dehydrogenase/reductase (SDR) superfamily.

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Modern organic chemistry faces many difficulties in the reliable production of cyclopeptides, such as poor yields and insufficient regio- and stereoselectivity. Thioesterase (TE) shows impressive stereospecificity, region- and chemoselectivity during the cyclization of peptide substrates. The biocatalytic properties of TE provide high value for industrial applications.

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The 2-carboxy-6-hydroxyoctahydroindole (Choi) moiety is a hallmark of aeruginosins, a class of cyanobacterial derived bioactive linear tetrapeptides that possess antithrombotic activity. The biosynthetic pathway of Choi has yet to be resolved. AerE is a cupin superfamily enzyme that was shown to be involved in the biosynthesis of Choi, but its exact role remains unclear.

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Carboxyl-terminal repeat domain (CTD) of the largest subunit Rpb1 of RNA polymerace II is essential for transcription regulation. Heptapeptide repeat of CTD of Rpb1 is phosphorylated by carboxyl-terminal repeat domain kinase (CTDK-I), composed of CTK1, CTK2 and CTK3, in order to regulate transcription and transcription associated processes. The yeast specific protein CTK3 binds to cyclin CTK2 to form a heterodimer serving as a regulational factor to control CTK1 activity by binding to CTK1.

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Reaction of [Et4N][Tp*WS3] (1) with [Cu(MeCN)4]PF6, CsCl, isonicotinic acid and CuCN, and treatment of [Et4N][Tp*WS3(CuCl)3] (2)/[Et4N][{Tp*WS3Cu3Cl}2(μ-Cl)2(μ4-Cl)] (3) with AgOTf and bpp (Tp* = hydridotris(3,5-dimethylpyrazol-1-yl)borate; bpp = 1,3-di(4-pyridyl)propane) give rise to [Et4N]2[{Tp*WS3Cu3(CN)0.5}2(μ-Cl)2(μ4-Cl)]2(PF6)2 (4) and [(Tp*WS3Cu3)2(μ3-Cl)2(bpp)3]2(OTf)4 (5), respectively. Compounds 4 and 5 feature cluster-based rectangle and [2]catenane architecture, and both exhibit enhanced third-order nonlinear optical responses relative to those of 1.

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Six analogous two-dimensional (2D) [Tp*WSCu]-based (Tp* = hydridotris(3,5-dimethylpyrazol-1-yl)borate) networks, namely, {[(Tp*WSCu)L](μ-N)} (2: L = 5-methyltetrazolate (Mtta); 3a: L = 5-ethyltetrazolate (Etta)) and {[(Tp*WSCu)L]BF} (3b: L = Etta; 4: L = 5-propyltetrazolate (Ptta); 5: L = 5-butyltetrazolate (Btta); 6: L = 5-pentyltetrazolate (Petta)) were synthesized by reactions of [EtN][Tp*WS] (1), [Cu(CHCN)]BF, NaN, and NHBF in different nitrile solvents (CH(CH)CN, n = 0, 1, 2, 3, and 4) under solvothermal conditions. In the structures of 2-6, each alkyl tetrazolate L as a bridging ligand was generated in situ from the "click" reaction between azide and nitrile. These 2D (6,3) networks support two types of voids wherein the pendant alkyl groups are accommodated.

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Article Synopsis
  • * This study reveals the crystal structure of the C2A domain from synaptotagmin 5, which successfully binds Ca, allowing researchers to understand its calcium-binding mechanism at a high resolution of 1.90Å.
  • * A specific serine residue in the Ca-binding loop influences the shape of the calcium-binding pocket, affecting how synaptotagmins respond to calcium, which is crucial for their roles in triggering vesicle fusion during various cellular processes.
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