Ouyang J

References (4)

Title : Integrating Enzymes with Supramolecular Polymers for Recyclable Photobiocatalytic Catalysis - Ouyang_2024_Angew.Chem.Int.Ed.Engl__e202400105
Author(s) : Ouyang J , Zhang Z , Li J , Wu C
Ref : Angew Chem Int Ed Engl , :e202400105 , 2024
Abstract : Chemical modifications of enzymes excel in the realm of enzyme engineering due to its directness, robustness, and efficiency; however, challenges persist in devising versatile and effective strategies. In this study, we introduce a supramolecular modification methodology that amalgamates a supramolecular polymer with Candida antarctica lipase B (CalB) to create supramolecular enzymes (SupEnzyme). This approach features the straightforward preparation of a supramolecular amphiphilic polymer (beta-CD@SMA), which was subsequently conjugated to the enzyme, resulting in a SupEnzyme capable of self-assembly into supramolecular nanoparticles. The resulting SupEnzyme nanoparticles can form micron-scale supramolecular aggregates via supramolecular and electrostatic interactions with guest entities, thus enhancing catalyst recycling. Remarkably, these aggregates maintain 80% activity after seven cycles, outperforming Novozym 435. Additionally, they can effectively initiate photobiocatalytic cascade reactions using guest photocatalysts. As a consequence, our SupEnzyme methodology exhibits noteworthy adaptability in enzyme modification, presenting a versatile platform for various polymer, enzyme, and biocompatible catalyst pairings, with potential applications in the fields of chemistry and biology.
ESTHER : Ouyang_2024_Angew.Chem.Int.Ed.Engl__e202400105
PubMedSearch : Ouyang_2024_Angew.Chem.Int.Ed.Engl__e202400105
PubMedID: 38386281

Title : An Individualized Nomogram for Predicting Mortality Risk of Septic Shock Patients During Hospitalization: A ten Years Retrospective Analysis - Wang_2023_Infect.Drug.Resist_16_6247
Author(s) : Wang M , Shi Y , Pan X , Wang B , Lu B , Ouyang J
Ref : Infect Drug Resist , 16 :6247 , 2023
Abstract : PURPOSE: We intend to develop a nomogram for predicting the mortality risk of hospitalized septic shock patients. PATIENTS AND METHODS: Data were collected from patients hospitalized with septic shock in Affiliated Dongyang Hospital of Wenzhou Medical University in China, over 10 years between January 2013 and January 2023. The eligible study participants were divided into modeling and validation groups. Factors independently related to the mortality in the modeling group were obtained by stepwise regression analysis. A logistic regression model and a nomogram were built. The model was evaluated based on the discrimination power (the area under the curve of the receiver operating characteristic, AUC), the calibration degree and decision curve analysis. In the validation group, the discrimination powers of the logistic regression model, the sequential organ failure assessment (SOFA) scoring model and machine learning model were compared. RESULTS: A total of 1253 patients, including 878 patients in the modeling group and 375 patients in the validation group, were included in this study. Age, respiratory failure, serum cholinesterase, lactic acid, blood phosphorus, blood magnesium, total bilirubin, and pH were independent risk factors related to the mortality risk of septic shock. The AUCs of the prediction model for the modeling and validation groups were 0.881 and 0.868, respectively. The models had a good calibration degree and clinical applicability. The AUC of the SOFA model for the validation population was 0.799, significantly lower than that of our model. The AUCs of the random forest and ensemble models were 0.865 and 0.863, respectively, comparable to that of our logistical prediction model. CONCLUSION: The model established in this study can effectively predict the mortality risk in patients hospitalized with septic shock. Thus, the model could be used clinically to determine the best therapy or management for patients with septic shock.
ESTHER : Wang_2023_Infect.Drug.Resist_16_6247
PubMedSearch : Wang_2023_Infect.Drug.Resist_16_6247
PubMedID: 37750174

Title : Should we pay attention to the aberrant nerve communication between the lingual and mylohyoid nerves? - Zhan_2019_Br.J.Oral.Maxillofac.Surg_57_317
Author(s) : Zhan C , Yuan Z , Qu R , Zou L , He S , Li Z , Liu C , Xiao Z , Ouyang J , Dai J
Ref : Br J Oral Maxillofac Surg , 57 :317 , 2019
Abstract : An unusual communication between the lingual and mylohyoid nerves has been identified as one reason for incomplete mandibular anaesthesia, and for neuropathy. However, its anatomical features and function are poorly understood and its relations with neighbouring structures, which are valuable in reducing the side effects of surgical operations, have not been sufficiently described. The aim of this study, therefore, was to describe the communication between the nerves and to assess the implications for oral and maxillofacial surgery. We explored the communication between the mylohyoid nerves of 62 embalmed, and 16 fresh, hemifaces. The diameter, length of the communication, and other variables were measured, and the junctions with the two nerves microdissected. The nervous communications of fresh specimens and relative nerves were stained histochemically for acetylcholinesterase. Of the 62 embalmed specimens, 19 had a communication that pierced the mylohyoid muscle, and staining showed that this was a sensory nerve. Our results suggest that the sensory communication between the lingual and mylohyoid nerves pierces the mylohyoid muscle and connects these otherwise unrelated nerves, thereby contributing to the likelihood of operative side effects.
ESTHER : Zhan_2019_Br.J.Oral.Maxillofac.Surg_57_317
PubMedSearch : Zhan_2019_Br.J.Oral.Maxillofac.Surg_57_317
PubMedID: 30940405

Title : Crystal structure of an alpha\/beta serine hydrolase (YDR428C) from Saccharomyces cerevisiae at 1.85 A resolution -
Author(s) : Arndt JW , Schwarzenbacher R , Page R , Abdubek P , Ambing E , Biorac T , Canaves JM , Chiu HJ , Dai X , Deacon AM , DiDonato M , Elsliger MA , Godzik A , Grittini C , Grzechnik SK , Hale J , Hampton E , Han GW , Haugen J , Hornsby M , Klock HE , Koesema E , Kreusch A , Kuhn P , Jaroszewski L , Lesley SA , Levin I , McMullan D , McPhillips TM , Miller MD , Morse A , Moy K , Nigoghossian E , Ouyang J , Peti WS , Quijano K , Reyes R , Sims E , Spraggon G , Stevens RC , van den Bedem H , Velasquez J , Vincent J , von Delft F , Wang X , West B , White A , Wolf G , Xu Q , Zagnitko O , Hodgson KO , Wooley J , Wilson IA
Ref : Proteins , 58 :755 , 2005
PubMedID: 15624212
Gene_locus related to this paper: yeast-YDR428C