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A preliminary study on the prognostic significance of cysteine-rich EGF ligand domain 2 protein (CRELD2) in patients with triple negative breast cancer.
Biomol Biomed
January 2025
Necmettin Erbakan University, Meram Faculty of Medicine, Department of Medical Oncology, Konya, Turkey.
The cysteine-rich epidermal growth factor ligand domain 2 protein (CRELD2) is associated with pathways that regulate epithelial-to-mesenchymal transition, a critical process driving cancer metastasis. This study aimed to determine the prognostic value of CRELD2 status on survival outcomes in triple-negative breast cancer (TNBC). Seventy patients were included in the study.
View Article and Find Full Text PDFThe role of canopy family proteins: biological mechanism and disease function.
Mol Biol Rep
January 2025
Department of Gastroenterology, Beijing Friendship Hospital, Capital Medical University, No. 95, Yong An Road, Xi Cheng District, Beijing, 100050, China.
Canopy family proteins are highly sequence-conserved proteins with an N-terminal hydrophobic signal sequence, a unique pattern of six cysteine residues characteristic of the saposin-like proteins, and a C-terminal putative endoplasmic reticulum retention signal sequence. At present, the known canopy family proteins are canopy fibroblast growth factor signaling regulator 1 (CNPY1), CNPY2, CNPY3, and CNPY4. Despite similar structures, canopy family proteins regulate complex signal networks to participate in various biological processes.
View Article and Find Full Text PDFTuning the lanthanide binding tags for preferential actinide chelation: an all atom molecular dynamics study.
Phys Chem Chem Phys
January 2025
Chemistry Division, Bhabha Atomic Research Centre, Mumbai, 400085, India.
The present study focuses on designing mutant peptides derived from the lanthanide binding tag (LBT) to enhance selectivity for trivalent actinide (An) ions over lanthanide (Ln) metal ions (M). The LBT is a short peptide consisting of only 17 amino acids, and is known for its high affinity towards Ln. LBT was modified by substituting hard-donor ligands like asparagine (ASN or N) and aspartic acid (ASP or D) with softer ligand cysteine (CYS or C) to create four mutant peptides: M-LBT (wild-type), M-N103C, M-D105C, and M-N103C-D105C.
View Article and Find Full Text PDFProbing the Influence of the Protein Scaffold on H-Cluster Reactivity via Gain-of-Function Studies─Improved H Evolution and O Tolerance through Rational Design of [FeFe] Hydrogenase.
J Am Chem Soc
January 2025
Molecular Biomimetics, Department of Chemistry, Ångström Laboratory, Uppsala University, P.O. Box 523, Uppsala SE-75120, Sweden.
[FeFe] hydrogenases make up a structurally diverse family of metalloenzymes that catalyze proton/dihydrogen interconversion. They can be classified into phylogenetically distinct groups denoted A-G, which differ in structure and reactivity. Prototypical Group A hydrogenases have high turnover rates and remarkable energy efficiency.
View Article and Find Full Text PDFA steric hindrance-regulated probe with single excitation dual emissions for self-adaptive detection of biothiols and HS in human urine samples and living cells.
J Mater Chem B
January 2025
Department of General Surgery, The Second Xiangya Hospital, Central South University, Changsha, China.
Sulfur-containing small molecules, mainly including cysteine (Cys), homocysteine (Hcy), glutathione (GSH), and hydrogen sulfide (HS), are crucial biomarkers, and their levels in different body locations (living cells, tissues, blood, urine, saliva, ) are inconsistent and constantly changing. Therefore, it is highly meaningful and challenging to synchronously and accurately detect them in complex multi-component samples without mutual interference. In this work, we propose a steric hindrance-regulated probe, NBD-2FDCI, with single excitation dual emissions to achieve self-adaptive detection of four analytes.
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