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http://dx.doi.org/10.1016/j.bmc.2012.02.053 | DOI Listing |
J Biol Chem
January 2025
T.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland, 21218, USA. Electronic address:
Truncated hemoglobins (TrHbs) have an ancient origin and are widely distributed in microorganisms where they often serve roles other than dioxygen transport and storage. In extremophiles, these small heme proteins must have features that secure function under challenging conditions: at minimum, they must be folded, retain the heme group, allow substrates to access the heme cavity, and maintain their quaternary structure if present and essential. The genome of the obligate psychropiezophile Shewanella benthica strain KT99 harbors a gene for a TrHb belonging to a little-studied clade of globins (subgroup 2 of group N).
View Article and Find Full Text PDFCell
January 2025
Program in Bioinformatics, Boston University, Boston, MA 02215, USA; Department of Molecular Genetics, University of Toronto, Toronto, ON M5S 1A8, Canada; Center for Network Systems Biology, Boston University, Boston, MA 02218, USA; Department of Chemistry, Boston University, Boston, MA 02215, USA; Department of Chemical Physiology and Biochemistry, Division of Oncological Sciences, Knight Cancer Institute, Oregon Health and Science University, Portland, OR, USA. Electronic address:
Knowledge of protein-metabolite interactions can enhance mechanistic understanding and chemical probing of biochemical processes, but the discovery of endogenous ligands remains challenging. Here, we combined rapid affinity purification with precision mass spectrometry and high-resolution molecular docking to precisely map the physical associations of 296 chemically diverse small-molecule metabolite ligands with 69 distinct essential enzymes and 45 transcription factors in the gram-negative bacterium Escherichia coli. We then conducted systematic metabolic pathway integration, pan-microbial evolutionary projections, and independent in-depth biophysical characterization experiments to define the functional significance of ligand interfaces.
View Article and Find Full Text PDFJ Colloid Interface Sci
January 2025
State Key Laboratory of Medicinal Chemical Biology, Tianjin Key Laboratory of Biosensing and Molecular Recognition, Research Center for Analytical Sciences, College of Chemistry, Nankai University, Tianjin 300071 China; National Chromatographic Research and Analysis Center, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023 China.
Macrophages have emerged as promising cellular vehicles for the delivery of therapeutic agents to tumor sites. However, the cytotoxicity of therapeutic agents toward the cellular carriers and the effective release of therapeutic agents at the tumor site remain the main challenges faced by macrophage-mediated drug delivery systems. Herein, a near-infrared (NIR)-triggered release of self-accelerating cascade nanoreactor (HCFG) delivered by macrophages (HCFG@R) was developed for synergistic tumor photothermal therapy (PTT)/starvation therapy (ST)/chemodynamic therapy (CDT).
View Article and Find Full Text PDFJ Colloid Interface Sci
January 2025
School of Chemistry, Dalian University of Technology, Dalian 116024 PR China. Electronic address:
The development of electrode materials for aqueous ammonium-ion supercapacitors (NH-SCs) has garnered significant attention in recent years. Poor intrinsic conductivity, sluggish electron transfer and ion diffusion kinetics, as well as structural degradation of vanadium oxides during the electrochemical process, pose significant challenges for their efficient ammonium-ion storage. In this work, to address the above issues, the core-shell VO·nHO@poly(3,4-ethylenedioxithiophene) composite (denoted as VOH@PEDOT) is designed and prepared by a simple agitation method to boost the ammonium-ion storage of VO·nHO (VOH).
View Article and Find Full Text PDFLife (Basel)
January 2025
Laboratory of Animal Histology, Faculty of Biology, "Alexandru Ioan Cuza" University of Iași, Carol I bvd. 20A, 700505 Iasi, Romania.
Post-translational modifications (PTMs) of proteins dynamically build the buffering and adapting interface between oncogenic mutations and environmental stressors, on the one hand, and cancer cell structure, functioning, and behavior. Aberrant PTMs can be considered as enabling characteristics of cancer as long as they orchestrate all malignant modifications and variability in the proteome of cancer cells, cancer-associated cells, and tumor microenvironment (TME). On the other hand, PTMs of proteins can enhance anticancer mechanisms in the tumoral ecosystem or sustain the beneficial effects of oncologic therapies through degradation or inactivation of carcinogenic proteins or/and activation of tumor-suppressor proteins.
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