Results 61 to 70 of about 3,840,867 (319)

Polyphosphate and tyrosine phosphorylation in the N-terminal domain of the human mitochondrial Lon protease disrupts its functions

open access: yesScientific Reports
Phosphorylation plays a crucial role in the regulation of many fundamental cellular processes. Phosphorylation levels are increased in many cancer cells where they may promote changes in mitochondrial homeostasis.
Nina Kunová   +16 more
doaj   +1 more source

Cilia regeneration requires an RNA splicing factor from the ciliary base

open access: yesCell Regeneration, 2022
Cilia are microtubule-based organelles projected from most eukaryotic cell surfaces performing cell motility and signaling. Several previously recognized non-ciliary proteins play crucial roles in cilium formation and function.
Kaiming Xu, Guangshuo Ou
doaj   +1 more source

Flexible protein folding by ant colony optimization [PDF]

open access: yes, 2008
Protein structure prediction is one of the most challenging topics in bioinformatics. As the protein structure is found to be closely related to its functions, predicting the folding structure of a protein to judge its functions is meaningful to the ...
Hu, X., Li, Y., Zhang, J.
core   +1 more source

Refining the NaV1.7 pharmacophore of a class of venom‐derived peptide inhibitors via a combination of in silico screening and rational engineering

open access: yesFEBS Letters, EarlyView.
Venom peptides have shown promise in treating pain. Our study uses computer screening to identify a peptide that targets a sodium channel (NaV1.7) linked to chronic pain. We produced the peptide in the laboratory and refined its design, advancing the search for innovative pain therapies.
Gagan Sharma   +8 more
wiley   +1 more source

Molecular basis for protein histidine N1-specific methylation of the “His-x-His” motifs by METTL9

open access: yesCell Insight, 2023
Histidine methylation serves as an intriguing strategy to introduce altered traits of target proteins, including metal ion chelation, histidine-based catalysis, molecular assembly, and translation regulation.
Wentao Zhao   +6 more
doaj  

Crystal structure of 4,6-diamino-2,2-dimethyl-3-[3-(2,4,5-trichlorophenoxy)propoxy]-2,3-dihydro-1,3,5-triazin-1-ium chloride methanol monosolvate

open access: yesActa Crystallographica Section E: Crystallographic Communications, 2015
In the title methanol-solvated salt, C14H19Cl3N5O2+·Cl−·CH3OH, the triazine molecule is protonated at one of the triazine N atoms. In the crystal, the triazine cations are linked through a pair of N—H...N hydrogen bonds, with graph-set R22(8), forming an
Pattarapol Khongsuk   +2 more
doaj   +1 more source

The power of microRNA regulation—insights into immunity and metabolism

open access: yesFEBS Letters, EarlyView.
MicroRNAs are emerging as crucial regulators at the intersection of metabolism and immunity. This review examines how miRNAs coordinate glucose and lipid metabolism while simultaneously modulating T‐cell development and immune responses. Moreover, it highlights how cutting‐edge artificial intelligence applications can identify miRNA biomarkers ...
Stefania Oliveto   +2 more
wiley   +1 more source

Macromolecular crystallography from an industrial perspective – the impact of synchrotron radiation on structure-based drug discovery

open access: yesJournal of Synchrotron Radiation
Structure-based drug design has been an integral part of drug discovery for over three decades, contributing to the development of numerous approved drugs. Here we discuss the evolution, as well as the current state, of structure-based drug design within
H. Käck, T. Sjögren
doaj   +1 more source

Protein Structure Prediction until CASP15 [PDF]

open access: yesarXiv, 2022
In Dec 2020, the results of AlphaFold2 were presented at CASP14, sparking a revolution in the field of protein structure predictions. For the first time, a purely computational method could challenge experimental accuracy for structure prediction of single protein domains.
arxiv  

On the optimal contact potential of proteins

open access: yes, 2007
We analytically derive the lower bound of the total conformational energy of a protein structure by assuming that the total conformational energy is well approximated by the sum of sequence-dependent pairwise contact energies.
Akira R. Kinjo   +32 more
core   +1 more source

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