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Structure-function coupling alterations in cognitively normal individuals with white matter hyperintensities.
J Alzheimers Dis
January 2025
Department of Neurology, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, China.
Background: White matter hyperintensities (WMH) are prominent neuroimaging markers of cerebral small vessel disease (CSVD) linked to cognitive decline. Nevertheless, the pathophysiological mechanisms underlying WMH remain unclear.
Objective: This study aimed to assess the structural decoupling index (SDI) as a novel metric for quantifying the brain's hierarchical organization associated with WMH in cognitively normal older adults
Methods: We analyzed data from 112 cognitively normal individuals with varying WMH burdens (43 high WMH burden and 69 low WMH burden).
Elucidating the structure and function of a membrane-active plant protein domain using in silico mutagenesis.
Biochim Biophys Acta Biomembr
January 2025
Land and Food Systems, University of British Columbia, Vancouver, Canada; Faculty of Agricultural, Life and Environmental Sciences, University of Alberta, Edmonton, Canada. Electronic address:
The Solanum tuberosum (common potato) plant specific insert (StPSI) is an antimicrobial protein domain that exhibits membrane-disrupting and membrane-fusing activity upon dimerization at acidic pH, activity proposed to involve electrostatic attraction and membrane anchoring mediated by specific positively-charged and conserved tryptophan residues, respectively. This study is the first to employ an in silico mutagenesis approach to clarify the structure-function relationship of a plant specific insert (PSI), where ten rationally-mutated StPSI variants were investigated using all-atom and coarse-grained molecular dynamics. The tryptophan (W) residue at position 18 (W18) of wild-type StPSI was predicted to confer structural flexibility to the dimer and mediate a partial separation of the assembled monomers upon bilayer contact, while residues including W77 and the lysine (K) residue at position 83 (K83) were predicted to stabilize secondary structure and influence association with the model membrane.
View Article and Find Full Text PDFBayesian thresholded modeling for integrating brain node and network predictors.
Biostatistics
December 2024
Department of Biostatistics, Yale University, 300 George St, New Haven, CT 06511, United States.
Progress in neuroscience has provided unprecedented opportunities to advance our understanding of brain alterations and their correspondence to phenotypic profiles. With data collected from various imaging techniques, studies have integrated different types of information ranging from brain structure, function, or metabolism. More recently, an emerging way to categorize imaging traits is through a metric hierarchy, including localized node-level measurements and interactive network-level metrics.
View Article and Find Full Text PDFThe properties of solids: 'If you want to understand function, study structure'.
J Phys Condens Matter
January 2025
Peter-Grünberg-Institut PGI-1, Forschungszentrum Jülich, D-52425 Jülich, Germany.
The importance of the structure-function relationship in molecular biology was confirmed dramatically by the recent award of the 2024 Nobel Prize in Chemistry 'for computational protein design' and 'for protein structure prediction'. The relationship is also important in chemistry and condensed matter physics, and we survey here structural concepts that have been developed over the past century, particularly in chemistry. As an example we take structural phase transitions in phase-change materials (PCM), which can be switched rapidly and reversibly between amorphous and crystalline states.
View Article and Find Full Text PDFThe sequence-structure-function relationship of intrinsic ERα disorder.
Nature
January 2025
Case Comprehensive Cancer Center and Department of Nutrition, Case Western Reserve University School of Medicine, Cleveland, OH, USA.
The oestrogen receptor (ER or ERα), a nuclear hormone receptor that drives most breast cancer, is commonly activated by phosphorylation at serine 118 within its intrinsically disordered N-terminal transactivation domain. Although this modification enables oestrogen-independent ER function, its mechanism has remained unclear despite ongoing clinical trials of kinase inhibitors targeting this region. By integration of small-angle X-ray scattering and nuclear magnetic resonance spectroscopy with functional studies, we show that serine 118 phosphorylation triggers an unexpected expansion of the disordered domain and disrupts specific hydrophobic clustering between two aromatic-rich regions.
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