Results 121 to 130 of about 9,273,371 (361)

The role and implications of mammalian cellular circadian entrainment

open access: yesFEBS Letters, EarlyView.
At their most fundamental level, mammalian circadian rhythms occur inside every individual cell. To tell the correct time, cells must align (or ‘entrain’) their circadian rhythm to the external environment. In this review, we highlight how cells entrain to the major circadian cues of light, feeding and temperature, and the implications this has for our
Priya Crosby
wiley   +1 more source

Molecular bases of circadian magnesium rhythms across eukaryotes

open access: yesFEBS Letters, EarlyView.
Circadian rhythms in intracellular [Mg2+] exist across eukaryotic kingdoms. Central roles for Mg2+ in metabolism suggest that Mg2+ rhythms could regulate daily cellular energy and metabolism. In this Perspective paper, we propose that ancestral prokaryotic transport proteins could be responsible for mediating Mg2+ rhythms and posit a feedback model ...
Helen K. Feord, Gerben van Ooijen
wiley   +1 more source

Crosstalk between the ribosome quality control‐associated E3 ubiquitin ligases LTN1 and RNF10

open access: yesFEBS Letters, EarlyView.
Loss of the E3 ligase LTN1, the ubiquitin‐like modifier UFM1, or the deubiquitinating enzyme UFSP2 disrupts endoplasmic reticulum–ribosome quality control (ER‐RQC), a pathway that removes stalled ribosomes and faulty proteins. This disruption may trigger a compensatory response to ER‐RQC defects, including increased expression of the E3 ligase RNF10 ...
Yuxi Huang   +8 more
wiley   +1 more source

Central Africa

open access: yes
The pattern of infectious diseases in Central Africa is determined by climatic conditions and socioeconomic factors. The climate in most parts is tropical, i.e., hot and humid. The region is dominated by the Congo River and its tributaries, and the area is covered mostly by savannah or primary and secondary tropical rainforests.
Grobusch, Martin P.   +2 more
openaire   +2 more sources

Peptide‐based ligand antagonists block a Vibrio cholerae adhesin

open access: yesFEBS Letters, EarlyView.
The structure of a peptide‐binding domain of the Vibrio cholerae adhesin FrhA was solved by X‐ray crystallography, revealing how the inhibitory peptide AGYTD binds tightly at its Ca2+‐coordinated pocket. Structure‐guided design incorporating D‐amino acids enhanced binding affinity, providing a foundation for developing anti‐adhesion therapeutics ...
Mingyu Wang   +9 more
wiley   +1 more source

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