Results 121 to 130 of about 1,113,140 (269)

AscF in the mycobacterial CIII–CIV supercomplex lacks metal and nucleotide binding but links malate oxidation to respiration

open access: yesFEBS Letters, EarlyView.
The mycobacterial CIII‐CIV respiratory supercomplex is an obligate assembly, encompassing several subunits of unknown functions. We have characterized the intracellular subunit AscF, and show that it is unlikely to be a sensor for metals or nucleotides, but is required for growth on nonfermentable energy sources, and likely works as an adapter for ...
Eni Rile   +8 more
wiley   +1 more source

The therapeutic opportunities and pitfalls of using iron ion chelators to treat neurodegenerative diseases

open access: yesFEBS Letters, EarlyView.
Although too much iron in the brain promotes neurodegeneration, iron ion chelators have had mixed effects in clinical trials. This review explains why; some chelators do not render the iron redox‐inactive (e.g., L1) whereas others do (e.g., desferrioxamine).
Barry Halliwell
wiley   +1 more source

An epithelial GPR35 isoform supports tumor‐associated transcriptional and metabolic phenotypes

open access: yesFEBS Letters, EarlyView.
GPR35 generates two functionally distinct isoforms with previously unresolved roles. GPR35‐short mediates immune‐cell chemotaxis, while GPR35‐long is enriched in colorectal cancer epithelium, where it supports increased metabolism, proliferation, and tumor‐associated transcriptional programs.
Jørgen D. Rønneberg   +14 more
wiley   +1 more source

Structure‐forward targeting of claudins with synthetic binders

open access: yesFEBS Letters, EarlyView.
Claudins form the paracellular barriers between epithelial and endothelial tissues at tight junctions and are targets for molecular binders with the goal of modulating barrier permeability. Claudin‐binding molecules are relevant in drug delivery or in altering claudin interactions with disease‐causing proteins.
Alex J. Vecchio
wiley   +1 more source

Discerning protein pools by selective staining with self‐labeling tags

open access: yesFEBS Letters, EarlyView.
Cell surface proteins have an intra‐ and extracellular pool. Combining genetic fusion to self‐labeling tags that can be addressed with small molecule fluorophores allows separating these pools. We highlight recent developments and techniques for state‐of‐the‐art interrogation of cell surface proteins in the complex tissue setting.
Kati Fischermanns, Johannes Broichhagen
wiley   +1 more source

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