Results 61 to 70 of about 882,725 (292)

β-Barrel Assembly Machinery (BAM) Complex as Novel Antibacterial Drug Target

open access: yesMolecules, 2023
The outer membrane of Gram-negative bacteria is closely related to the pathogenicity and drug resistance of bacteria. Outer membrane proteins (OMPs) are a class of proteins with important biological functions on the outer membrane.
Qian Xu, Min Guo, Feiyuan Yu
doaj   +1 more source

An upstream open reading frame regulates expression of the mitochondrial protein Slm35 and mitophagy flux

open access: yesFEBS Letters, EarlyView.
This study reveals how the mitochondrial protein Slm35 is regulated in Saccharomyces cerevisiae. The authors identify stress‐responsive DNA elements and two upstream open reading frames (uORFs) in the 5′ untranslated region of SLM35. One uORF restricts translation, and its mutation increases Slm35 protein levels and mitophagy.
Hernán Romo‐Casanueva   +5 more
wiley   +1 more source

Biogenesis of mitochondrial β‐barrel membrane proteins

open access: yesFEBS Open Bio
β‐barrel membrane proteins in the mitochondrial outer membrane are crucial for mediating the metabolite exchange between the cytosol and the mitochondrial intermembrane space. In addition, the β‐barrel membrane protein subunit Tom40 of the translocase of
Iniyan Ganesan   +3 more
doaj   +1 more source

Specific association of lectin LecB with the surface of Pseudomonas aeruginosa: role of outer membrane protein OprF. [PDF]

open access: yesPLoS ONE, 2012
The fucose binding lectin LecB affects biofilm formation and is involved in pathogenicity of Pseudomonas aeruginosa. LecB resides in the outer membrane and can be released specifically by treatment of an outer membrane fraction with fucose suggesting ...
Horst Funken   +8 more
doaj   +1 more source

Translocation arrest by reversible folding of a precursor protein imported into mitochondria [PDF]

open access: yes, 1989
Passage of precursor proteins through translocation contact sites of mitochondria was investigated by studying the import of a fusion protein consisting of the NH2-terminal 167 amino acids of yeast cytochrome b2 precursor and the complete mouse ...
Guiard, Bernard   +5 more
core  

Ultrastructural Localization of Rhodopsin in the Vertebrate Retina [PDF]

open access: yes, 1974
Early work by Dewey and collaborators has shown the distribution of rhodopsin in the frog retina. We have repeated these experiments on cow and mouse eyes using antibodies specific to rhodopsin alone.
Jan, Lily Yeh, Revel, Jean-Paul
core   +5 more sources

Deoxyribonucleic acid and outer membrane: binding to outer membrane involves a specific protein [PDF]

open access: yesJournal of Bacteriology, 1979
The binding of deoxyribonucleic acid (DNA) to the outer membrane of Escherichia coli was examined. The amount of DNA found to be bound to outer membrane was low and was estimated to be about 0.4% of the total DNA. Treatment of cells with chloramphenicol or rifampin caused a disassociation of the apparent DNA-outer membrane complex.
H, Wolf-Watz, A, Norqvist
openaire   +2 more sources

In situ molecular organization and heterogeneity of the Legionella Dot/Icm T4SS

open access: yesFEBS Letters, EarlyView.
We present a nearly complete in situ model of the Legionella Dot/Icm type IV secretion system, revealing its central secretion channel and identifying new components. Using cryo‐electron tomography with AI‐based modeling, our work highlights the structure, variability, and mechanism of this complex nanomachine, advancing understanding of bacterial ...
Przemysław Dutka   +11 more
wiley   +1 more source

Antibiotic Resistance and Regulation of the Gram-Negative Bacterial Outer Membrane Barrier by Host Innate Immune Molecules

open access: yesmBio, 2016
The Gram-negative outer membrane is an important barrier that provides protection against toxic compounds, which include antibiotics and host innate immune molecules such as cationic antimicrobial peptides.
Samuel I. Miller
doaj   +1 more source

Structural biology of ferritin nanocages

open access: yesFEBS Letters, EarlyView.
Ferritin is a conserved iron‐storage protein that sequesters iron as a ferric mineral core within a nanocage, protecting cells from oxidative damage and maintaining iron homeostasis. This review discusses ferritin biology, structure, and function, and highlights recent cryo‐EM studies revealing mechanisms of ferritinophagy, cellular iron uptake, and ...
Eloise Mastrangelo, Flavio Di Pisa
wiley   +1 more source

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