Results 61 to 70 of about 586,788 (291)

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

Structural characterisation of outer membrane proteins from Borrelia burgdorferi sensu lato by small-angle X-ray scattering [PDF]

open access: yes, 2015
Forming the interface between the bacterial cell and the host, the outer membrane of Borrelia is known to play a key role in pathogenicity. Although Borrelia burgdorferi sensu lato are considered to be Gram-negative, their outer membrane is unique ...
Stejskal, Lenka
core   +1 more source

Pseudomonas aeruginosa outer membrane: peptidoglycan-associated proteins [PDF]

open access: yesJournal of Bacteriology, 1981
The Pseudomonas aeruginosa outer membrane was isolated with attached peptidoglycan and fractionated with Triton X-100, ethylenediaminetetraacetate, and lysozyme. The data suggest that major outer membrane proteins F, H2, and I are noncovalently associated with the peptidoglycan.
R E, Hancock   +3 more
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

Mitochondrial protein import [PDF]

open access: yes, 1994
The transport of nuclear-encoded proteins from the cytosol into mitochondria is mediated by targeting (signal) sequences present on precursor forms.
Neupert, Walter, Schwarz, Elisabeth
core   +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

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

Cross Reaction among Antibody Pili sub unit Hemagglutinin Proteins and Outer Membrane sub unit Hemagglutinin Proteins of Shigella flexneri

open access: yesJournal of Tropical Life Science, 2017
Shigella  flexneri is the most common causal agent of shigellosis. Its pili are composed of pili protein subunits. Adhesion molecules can be found on the pili and outer membrane proteins (Omp).
Avin Ainur Fitrianingsih   +6 more
doaj   +1 more source

Defining the core proteome of the chloroplast envelope membranes [PDF]

open access: yes, 2013
High-throughput protein localization studies require multiple strategies. Mass spectrometric analysis of defined cellular fractions is one of the complementary approaches to a diverse array of cell biological methods. In recent years, the protein content
Ibrahim, Mohamed   +9 more
core   +2 more sources

Outer Membrane Proteins of Fusobacterium nucleatum Fev1 [PDF]

open access: yesMicrobiology, 1986
Outer membrane enriched material from six strains of Fusobacterium nucleatum was analysed by SDS-PAGE. The protein profiles of all the strains were dominated by proteins with molecular masses of about 40 kDa, and a very high degree of homology in relation to apparent molecular masses was observed.
V, Bakken, H B, Jensen
openaire   +2 more sources

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