Results 81 to 90 of about 2,014,126 (252)

Exploring the influence of lactoferrin on wound healing and related signaling pathways: a systematic review

open access: yesFEBS Open Bio, EarlyView.
Lactoferrin promotes wound healing by activating MAPK, PI3K/Akt, and extracellular matrix pathways, enhancing fibroblast remodeling, proliferation, and re‐epithelialization. These mechanisms highlight its therapeutic potential in inflammation control, tissue repair, and remodeling.
Morgana Lüdtke Azevedo   +4 more
wiley   +1 more source

A mechanism of protein localization : the signal hypothesis and bacteria [PDF]

open access: yes, 1980
We are studying the molecular mechanism of cellular protein localization. The availability of genetic techniques, such as gene fusion in Escherichia coli, has made this problem particularly amenable to study in this prokaryote.
Hall, M. N.   +5 more
core   +1 more source

Structural studies and functional engineering of NanX: an anhydro‐sialic acid transporter from Escherichia coli

open access: yesFEBS Open Bio, EarlyView.
Biophysical characterisation shows that NanX, a membrane transport protein from the major facilitator superfamily (MFS), forms both monomers and dimers after purification. AlphaFold modelling and substrate docking provide information on residues likely involved in substrate recognition for NanX and another MFS member, NanT.
Michael C. Newton‐Vesty   +13 more
wiley   +1 more source

Porphyromonas gingivalis Outer Membrane Vesicles Mediate Coaggregation and Piggybacking of Treponema denticola and Lachnoanaerobaculum saburreum

open access: yesInternational Journal of Dentistry, 2013
Porphyromonas gingivalis sheds outer membrane vesicles that contain several virulence factors, including adhesins. In this study, we investigated the ability of P.
Daniel Grenier
doaj   +1 more source

Outer Membrane Vesicle Production Facilitates LPS Remodeling and Outer Membrane Maintenance in Salmonella during Environmental Transitions

open access: yesmBio, 2016
The ability of Gram-negative bacteria to carefully modulate outer membrane (OM) composition is essential to their survival. However, the asymmetric and heterogeneous structure of the Gram-negative OM poses unique challenges to the cell’s successful ...
Katherine E. Bonnington, Meta J. Kuehn
doaj   +1 more source

Genetic dissection of human ABCE1 in yeast reveals separable requirements for ribosome recycling and suppression of aberrant reinitiation

open access: yesFEBS Open Bio, EarlyView.
Human ABCE1 cannot functionally replace its yeast ortholog. Yeast–human chimera analysis identified NBD1 as a major interspecies barrier. Genetic screening yielded hABCE1 revertants that rescue yeast viability but fail to suppress aberrant translation reinitiation in the 3′ UTR.
Eriko Nakata   +3 more
wiley   +1 more source

Outer membrane protein assembly mediated by BAM-SurA complexes

open access: yesNature Communications
The outer membrane is a formidable barrier that protects Gram-negative bacteria against environmental threats. Its integrity requires the correct folding and insertion of outer membrane proteins (OMPs) by the membrane-embedded β-barrel assembly machinery
Katherine L. Fenn   +8 more
doaj   +1 more source

Discovery of new biosynthetic pathways: the lipid A story

open access: yesJournal of Lipid Research, 2009
The outer monolayer of the outer membrane of Gram-negative bacteria consists of the lipid A component of lipopolysaccharide (LPS), a glucosamine-based saccharolipid that is assembled on the inner surface of the inner membrane.
Christian R.H. Raetz   +6 more
doaj   +1 more source

The mitochondrial receptor complex [PDF]

open access: yes, 1993
The receptor complex in the mitochondrial outer membrane, which consists of at least seven different proteins, is responsible for the recognition and translocation of cytosolically synthesized preproteins.
Klei, Ida J. van der; id_orcid   +6 more
core   +1 more source

Characterization of the key membrane protein cytochrome Cyc2 from Ghiorsea bivora

open access: yesFEBS Open Bio, EarlyView.
This study reports the first detailed biochemical analysis of Cyc2TAG1_1, a cytochrome protein involved in microbial iron oxidation. We produced and purified this enzyme in E. coli, then measured its iron‐oxidizing efficiency, and characterized its electrical and structural properties.
Josiane Azizi   +6 more
wiley   +1 more source

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