Results 51 to 60 of about 7,997,979 (337)

Ubiquitin-derived artificial binding proteins targeting oncofetal fibronectin reveal scaffold plasticity by β-strand slippage

open access: yesCommunications Biology
Affilin proteins, artificial binding proteins based on the ubiquitin scaffold, have been generated by directed protein evolution to yield de-novo variants that bind the extra-domain B (EDB) of oncofetal fibronectin, an established marker of tumor ...
Anja Katzschmann   +6 more
doaj   +1 more source

Structure and stability of recombinant bovine odorant-binding protein: II. Unfolding of the monomeric forms [PDF]

open access: yesPeerJ, 2016
In a family of monomeric odorant-binding proteins (OBPs), bovine OBP (bOBP), that lacks conserved disulfide bond found in other OBPs, occupies unique niche because of its ability to form domain-swapped dimers.
Olga V. Stepanenko   +5 more
doaj   +2 more sources

Food proteins and peptides [PDF]

open access: yes, 2015
The qualitative and quantitative determination of proteins and peptides in raw or processed food is experiencing a growing interest and importance from both scientific and economic point of view.
CAPRIOTTI, ANNA LAURA   +5 more
core   +1 more source

Mapping the evolution of mitochondrial complex I through structural variation

open access: yesFEBS Letters, EarlyView.
Respiratory complex I (CI) is crucial for bioenergetic metabolism in many prokaryotes and eukaryotes. It is composed of a conserved set of core subunits and additional accessory subunits that vary depending on the organism. Here, we categorize CI subunits from available structures to map the evolution of CI across eukaryotes. Respiratory complex I (CI)
Dong‐Woo Shin   +2 more
wiley   +1 more source

Structure and stability of recombinant bovine odorant-binding protein: I. Design and analysis of monomeric mutants [PDF]

open access: yesPeerJ, 2016
Bovine odorant-binding protein (bOBP) differs from other lipocalins by lacking the conserved disulfide bond and for being able to form the domain-swapped dimers.
Olga V. Stepanenko   +5 more
doaj   +2 more sources

Specific protein-protein binding in many-component mixtures of proteins [PDF]

open access: yes, 2003
Proteins must bind to specific other proteins in vivo in order to function. The proteins must bind only to one or a few other proteins of the of order a thousand proteins typically present in vivo.
Alberts B   +14 more
core   +2 more sources

Enteropathogenic E. coli shows delayed attachment and host response in human jejunum organoid‐derived monolayers compared to HeLa cells

open access: yesFEBS Letters, EarlyView.
Enteropathogenic E. coli (EPEC) infects the human intestinal epithelium, resulting in severe illness and diarrhoea. In this study, we compared the infection of cancer‐derived cell lines with human organoid‐derived models of the small intestine. We observed a delayed in attachment, inflammation and cell death on primary cells, indicating that host ...
Mastura Neyazi   +5 more
wiley   +1 more source

Structure and stability of recombinant bovine odorant-binding protein: III. Peculiarities of the wild type bOBP unfolding in crowded milieu [PDF]

open access: yesPeerJ, 2016
Contrary to the majority of the members of the lipocalin family, which are stable monomers with the specific OBP fold (a β-barrel consisting of a 8-stranded anti-parallel β-sheet followed by a short α-helical segment, a ninth β-strand, and a disordered C-
Olga V. Stepanenko   +5 more
doaj   +2 more sources

Plasmodium falciparum gametogenesis essential protein 1 (GEP1) is a transmission‐blocking target

open access: yesFEBS Letters, EarlyView.
This study shows Plasmodium falciparum GEP1 is vital for activating sexual stages of malarial parasites even independently of a mosquito factor. Knockout parasites completely fail gamete formation even when a phosphodiesterase inhibitor is added. Two single‐nucleotide polymorphisms (V241L and S263P) are found in 12%–20% of field samples.
Frederik Huppertz   +5 more
wiley   +1 more source

Ferritins: furnishing proteins with iron [PDF]

open access: yes, 2016
Ferritins are a superfamily of iron oxidation, storage and mineralization proteins found throughout the animal, plant, and microbial kingdoms. The majority of ferritins consist of 24 subunits that individually fold into 4-α-helix bundles and assemble in ...
A Crow   +88 more
core   +1 more source

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