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The structure of bacterial outer membrane proteins
Biochimica et Biophysica Acta (BBA) - Biomembranes, 2002 Integral membrane proteins come in two types, alpha-helical and beta-barrel proteins. In both types, all hydrogen bonding donors and acceptors of the polypeptide backbone are completely compensated and buried while nonpolar side chains point to the membrane. The alpha-helical type is more abundant and occurs in cytoplasmic (or inner) membranes, whereas
openaire +3 more sources
FEBS Open Bio, EarlyView.Amino acids sequence of two different proteins with the same sequence (chameleon sequence—black boxes) represent in 3D structure of the proteins different secondary structures: HHHH—helical and BBB—Beta‐structural. The chains folded in water environment adopt different III‐order structures in which the chameleon fragments appear to adopt similar status
Irena Roterman +4 more
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MembranesThe alarming rise of antibiotic resistance in Gram-negative bacteria has emerged as a major global health challenge. A key factor contributing to this crisis is the low permeability of the bacterial outer membrane, which acts as a barrier that prevents ...
Ishan Ghai
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Evasion of autophagy mediated by Rickettsia surface protein OmpB is critical for virulence. [PDF]
, 2019 Rickettsia are obligate intracellular bacteria that evade antimicrobial autophagy in the host cell cytosol by unknown mechanisms. Other cytosolic pathogens block different steps of autophagy targeting, including the initial step of polyubiquitin-coat ...
Burke, Thomas P +9 more
core
BUSCA: An integrative web server to predict subcellular localization of proteins [PDF]
, 2018 Here, we present BUSCA (http://busca.biocomp.unibo.it), a novel web server that integrates different computational tools for predicting protein subcellular localization.
Casadio, Rita +4 more
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Evolutionarily divergent DUF4465 domains have a common vitamin B12‐binding function
FEBS Open Bio, EarlyView.We show that DUF4465 family proteins, widespread across bacteria from gut microbiomes, hydrothermal vents, and soil, share a common vitamin B12‐binding function. These augmented β‐jellyroll proteins bind vitamin B12 via extended loops. Our findings establish sequence‐diverse DUF4465 proteins as a widespread class of B12‐binding proteins, highlighting ...
Charlea Clarke +4 more
wiley +1 more source
Oxidative protein biogenesis and redox regulation in the mitochondrial intermembrane space [PDF]
, 2016 Mitochondria are organelles that play a central role in cellular metabolism, as they are responsible for processes such as iron/sulfur cluster biogenesis, respiration and apoptosis.
MacPherson, Lisa +2 more
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FEBS Open Bio, EarlyView.Activation of the mitochondrial protein OXR1 increases pSyn129 αSynuclein aggregation by lowering ATP levels and altering mitochondrial membrane potential, particularly in response to MSA‐derived fibrils. In contrast, ablation of the ER protein EMC4 enhances autophagic flux and lysosomal clearance, broadly reducing α‐synuclein aggregates.
Sandesh Neupane +11 more
wiley +1 more source
Complement-mediated killing of Escherichia coli by mechanical destabilization of the cell envelope
The EMBO JournalComplement proteins eliminate Gram-negative bacteria in the blood via the formation of membrane attack complex (MAC) pores in the outer membrane. However, it remains unclear how outer membrane poration leads to inner membrane permeation and cell lysis ...
Georgina Benn +5 more
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Detection of the babA2 adhesin gene in Helicobacter pylori clinical isolates and correlation with upper gastrointestinal diseases [PDF]
Anais da Academia Brasileira de CiênciasHelicobacter pylori is an oncobacteria that infects more than half of the world’s population. Adhesins are virulence factors that are essential for the microorganism to bind to the gastric mucosa, such as the BabA adhesion protein, which is associated ...
DIOGO NERY MACIEL +5 more
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