Adjuvants comprising OmpC porin, OmpF porin, or a combination thereof, are provided.
Provided herein are isolated polypeptides comprising the amino-terminal domain of Mycobacterium tuberculosis porin A (MtpA), wherein the polypeptide is a porin monomer.
The invention relates to a porin gene from Campylobacter jejuni [SEQ ID NO:3].
The composition can further optionally comprise a Salmonella spp. porin component.
Voltage-dependent anion-selective channel protein 1 (VDAC1), also named porin 31HM, porin 31HL or plasmalemmal porin, is universally expressed throughout tissues and conserved across species.
OmpC, OmpF or a combination thereof, and can be combined with the PapMV component or conjugated to the PapMV component.
The porin component can be a Salmonella spp.
The treatment with angiotensin II can be combined with use of the peptide RGD to compete with the binding of the extracellular matrix protein and so suppress its effect.
Carbapenems, for example, pass through a specific porin, a sort of channel normally used to import nutrients.
Oxytetracycline is lipophilic and can easily pass through the cell membrane or passively diffuses through porin channels in the bacterial membrane.
Lymecycline is lipophilic and can easily pass through the cell membrane or passively diffuses through porin channels in the bacterial membrane.
VDAC, also called porin, is the most abundant protein of the outer mitochondrial membrane and forms a non-selective pore through the outer membrane.
The present invention relates, in general, to a method for obtaining the outer membrane protein meningococcal group B porin proteins, in particular MB3, and fusion proteins thereof.
Porin Each defines a channel through the aqueous and lipid bilayer letting all the molecules of molecular weight or less 7KDa.
The invention discloses the uses of the polynucleotide, which encodes a human protein 9 containing the fragment of prion characteristic sequence.
Since the different pathways leading to the inhibition of the production of this porin use Hfq, this chaperone becomes a promising therapeutic target.
Porin-like barrel structures are encoded by as many as 2–3% of the genes in Gram-negative bacteria.[1]
Porin-like barrel structures account for as many as 2–3% of the genes in gram-negative bacteria.[1]
These iron channels also enable the drug to bypass the bacteria’s porin channels and gain repeat entry even if the bacterium has evolved efflux pumps.
These iron channels also enable the drug to bypass the bacteria's porin channels and gain repeat entry even if the bacterium has evolved efflux pumps.
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