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A putative 'translocator' complex resides in the PV membrane (PVM); it consists of 5 proteins that coprecipitate some of the proteins bearing a host cell targeting signal, but a function of the complex has not been demonstrated in any way, nor has it been investigated whether the association of the complex and the PEXEL proteins is mediated by the PEXEL signal.
Therefore, the present study indicates the in-vivo immunogenic and inflammatory potential of flagellin (FliC) phenotype which is an integral part of flagellar motor complex, resides in the outer membrane of the serovar Typhi.
The Hsp60/HSPD complex resides in mitochondria; however, a comparable eukaryotic chaperonin system known as TRiC (also known as CCT) is present in the cytosol and is mainly involved in tubulin and actin folding.
In yeast, a Class III phosphatidylinositol 3-kinase (PI3K) complex resides in the pre-autophagosomal structure/phagophore assembly site (PAS) where it catalyzes phosphatidylinositol 3-phosphate (PI3P) synthesis and recruits PI3P-binding proteins, especially the ATG18-ATG2 complex, for the initiation of autophagic membranes [ 11- 13].
As revealed by electron and light microscopy the MIND/MIS12 complex resides in the inner plate of the kinetochore and consists of four subunits; Mis12, Nnf1, Nsl1 and Dsn1 [1].
The Rh(I) metal complex resides in the original liquid phase, while the product of hydrogen addition is found exclusively in the gaseous phase based on the affinity.
Insect desaturases are homologous to the ancestral Δ9 acyl-CoA desaturases of plants, vertebrates and fungi and are functioning as part of a multienzyme complex residing in the endoplasmic reticulum (ER) [ 11- 14].
For example, a protein-protein complex residing in the bound conformational state while performing its function and before proceeding to the dissociation state, or the components of the complex becoming trapped in a local minimum of the free energy landscape before finding their optimal docked, and fully functional, conformational state.
The seven nuclear encoded-subunits of the "core complex" reside in the hydrophilic domain and participate in the oxidation of NADH and transfer of electrons to ubiquinone.
In mitotically dividing cells, Csm1 and Lrs4 form a complex that resides in the nucleolus [ 41], where it recruits condensin to replication fork barriers within each rDNA repeat [ 42].
The SR45/U1-70K complexhibithibit very slow mobility, indicating that SR45/U1-70K complexes reside in the speckles for a longer time probably in a storage form consistent with the proposed role of speckles as storage sites for pre-mRNA processing factors [28].
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