Pages that link to "Q42126957"
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The following pages link to Targeting of passenger protein domains to multiple intracellular membranes (Q42126957):
Displaying 13 items.
- Structural insights into tail-anchored protein binding and membrane insertion by Get3 (Q27658386) (← links)
- Identification of the endoplasmic reticulum targeting signal in vesicle-associated membrane proteins. (Q33883841) (← links)
- Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins (Q37307105) (← links)
- The approaches for manipulating mitochondrial proteome (Q37764798) (← links)
- A site-specific, membrane-dependent cleavage event defines the membrane binding domain of FtsY. (Q38318537) (← links)
- The signal recognition particle receptor alpha subunit assembles co-translationally on the endoplasmic reticulum membrane during an mRNA-encoded translation pause in vitro. (Q41063577) (← links)
- Bcl-2 mutants with restricted subcellular location reveal spatially distinct pathways for apoptosis in different cell types (Q41076577) (← links)
- The C-terminus of cytochrome b5 confers endoplasmic reticulum specificity by preventing spontaneous insertion into membranes (Q43010046) (← links)
- Hydrophobic-domain-dependent protein-protein interactions mediate the localization of GPAT enzymes to ER subdomains (Q44350917) (← links)
- Membrane-bound fatty acid desaturases are inserted co-translationally into the ER and contain different ER retrieval motifs at their carboxy termini (Q44702894) (← links)
- Novel targeting signals mediate the sorting of different isoforms of the tail-anchored membrane protein cytochrome b5 to either endoplasmic reticulum or mitochondria (Q48168157) (← links)
- An amino-terminal domain containing hydrophobic and hydrophilic sequences binds the signal recognition particle receptor alpha subunit to the beta subunit on the endoplasmic reticulum membrane. (Q54170054) (← links)
- The cotranslational integration of membrane proteins into the phospholipid bilayer is a multistep process (Q71046930) (← links)