Human La protein is an essential factor in the biology of both coding and non-coding RNAs. In the nucleus, La binds primarily to 3' oligoU containing RNAs, while in the cytoplasm La interacts with an array of different mRNAs lacking a 3' UUUOH trailer. An example of the latter is the binding of La to the IRES domain IV of the hepatitis C virus (HCV) RNA, which is associated with viral translation stimulation. By systematic biophysical investigations, we have found that La binds to domain IV using an RNA recognition that is quite distinct from its mode of binding to RNAs with a 3' UUUOH trailer: although the La motif and first RNA recognition motif (RRM1) are sufficient for high-affinity binding to 3' oligoU, recognition of HCV domain IV req...
Human La protein is known to interact with hepatitis C virus (HCV) internal ribosome entry site (IRE...
The La protein (lupus antigen) is a ubiquitous RNA-binding protein found in all human cells. It is m...
AbstractThe La protein is an important component of ribonucleoprotein complexes that acts mainly as ...
Human La protein has been implicated in facilitating internal ribosome entry site (IRES)-mediated tr...
Human La protein is known to be an essential host factor for translation and replication of hepatiti...
The human La autoantigen has been shown to interact with the internal ribosome entry site (IRES) of ...
Human La autoantigen has been shown to influence internal initiation of translation of hepatitis C v...
Contains fulltext : 184508.pdf (Publisher’s version ) (Open Access)The 5'-noncodin...
Human La protein is known to interact with hepatitis C virus (HCV) internal ribosome entry site (IRE...
Human La protein has been implicated in facilitating the internal initiation of translation as well ...
The human La autoantigen has been shown to interact with the internal ribosome entry site (IRES) of ...
Human La protein has been implicated in facilitating the internal initiation of translation as well ...
Translation initiation of hepatitis C virus (HCV) RNA is the initial obligatory step of the viral li...
The human La autoantigen has been shown to interact with the internal ribosome entry site (IRES) of ...
Human La autoantigen has been shown to influence internal initiation of translation of hepatitis C v...
Human La protein is known to interact with hepatitis C virus (HCV) internal ribosome entry site (IRE...
The La protein (lupus antigen) is a ubiquitous RNA-binding protein found in all human cells. It is m...
AbstractThe La protein is an important component of ribonucleoprotein complexes that acts mainly as ...
Human La protein has been implicated in facilitating internal ribosome entry site (IRES)-mediated tr...
Human La protein is known to be an essential host factor for translation and replication of hepatiti...
The human La autoantigen has been shown to interact with the internal ribosome entry site (IRES) of ...
Human La autoantigen has been shown to influence internal initiation of translation of hepatitis C v...
Contains fulltext : 184508.pdf (Publisher’s version ) (Open Access)The 5'-noncodin...
Human La protein is known to interact with hepatitis C virus (HCV) internal ribosome entry site (IRE...
Human La protein has been implicated in facilitating the internal initiation of translation as well ...
The human La autoantigen has been shown to interact with the internal ribosome entry site (IRES) of ...
Human La protein has been implicated in facilitating the internal initiation of translation as well ...
Translation initiation of hepatitis C virus (HCV) RNA is the initial obligatory step of the viral li...
The human La autoantigen has been shown to interact with the internal ribosome entry site (IRES) of ...
Human La autoantigen has been shown to influence internal initiation of translation of hepatitis C v...
Human La protein is known to interact with hepatitis C virus (HCV) internal ribosome entry site (IRE...
The La protein (lupus antigen) is a ubiquitous RNA-binding protein found in all human cells. It is m...
AbstractThe La protein is an important component of ribonucleoprotein complexes that acts mainly as ...