The eIF4E-binding protein 1 (4EBP1) has long been known to be completely unstructured without any secondary structures, which contributed significantly to the proposal of the induced fit mechanism for target binding of intrinsically disordered proteins. We show here that 4EBP1 is not completely unstructured, but contains a pre-structured helix
SummaryCap-dependent translation initiation is regulated by the interaction of eukaryotic initiation...
Stapled-peptides have emerged as an exciting class of molecules which can modulate protein–protein i...
The dimeric beta-barrel is a characteristic topology initially found in the transcriptional regulato...
The eIF4E-binding protein 1 (4EBP1) has long been known to be completely unstructured without any se...
The molecular mechanism underpinning regulation of eukaryotic translation initiation factor eIF4E by...
Eukaryotic initiation factor-4E (eIF4E) controls the rate of cap-dependent translation initiation an...
Proteins containing intrinsic disorder often form secondary structure upon interaction with a bindin...
AbstractAlthough the α-helical Y(X)4Lϕ containing region of eIF4E-binding protein (4EBP) is the majo...
Protein disorder plays a crucial role in signal transduction and is key for many cellular processes ...
The Epstein-Barr nuclear antigen 1 (EBNA1) is essential for DNA replication and episome segregation ...
eIF4E binding protein (4E-BP) inhibits translation of capped mRNA by binding to the initiation facto...
The eIF4E-binding proteins (4E-BPs) represent a diverse class of translation inhibitors that are oft...
<p><b>(A)</b> The complex between the TAZ1 domain of the transcriptional coactivator CREB-binding pr...
The central role of eukaryotic translation initiation factor 4E (eIF4E) in controlling mRNA translat...
The control of mRNA translation is a complex process that is critical for gene expression during dev...
SummaryCap-dependent translation initiation is regulated by the interaction of eukaryotic initiation...
Stapled-peptides have emerged as an exciting class of molecules which can modulate protein–protein i...
The dimeric beta-barrel is a characteristic topology initially found in the transcriptional regulato...
The eIF4E-binding protein 1 (4EBP1) has long been known to be completely unstructured without any se...
The molecular mechanism underpinning regulation of eukaryotic translation initiation factor eIF4E by...
Eukaryotic initiation factor-4E (eIF4E) controls the rate of cap-dependent translation initiation an...
Proteins containing intrinsic disorder often form secondary structure upon interaction with a bindin...
AbstractAlthough the α-helical Y(X)4Lϕ containing region of eIF4E-binding protein (4EBP) is the majo...
Protein disorder plays a crucial role in signal transduction and is key for many cellular processes ...
The Epstein-Barr nuclear antigen 1 (EBNA1) is essential for DNA replication and episome segregation ...
eIF4E binding protein (4E-BP) inhibits translation of capped mRNA by binding to the initiation facto...
The eIF4E-binding proteins (4E-BPs) represent a diverse class of translation inhibitors that are oft...
<p><b>(A)</b> The complex between the TAZ1 domain of the transcriptional coactivator CREB-binding pr...
The central role of eukaryotic translation initiation factor 4E (eIF4E) in controlling mRNA translat...
The control of mRNA translation is a complex process that is critical for gene expression during dev...
SummaryCap-dependent translation initiation is regulated by the interaction of eukaryotic initiation...
Stapled-peptides have emerged as an exciting class of molecules which can modulate protein–protein i...
The dimeric beta-barrel is a characteristic topology initially found in the transcriptional regulato...