ribosomal

Entry of a new ribosomal complex at Met701 seems a more likely explanation.

The ribosomal phosphoprotein P0 also seems to be involved in the invasion process.

They examined the 18S ribosomal gene in the same 45 pairs of plants.

The fold of this family is similar to that found in ribosomal protein S5 domain 2-like.

The 74 ribosomal protein transcripts identified here thus account for no more than 0.33% of this total.

As the name suggests, its target substrate is the S6 ribosomal protein.

Told me that my own ribosomal structure might hold the solution to helping the Vulcans.

See nuclear import for more about the movement of the ribosomal proteins into the nucleus.

It is found within intron 2 of the L21 ribosomal protein gene.

Ribosomal protein S2 has been previously cloned from rat (3).

Many ribosomal protein L23a pseudogenes are scattered through the human genome.

Many other ribosomal protein genes exist as multigene families (3, 6).

The protein belongs to the S10E family of ribosomal proteins.

They are both encoded in the introns of the ribosomal protein S3.

More surprisingly, this list also includes translation initiation factors and several ribosomal proteins.

The ribosomal complexes are allowed to bind to surface-immobilized target.

Historically, different nomenclatures have been used for ribosomal proteins.

Contacts across the two ribosomal subunits are known as intersubunit bridges.

In mammalian cells, ribosomal proteins accounts for up to 12% of the total cellular protein.

The peptide families in this section are all ribosomal peptides, usually with hormonal activity.

Ribosomes and ribosomal subunits are found in these bodies.

They have also been found to act as promoters of programmed ribosomal frameshifting during translation.

The assembled ribosomal subunits are the largest structures passed through the nuclear pores.

The ribosomal subunits of prokaryotes and eukaryotes are quite similar.

Human ribosomal protein L5 contains defined nuclear localization and export signals.