(Q24313453)

RNA ligands selected by cleavage stimulation factor contain distinct sequence motifs that function as downstream elements in 3'-end processing of pre-mRNA.

GOA release 2020-03-11

author name string

U Rüegsegger

series ordinal

1

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D Blank

series ordinal

2

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W Keller

series ordinal

3

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language of work or name

English

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publication date

January 1998

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published in

Molecular Cell

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volume

1

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issue

2

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page(s)

243-53

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cites work

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Conserved structures and diversity of functions of RNA-binding proteins

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cDNA cloning and characterization of the protein encoded by RD, a gene located in the class III region of the human major histocompatibility complex

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7 January 2021

3' cleavage and polyadenylation of mRNA precursors in vitro requires a poly(A) polymerase, a cleavage factor, and a snRNP

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Specific commitment of different pre-mRNAs to splicing by single SR proteins

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An ordered pathway of assembly of components required for polyadenylation site recognition and processing.

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RNA structure is a critical determinant of poly(A) site recognition by cleavage and polyadenylation specificity factor

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Restoration of both structure and function to a defective poly(A) site by in vitro selection

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Protein-protein interactions and 5'-splice-site recognition in mammalian mRNA precursors

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The 64-kilodalton subunit of the CstF polyadenylation factor binds to pre-mRNAs downstream of the cleavage site and influences cleavage site location

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A conserved epitope on a subset of SR proteins defines a larger family of Pre-mRNA splicing factors

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Polar zippers: their role in human disease

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A multisubunit 3' end processing factor from yeast containing poly(A) polymerase and homologues of the subunits of mammalian cleavage and polyadenylation specificity factor

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Purification and characterization of human cleavage factor Im involved in the 3' end processing of messenger RNA precursors

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The human U1-70K snRNP protein: cDNA cloning, chromosomal localization, expression, alternative splicing and RNA-binding

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Characterization of a novel protein-binding module--the WW domain

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The human RD protein is closely related to nuclear RNA-binding proteins and has been highly conserved

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Separation and characterization of a poly(A) polymerase and a cleavage/specificity factor required for pre-mRNA polyadenylation

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Four factors are required for 3'-end cleavage of pre-mRNAs

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The human 64-kDa polyadenylylation factor contains a ribonucleoprotein-type RNA binding domain and unusual auxiliary motifs

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Interaction of U2AF65 RS region with pre-mRNA branch point and promotion of base pairing with U2 snRNA [corrected]

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A novel poly(A)-binding protein acts as a specificity factor in the second phase of messenger RNA polyadenylation

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Poly(A) site efficiency reflects the stability of complex formation involving the downstream element

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SR proteins: a conserved family of pre-mRNA splicing factors

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