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Multisite phosphorylation of a synthetic peptide derived from the carboxyl terminus of the ribosomal protein S6 (open access)

Multisite phosphorylation of a synthetic peptide derived from the carboxyl terminus of the ribosomal protein S6

Article synthesizing and testing the synthetic peptide AKRRRLSSLRASTSKSESSQK (56-21) which corresponds to the carboxyl-terminal 21 amino acids of human ribosomal protein S6 as a substrate for S6/H4 kinase purified from human placenta. The data suggests that multiple S6 kinases may be required to phosphorylate S6 at all five sites which are modified in vivo.
Date: January 5, 1991
Creator: Brandon, Stanley D. & Masaracchia, Ruthann A.
System: The UNT Digital Library
Activation of an S6/H4 Kinase (PAK 65) from Human Placenta by Intramolecular and Intermolecular Autophosphorylation (open access)

Activation of an S6/H4 Kinase (PAK 65) from Human Placenta by Intramolecular and Intermolecular Autophosphorylation

Article proposing a model in which phosphorylation of sites 1 and 2 occurs sequentially. The model proposes that trypsin treatment of the inactive holoenzyme removes an inhibitory rac-binding domain which blocks MgATP access to the catalytic site. The pseudosubstrate domain at site 1 is autophosphorylated and subsequent bimolecular autophosphorylation at site 2 fully opens the catalytic site.
Date: September 8, 1995
Creator: Benner, Gretchen E.; Dennis, Patrick B. & Masaracchia, Ruthann A.
System: The UNT Digital Library
Molecular cloning and characterization of a gene encoding pea cytosolic ascorbate peroxidase (open access)

Molecular cloning and characterization of a gene encoding pea cytosolic ascorbate peroxidase

Article isolating a gene encoding cytosolic bate peroxidase (ApxI) from pea (Pisum sativum L.) and determining its nucleotide sequence.
Date: October 25, 1992
Creator: Mittler, Ron & Zilinskas, B.A.
System: The UNT Digital Library
Activation of an S6 Kinase From Human Placenta by Autophosphorylation (open access)

Activation of an S6 Kinase From Human Placenta by Autophosphorylation

Article describing a novel S6 kinase isolated from human placenta which autoactivates through autophosphorylation in vitro. The data supports the hypothesis that this previously uncharacterized S6 kinase belongs to a unique family of protein kinases which utilize autophosphorylation as part of their in vivo activation mechanism.
Date: September 15, 1993
Creator: Dennis, Patrick B. & Masaracchia, Ruthann A.
System: The UNT Digital Library