scholarly article | Q13442814 |
P356 | DOI | 10.1016/S0022-2836(02)00645-9 |
P698 | PubMed publication ID | 12162954 |
P2093 | author name string | Nathalie Mathy | |
Dominique Bréchemier-Baey | |||
Claude Portier | |||
Ophélie Duché | |||
Anne Jarrige | |||
P2860 | cites work | Localized Bicaudal-C RNA encodes a protein containing a KH domain, the RNA binding motif of FMR1. | Q37696957 |
Kinetics of Polymerization and Phosphorolysis Reactions of E. coli Polynucleotide Phosphorylase. Role of Oligonucleotides in Polymerization | Q38362986 | ||
Increased expression of Escherichia coli polynucleotide phosphorylase at low temperatures is linked to a decrease in the efficiency of autocontrol | Q39503894 | ||
In vitro genetic analysis of the RNA binding site of vigilin, a multi-KH-domain protein | Q39575228 | ||
Guanosine pentaphosphate synthetase from Streptomyces antibioticus is also a polynucleotide phosphorylase | Q39842042 | ||
Low copy number plasmids for regulated low-level expression of cloned genes in Escherichia coli with blue/white insert screening capability | Q40519280 | ||
A point mutation in the FMR-1 gene associated with fragile X mental retardation | Q41579799 | ||
Isolation of a polynucleotide phosphorylase mutant using a kanamycin resistant determinant | Q44087137 | ||
Kinetics of Polymerization and Phosphorolysis Reactions of Escherichia coli Polynucleotide Phosphorylase. Evidence for Multiple Binding of Polynucleotide in Phosphorolysis | Q47767974 | ||
Quaternary Structure of Polynucleotide Phosphorylase from Escherichia coli: Evidence of a Complex between Two Types of Polypeptide Chains | Q52872640 | ||
Electron microscopy of Escherichia coli polynucleotide phosphorylase molecules and polyribonucleotide formation | Q53692775 | ||
[Kinetics of reactions catalyzed by Escherichia coli polynucleotide phosphorylase. 2-deoxy-ADP as substrate and inhibitor]. | Q53790760 | ||
Copurification of E. coli RNAase E and PNPase: evidence for a specific association between two enzymes important in RNA processing and degradation. | Q54637941 | ||
A novel mutation in the KH domain of polynucleotide phosphorylase affects autoregulation and mRNA decay in Escherichia coli | Q57732836 | ||
Quaternary structure ofEscherichia colipolynucleotide phosphorylase: new evidence for a trimeric structure | Q66891610 | ||
Essential role for KH domains in RNA binding: impaired RNA binding by a mutation in the KH domain of FMR1 that causes fragile X syndrome | Q24310518 | ||
Polynucleotide phosphorylase functions as both an exonuclease and a poly(A) polymerase in spinach chloroplasts | Q24550883 | ||
KH domain: one motif, two folds | Q24625767 | ||
A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation | Q27628410 | ||
The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold | Q27734665 | ||
Rapid and efficient site-specific mutagenesis without phenotypic selection | Q27860608 | ||
The protein product of the fragile X gene, FMR1, has characteristics of an RNA-binding protein | Q28117885 | ||
The first step in the functional inactivation of the Escherichia coli polynucleotide phosphorylase messenger is a ribonuclease III processing at the 5' end. | Q33929386 | ||
PNPase autocontrols its expression by degrading a double-stranded structure in the pnp mRNA leader | Q34103527 | ||
RNA degradosomes exist in vivo in Escherichia coli as multicomponent complexes associated with the cytoplasmic membrane via the N-terminal region of ribonuclease E. | Q34583159 | ||
Polynucleotide phosphorylase functions both as a 3' right-arrow 5' exonuclease and a poly(A) polymerase in Escherichia coli | Q35358676 | ||
Polynucleotide phosphorylase of Escherichia coli induces the degradation of its RNase III processed messenger by preventing its translation | Q37585931 | ||
P433 | issue | 3 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | mutational analysis | Q1955810 |
Escherichia coli | Q25419 | ||
P304 | page(s) | 397-409 | |
P577 | publication date | 2002-08-01 | |
P1433 | published in | Journal of Molecular Biology | Q925779 |
P1476 | title | Mutational analysis of polynucleotide phosphorylase from Escherichia coli. | |
P478 | volume | 321 |
Q50165023 | "A high-throughput and rapid computational method for screening of RNA post-transcriptional modifications that can be recognized by target proteins". |
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