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Query: UNIPROT:P06889 (
Mol
)
630,302
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Disulphide-rich proteins of widely differing functions were aligned with the aid of their half-cystinyl residues. This led to the grouping of
ribonuclease
, phospholipase A, lysozyme, snake venom toxins, bee and scorpion venom peptides, and the plant proteins potatoe carboxypeptidase inhibitor, ragweed pollen allergen, mistletoe toxins and pineapple sulfhydryl protease inhibitor into one super-family of proteins. Very few deletions/insertions were needed to effect alignment and probabilities were calculated for random occurrence of the matches that were found.
J
Mol
Evol 1977 Aug 05
PMID:Homology of functionally diverse proteins. 89 36
In terms of the mechanical model of molecules, a calculation has been carried out of possible positions and binding energies of 1-methyl uracyl in the contact region of the
ribonuclease
S active site. In the most preferential orientation, 1-methyl uracyl forms hydrogen bonds C(2)=O(uracyl)...H-N(Thr-45), N-H...Ogamma (Thr-45), C(4)=O... ...H-Ogamma (Ser-123). The base position found (atom coordinates are given) is in complete qualitative agreement with the position of the uracyl in UpcA bound to
ribonuclease
S as revealed by X-ray analysis. The influence studied of methyl substitution in positions 3 and 5 of the pyrimidine cycle on the base orientation within the protein field. It has been shown that the formation of hydrogen bonds with Thr-45 and Ser-123 is not prerequisite for productive fixation of the phosphoribosyl nucleotide moiety in the catalytic region of the enzyme active site.
Mol
Biol (Mosk)
PMID:[A theoretical analysis of the binding of methyl derivatives of uracil at the contact portion of the active center of ribonuclease S]. 94 May 57
The quantitative changes of double-stranded RNA components of nuclear ribonucleo-protein particles containing pre-mRNA was investigated in the course of incubation of particles at 37 degrees C. The incubation of purified nuclear particles revealed the fragmentation of long double-stranded RNA sequences into shorter stretches. The presence of nuclear sap in the incubation mixture resulted in degradation of the double-stranded RNAs into acid soluble products. Autodegradation and/or
ribonuclease
treatment of nuclear RNP particles is accompanied by quantitative changes in the minor protein constituents of informofer.
Mol
Biol Rep 1976 Nov
PMID:Autodegradation of pre-mRNA containing nuclear ribo-nucleoprotein particles. The effect of autodegradation on the double-stranded RNA sequences and on the protein composition of particles. 101 80
After the annealing of pre-mRNA at high Cot values, up to 20% of the material becomes resistant to the action of
ribonuclease
. This has been attributed to the presence of self-complementary sequences (scRNA) in the pre-mRNA. The most important properties of scRNA, which was isolated in preparative amounts, have been studied. The approximate dimensions of the complementary segments are 45-50 nucleotides. Hybridization experiments have shown that scRNA is transcribed from repeated segments of the genome. It may be postulated that the rapidly hybridizing pre-mRNA fraction consists mainly of self-complementary sequences.
Mol
Biol (Mosk)
PMID:Structure of nuclear pre-mRNA. VIII. Isolation and characterization of complementary sequences. 102 53
Variation of
ribonuclease
S structure is analysed with the potential energy being minimized by a computer. The function of potential energy contains the potentials of bond and angle distortions, torsional and non-valent interactions. It is shown that after 100 iterations the potential energy is decreased from the value of 6500 kcal/mole to--1012 kcal/mole, 92% of complete change of energy fitting the first ten iterations. The root mean square deviation (r. ms. d.) of final structure from the initial one is 0.232 A (0.206 A for the backbone and 0.257 A for side groups). The forbidden non-valent contacts are completely removed after minimization. R. ms. d. of the equilibrium value is decreased from 0.097 to 0.006 A for bond lengths; from 7.660 to 3.65 degrees for valence an-les and from 9.44 to 6.95 degrees for rotation angles around the peptide bonds. Distribution of tensions along the protein chain after minimization is considerably changed, the tensions decreasing in average by 100 times.
Mol
Biol (Mosk)
PMID:[Theoretic analysis of conformation of proteins. I. Minimization of potential energy of ribonuclease S]. 105 89
In a mutant strain defective in polynucleotide phosphorylase, under conditions where the enzyme becomes limiting, it is possible to demonstrate that chemical as well as functional half lives of mRNA become longer if the strain is also missing
ribonuclease II
. These results allow to unify in a simple model a variety of observations about turnover of RNA in a variety of bacteria.
Mol
Gen Genet 1975 Sep 08
PMID:Polynucleotide phosphorylase can participate in decay of mRNA in Escherichia coli in the absence of ribonuclease II. 110 47
Yersinia pestis has been characterized in terms of fingerprints of digests (pancreatic and/or T1
ribonuclease
) of its 16S and 5S ribosomal RNAs. These show clearly that Y. pestis is a member of the Enterobacteriaceae and suggest that within the Family it is most closely related to Serratia and/or Proteus.
J
Mol
Evol 1975 Mar 24
PMID:The phylogenetic status of Pasteurella pestis. 110 66
Nuclei of MPC 11 mouse myeloma cells contain several species of small RNAs related to those found in other mammalian cells. These include U1 RNA, about 190 nucleotides in length and U2 RNA, about 170 nucleotides long. The 5'-termini of 32P-labelled U1 and U2 RNAs have been investigated by a fingerprinting technique involving digestion with T2-
ribonuclease
. The RNAs were found to have modified 5'-terminal structures of the form m3G(5')ppp (5')AmpUmpAp for U1 RNA and m3G(5')ppp(5')AmpUmpCmpCp for U2 RNA, where m3G is N2, N27-trimethyl guanosine and Am and Um are 2'-O-methyl nucleosides. These 5'-terminal sequences are the same as those proposed for rat hepatoma U1 and U2 RNAs (Ro-Choi et al., Fed. Proc. 33, 1548, 1974) but with triphosphate rather than diphosphate links.
Mol
Biol Rep 1975 Dec
PMID:Modified 5'-termini in small nuclear RNAs of mouse myeloma cells. 121 81
The theory of melting of DNA complexes with extended ligands (ties) is considered. Influence of ties interacting electorally with certain DNA regions and influence of extender ties, interacting unelectorally on the helix coil transition parameters is compared. It has been shown that both types of ties cause, coincided qualitatively, but differed quantatively, shifts of melting temperature and change of the melting range width of DNA. Comparison of theory with experiment in the case of DNA complexes with
ribonuclease
is given.
Mol
Biol (Mosk)
PMID:[Fusion of complexes of DNA and extended ligands]. 122 69
The total poly(A)-containing mRNA from mouse liver or Ehrlich ascites carcinoma cells was annealed with denatured ds RNA prepared from heavy nuclear 3H-labeled pre-mRNA of the same tissue. The hybrids formed were detected by binding of complexes to poly(U)-Sepharose columns through the poly(A) of mRNA. With this technique, about 30% of labeled ds RNA was bound to poly(U)-Sepharose after annealing it with an mRNA excess. The proportion of hybrid material detected by
RNase
treatment was two to three times lower than that obtained by poly(U)-Sepharose binding. The length of the
RNase
-stable acid precipitable hybrid material consisted of heterogeneous sequences of 10-100 nucleotides long when cytoplasmic, and 10-60 nucleotides long when polysomal mRNA was used in the hybridization reaction. The results obtained show that at least some of the mRNA molecules contain sequences complementary to one of the branches of the pre-mRNA hairpins. These results are compatible with the idea that the hairpin-like sequences in pre-mRNA are localized between mRNA and the non-informative part of the precursor molecule.
Mol
Biol Rep 1976 Apr
PMID:Direct demonstration of a complementarity between mRNA and double-stranded sequences of pre-mRNA. 127 59
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