Results 1 to 10 of about 6,611 (182)

Molecular dynamics of three different α-helices in ribosomal protein L25 from Escherichia coli [PDF]

open access: goldBiochemistry and Biophysics Reports
A true native protein state is realized in a water solution where proteins exhibit their dynamic properties important for the functioning. This is way we have analyzed the dynamics of α-helices inside ribosomal protein L25 from Escherichia coli in a ...
Yuri Chirgadze   +3 more
doaj   +5 more sources

Structural and putative regulatory sequences of the gene encoding ribosomal protein L25 in Candida utilis [PDF]

open access: bronzeCurrent Genetics, 1987
Using a heterologous probe containing a fragment of the L25-gene from Saccharomyces carlsbergensis we have isolated a DNA-fragment of Candida utilis carrying the gene encoding ribosomal protein L25. This gene is present in a single copy on the C. utilis genome, though as two distinguishable alleles.
Rudi J Planta   +2 more
exaly   +4 more sources

Alteration of 5S RNA conformation by ribosomal proteins L18 and L25

open access: greenNucleic Acids Research, 1977
The effects of ribosomal proteins L18, L25 and L5 on the conformation of 5S RNA have been studied by circular dichroism and temperature dependent ultraviolet absorbance. The circular dichroism spectrum of native 5S RNA is characterized in the near ultraviolet by a large positive band at 267 nm and a small negative band at 298 nm.
Roger A Garrett   +2 more
exaly   +6 more sources

A ribonuclease-resistant region of 5S RNA and its relation to the RNA binding sites of proteins L18 and L25 [PDF]

open access: bronzeNucleic Acids Research, 1979
An RNA fragment, constituting three subfragments of nucleotide sequences 1-11, 69-87 and 89-120, is the most ribonuclease-resistant part of the native 5S RNA of Escherichia coli, at 0 degrees C. A smaller fragment of nucleotide sequence 69-87 and 90-110 is ribonuclease-resistant at 25 degrees.
Stephen Douthwaite   +2 more
exaly   +6 more sources

The cellular level of yeast ribosomal protein L25 is controlled principally by rapid degradation of excess protein [PDF]

open access: bronzeCurrent Genetics, 1986
When the gene dosage for the primary rRNA-binding ribosomal protein L25 in yeast cells was raised about 50-fold, the level of mature L25 transcripts was found to increase almost proportionally. The plasmid-derived L25 transcripts were structurally indistinguishable from their genomic counterparts, freely entered polysomes in vivo and were fully ...
H A Raue, Rudi J Planta, W H Mager
exaly   +4 more sources

A Proton NMR Study of Ribosomal Protein L25 from Escherichia coli [PDF]

open access: bronzeEuropean Journal of Biochemistry, 1981
A highly folded form of the ribosomal protein L25 from Escherichia coli can be obtained from urea-denatured preparations. Proton NMR data show that this form of the molecule must have a compact, globular tertiary structure. Spectroscopically it is indistinguishable from L25 prepared by methods which avoid denaturing solvents.
Matthew J. Kime   +3 more
openalex   +3 more sources

ERRATUM: “THE SIZES OF EARLY-TYPE GALAXIES” (2008, ApJL, 689, L25) [PDF]

open access: bronzeThe Astrophysical Journal, 2009
In the caption of Figure 3 the surface brightness limit of the model galaxies included in the figure should read: μ B < 25.5 mag arcsec–2.
Joachim Janz, T. Lisker
openalex   +3 more sources

Lymphocyte Surface Antigen L25 Is a Member of the Integrin Receptor Superfamily

open access: hybridJournal of Biological Chemistry, 1989
Monoclonal antibody (mAb) anti-L25 identifies an antigen on the surface of human lymphocytes. This mAb immunoprecipitated three distinct polypeptides of Mr 150,000, 85,000, and 75,000 from Nonidet P-40 lysates of surface radioiodinated lymphocytes. The three polypeptides were found under both nonreducing and reducing conditions.
Bradley W. McIntyre   +2 more
openalex   +3 more sources

Yrb4p, a yeast Ran–GTP‐binding protein involved in import of ribosomal protein L25 into the nucleus [PDF]

open access: greenThe EMBO Journal, 1997
Gsp1p, the essential yeast Ran homologue, is a key regulator of transport across the nuclear pore complex (NPC). We report the identification of Yrb4p, a novel Gsp1p binding protein. The 123 kDa protein was isolated from Saccharomyces cerevisiae cells and found to be related to importin-beta, the mediator of nuclear localization signal (NLS)-dependent ...
Gabriel Schlenstedt   +7 more
openalex   +5 more sources

Friction Characteristics of W100×L25 Micro Ellipse Type Pattern [PDF]

open access: bronzeJournal of the Korean Society of Tribologists and Lubrication Engineers, 2012
* Dept. of Bio Industrial Mechanical Engineering, Pusan National University*Dept. of Mechanical Engineering, Kyungpook National University(Received March 15, 2012; Revised April 30, 2012; Accepted May 3, 2012)Abstract − In this paper, we investigated the friction characteristics of W100°oL25m ellipse type surface pattern,on bearing steel.
Won‐Sik Choi   +7 more
openalex   +3 more sources

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