Zobrazeno 1 - 10
of 31
pro vyhledávání: '"L. K. Steinrauf"'
Publikováno v:
The Journal of Immunology. 145:2718-2724
A set of high affinity antidigoxin antibodies were previously identified with high homologous V kappa 1A L chain sequences but were associated with two entirely different VH regions and two dramatically different specificities for digoxin analogs. An
Publikováno v:
Archives of biochemistry and biophysics. 319(1)
Glycogenin, the proposed initiator of mammalian glycogen biosynthesis, transfers glucose residues from UDP-glucose to an oligosaccharide chain attached to Tyr-194 in a self-glucosylation reaction. Mutation of Tyr-194 to either Phe or Thr residues res
Publikováno v:
The Journal of biological chemistry. 268(4)
The structure of the Ala-109--Thr mutation of human transthyretin, a nonamyloidogenic variant with enhanced thyroxine binding, has been determined by x-ray diffraction to a resolution of 1.7 A. The model, including 175 solvent water molecules, has be
Autor:
J A, Hamilton, L K, Steinrauf, B C, Braden, J, Liepnieks, M D, Benson, G, Holmgren, O, Sandgren, L, Steen
Publikováno v:
The Journal of biological chemistry. 268(4)
The x-ray crystal structures of normal human transthyretin (prealbumin) and the amyloidogenic Val-30-Met variant have been refined at 1.7-A resolution to R-values of 0.168 and 0.179, respectively, for 19,882 and 20,362 reflections (Fobs2.0 sigma). St
Autor:
N W, Hudson, R E, Bruccoleri, L K, Steinrauf, J A, Hamilton, M, Mudgett-Hunter, M N, Margolies
Publikováno v:
Journal of immunology (Baltimore, Md. : 1950). 145(8)
A set of high affinity antidigoxin antibodies were previously identified with high homologous V kappa 1A L chain sequences but were associated with two entirely different VH regions and two dramatically different specificities for digoxin analogs. An
Publikováno v:
Journal of the American Chemical Society. 103:5880-5885
Autor:
Kirsten Folting, L. K. Steinrauf
Publikováno v:
Israel Journal of Chemistry. 24:290-296
The structure by X-ray crystallography of the valinomycin–cesium picrate complex has been determined by the heavy atom method. The crystal class was trigonal, space group P31, with unit cell dimensions a = b = 14.028(4) â, 31.888(10) Ǎ, Z = 3, fi
Autor:
L. K. Steinrauf
Publikováno v:
Journal of Biosciences. 8:293-306
A total of 19 different crystal forms of complexes of valinomycin or its analogues with monovalent cations have been observed. The crystal structure determinations of valinomycin potassium tetrachloroaurate and valinomycin rubidium tetrachloroaurate
Autor:
M. O. Chaney, L. K. Steinrauf
Publikováno v:
Acta Crystallographica Section B Structural Crystallography and Crystal Chemistry. 30:711-716
Publikováno v:
Acta Crystallographica Section B Structural Crystallography and Crystal Chemistry. 36:1052-1057