Search Results - "Petrosian, S A"

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  1. 1

    Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA by PETROSIAN, SUSAN A., MAKHATADZE, GEORGE I.

    Published in Protein science (01-02-2000)
    “…The stability of protein is defined not only by the hydrogen bonding, hydrophobic effect, van der Waals interactions, and salt bridges. Additional, much more…”
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    Journal Article
  2. 2

    Mutagenesis Disrupts Posttranslational Processing of the Na,K-ATPase Catalytic Subunit by Petrosian, Susan A., Carr, Deborah L., Guerrero, Georgina, Pressley, Thomas A.

    Published in Archives of biochemistry and biophysics (15-09-1998)
    “…The first 5 amino acids of the catalytic α1 isoform from Na,K-ATPase are cleaved enzymatically during or after translation. To evaluate the structural…”
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    ES-IPO-97 treatment protocol for prognostically poor Ewing's sarcoma forms in children: results of implementation by Ptushkina, E A, Ivanova, N M, Dolgopolov, I S, Izhogin, D G, Petrosian, A S, Glekov, I V, Durnov, L A, Mentkevich, G L

    “…The paper shows the high efficiency and moderate toxicity of inductive treatment in children with Young sarcoma and primitive neuroectodermal tumors by…”
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    Journal Article
  6. 6

    Acidic copper-containing proteins--an intermediate link to the electron transfer stage from cytochrome b-561 to dopamine-beta-monooxygenase by Oganesian, L L, Boiadzhian, A S, Petrosian, S A, Karagezian, K G

    Published in Molekuliarnaia biologiia (01-01-1991)
    “…The interaction of acidic copper-containing protein from the membranes of chromaffin granules has been investigated with cytochrome b-561 and…”
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  7. 7

    Purification of cytochrome B-561 from chromaffin granules and its physico-chemical properties by Petrosian, S A, Boiadzhian, A S, Karagezian, K G

    Published in Ukrainskij biohimičeskij žurnal (01-03-1991)
    “…A soft method of purification of cytochrome-561 from the membranes of chromaffin granules has been developed. It permits isolating a protein in its natural…”
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    Journal Article
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