• English
    • Ελληνικά
  • English 
    • English
    • Ελληνικά
  • Login
Browsing by Subject 
  •   Home
  • Browsing by Subject
  •   Home
  • Browsing by Subject
JavaScript is disabled for your browser. Some features of this site may not work without it.

Browsing by Subject "Peptide Mapping"

  • 0-9
  • Α
  • Β
  • Γ
  • Δ
  • Ε
  • Ζ
  • Η
  • Θ
  • Ι
  • Κ
  • Λ
  • Μ
  • Ν
  • Ξ
  • Ο
  • Π
  • Ρ
  • Σ
  • Τ
  • Υ
  • Φ
  • Χ
  • Ψ
  • Ω
  • A
  • B
  • C
  • D
  • E
  • F
  • G
  • H
  • I
  • J
  • K
  • L
  • M
  • N
  • O
  • P
  • Q
  • R
  • S
  • T
  • U
  • V
  • W
  • X
  • Y
  • Z

Sort by:

Order:

Results:

Now showing items 1-3 of 3

  • title
  • submit date
  • accessioned date
  • ascending
  • descending
  • 5
  • 10
  • 20
  • 40
  • 60
  • 80
  • 100
    • Article  

      Attenuation of drug-stimulated topoisomerase II-DNA cleavable complex formation in wild-type HL-60 cells treated with an intracellular calcium buffer is correlated with decreased cytotoxicity and site-specific hypophosphorylation of topoisomerase IIα 

      Aoyama, M.; Grabowski, D. R.; Dubyak, G. R.; Constantinou, Andreas I.; Rybicki, L. A.; Bukowski, R. M.; Ganapathi, M. K.; Hickson, I. D.; Ganapathi, R. (1998)
      Topoisomerase II (topo II), an essential enzyme for cell viability, is also the target for clinically important anti-neoplastic agents that stimulate topo II-mediated DNA scission. The role of alterations in topo IIα ...

    • Article  

      A lethal variant of osteogenesis imperfecta has a single base mutation that substitutes cysteine for glycine 904 of the α1(I) chain of type I procollagen. The asymptomatic mother has an unidentified mutation producing an overmodified and unstable type I procollagen 

      Constantinou-Deltas, Constantinos D.; Nielsen, K. B.; Prockop, D. J. (1989)
      A fraction of the proα1(I) and proα2(I) chains in type I procollagen synthesized by the fibroblasts from a proband with a lethal variant of osteogenesis imperfecta were overmodified by posttranslational reactions. After ...

    • Article  

      The substitution of arginine for glycine 85 of the α1(I) procollagen chain results in mild osteogenesis imperfecta. The mutation provides direct evidence for three discrete domains of cooperative melting of intact type I collagen 

      Deak, S. B.; Scholz, P. M.; Amenta, P. S.; Constantinou-Deltas, Constantinos D.; Levi-Minzi, S. A.; Gonzalez-Lavin, L.; Mackenzie, J. W. (1991)
      We report a case of mild osteogenesis imperfecta in a 56-year-old male undergoing aortic valve replacement surgery. The primary defect in this patient was the substitution of arginine for glycine 85 in one of the two chains ...

      Browse

      EverywhereCommunities & CollectionsBy Submission DateAuthorsTitlesSubjectsBy TypeBy DepartmentBy Faculty

      My Account

      Login
      Πνευματικά δικαιώματα ©  Βιβλιοθήκη Πανεπιστημίου Κύπρου
      Contact Us | Send Feedback
      Οδηγίες κατάθεσης διδακτορικής διατριβής
      Open Access
      ORCiD