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L V Medved

Showing results (11-20 of 40) with videos related to

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The Journal of Biological Chemistry|July 15, 1991
Domain structure and domain-domain interactions of recombinant tissue plasminogen activatorV V Novokhatny, K C Ingham, L V Medved
Ukrainskii Biokhimicheskii Zhurnal (1978)|July 1, 1996
Domain structure and interactions of plasminogen activatorsL V Medved, V V Novokhatny, K C Ingham
FEBS Letters|July 7, 1986
Domain organization of the terminal parts in the fibrinogen moleculeL V Medved', S V Litvinovich, P L Privalov
Biochemistry|June 27, 1989
Calorimetric investigation of the domain structure of human complement Cl-s: reversible unfolding of the short consensus repeat unitsL V Medved, T F Busby, K C Ingham
The Journal of Biological Chemistry|November 10, 1995
Localization of factor IXa and factor VIIIa interactive sitesL M O'Brien, L V Medved, P J Fay
Molekuliarnaia Biologiia|November 1, 1982
[Isolation and investigation of structural organization of active and inactive forms of fibrinogen D-fragment molecule]L V Medved', V V Novokhatnyĭ, P L Privalov
FEBS Letters|September 20, 1982
Isolation of thermostable structure from the fibrinogen D fragmentL V Medved', P L Privalov, T P Ugarova
The Journal of Biological Chemistry|August 15, 1993
Effect of tethered peptidylchloromethylketone inhibitors on thermal stability and domain interactions of urokinase and other serine proteasesV V Novokhatny, L V Medved, A Mazar, et al.
The Journal of Biological Chemistry|April 1, 1994
The NH2-terminal fibrin-binding site of fibronectin is formed by interacting fourth and fifth finger domains. Studies with recombinant finger fragments expressed in Escherichia coliY V Matsuka, L V Medved, S A Brew, et al.
Journal of Molecular Biology|February 5, 1991
Domain structure and interactions of the type I and type II modules in the gelatin-binding region of fibronectin. All six modules are independently foldedS V Litvinovich, D K Strickland, L V Medved, et al.
Pageof 4

Showing results (11-20 of 40) with videos related to

Sort By:
Pageof 4
The Journal of Biological Chemistry|July 15, 1991
Domain structure and domain-domain interactions of recombinant tissue plasminogen activatorV V Novokhatny, K C Ingham, L V Medved
Ukrainskii Biokhimicheskii Zhurnal (1978)|July 1, 1996
Domain structure and interactions of plasminogen activatorsL V Medved, V V Novokhatny, K C Ingham
FEBS Letters|July 7, 1986
Domain organization of the terminal parts in the fibrinogen moleculeL V Medved', S V Litvinovich, P L Privalov
Biochemistry|June 27, 1989
Calorimetric investigation of the domain structure of human complement Cl-s: reversible unfolding of the short consensus repeat unitsL V Medved, T F Busby, K C Ingham
The Journal of Biological Chemistry|November 10, 1995
Localization of factor IXa and factor VIIIa interactive sitesL M O'Brien, L V Medved, P J Fay
Molekuliarnaia Biologiia|November 1, 1982
[Isolation and investigation of structural organization of active and inactive forms of fibrinogen D-fragment molecule]L V Medved', V V Novokhatnyĭ, P L Privalov
FEBS Letters|September 20, 1982
Isolation of thermostable structure from the fibrinogen D fragmentL V Medved', P L Privalov, T P Ugarova
The Journal of Biological Chemistry|August 15, 1993
Effect of tethered peptidylchloromethylketone inhibitors on thermal stability and domain interactions of urokinase and other serine proteasesV V Novokhatny, L V Medved, A Mazar, et al.
The Journal of Biological Chemistry|April 1, 1994
The NH2-terminal fibrin-binding site of fibronectin is formed by interacting fourth and fifth finger domains. Studies with recombinant finger fragments expressed in Escherichia coliY V Matsuka, L V Medved, S A Brew, et al.
Journal of Molecular Biology|February 5, 1991
Domain structure and interactions of the type I and type II modules in the gelatin-binding region of fibronectin. All six modules are independently foldedS V Litvinovich, D K Strickland, L V Medved, et al.
Pageof 4