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1
Genetic evidence for the presence of two distinct hantaviruses associated with Apodemus mice in Croatia and analysis of local strains
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Genetic evidence for the presence of two distinct hantaviruses associated with Apodemus mice in Croatia and analysis of local strains

Plyusnina, Angelina ; Krajinović, Lidija Cvetko ; Margaletić, Josip ; Niemimaa, Jukka ; Nemirov, Kirill ; Lundkvist, Åke ; Markotić, Alemka ; Miletić‐Medved, Marica ; Avšič‐Županc, Tatjana ; Henttonen, Heikki ; Plyusnin, Alexander

Journal of medical virology, 2011-01, Vol.83 (1), p.108-114 [Periódico revisado por pares]

Hoboken: Wiley Subscription Services, Inc., A Wiley Company

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2
Factor XIIIa-Catalyzed Cross-Linking of Recombinant αC Fragments of Human Fibrinogen
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Factor XIIIa-Catalyzed Cross-Linking of Recombinant αC Fragments of Human Fibrinogen

Matsuka, Yury V ; Medved, Leonid V ; Migliorini, Mary M ; Ingham, Kenneth C

Biochemistry (Easton), 1996-05, Vol.35 (18), p.5810-5816 [Periódico revisado por pares]

United States: American Chemical Society

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3
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 coli
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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 coli

MATSUKA, V. V ; MEDVED, L. V ; BREW, S. A ; INGHAM, K. C

The Journal of biological chemistry, 1994-04, Vol.269 (13), p.9539-9546 [Periódico revisado por pares]

Bethesda, MD: American Society for Biochemistry and Molecular Biology

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4
Identification of a human CD36 isoform produced by exon skipping. Conservation of exon organization and pre-mRNA splicing patterns with a CD36 gene family member, CLA-1
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Identification of a human CD36 isoform produced by exon skipping. Conservation of exon organization and pre-mRNA splicing patterns with a CD36 gene family member, CLA-1

YANLIN TANG ; TAYLOR, K. T ; SOBIESKI, D. A ; MEDVED, E. S ; LIPSKY, R. H

The Journal of biological chemistry, 1994-02, Vol.269 (8), p.6011-6015 [Periódico revisado por pares]

Bethesda, MD: American Society for Biochemistry and Molecular Biology

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5
Domain structure and interactions of the type I and type II modules in the gelatin-binding region of fibronectin: All six modules are independently folded
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Domain structure and interactions of the type I and type II modules in the gelatin-binding region of fibronectin: All six modules are independently folded

Litvinovich, Sergei V. ; Strickland, Dudley K. ; Medved', Leonid V. ; Ingham, Kenneth C.

Journal of molecular biology, 1991-02, Vol.217 (3), p.563-575 [Periódico revisado por pares]

Oxford: Elsevier Ltd

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6
Effect of tethered peptidylchloromethylketone inhibitors on thermal stability and domain interactions of urokinase and other serine proteases
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Effect of tethered peptidylchloromethylketone inhibitors on thermal stability and domain interactions of urokinase and other serine proteases

NOVOKHATNY, V. V ; MEDVED, L. V ; MAZAR, A ; INGHAM, K. C

The Journal of biological chemistry, 1993-08, Vol.268 (23), p.17211-17218 [Periódico revisado por pares]

Bethesda, MD: American Society for Biochemistry and Molecular Biology

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7
Multiple binding sites in fibrinogen for integrin alphaMbeta2 (Mac-1)
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Multiple binding sites in fibrinogen for integrin alphaMbeta2 (Mac-1)

Lishko, Valeryi K ; Podolnikova, Nataly P ; Yakubenko, Valentin P ; Yakovlev, Sergiy ; Medved, Leonid ; Yadav, Satya P ; Ugarova, Tatiana P

The Journal of biological chemistry, 2004-10, Vol.279 (43), p.44897 [Periódico revisado por pares]

United States

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8
Domain structure and interactions of recombinant urokinase-type plasminogen activator
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Domain structure and interactions of recombinant urokinase-type plasminogen activator

NOVOKHATNY ; MEDVED, L ; MAZAR, A ; MARCOTTE, P ; HENKIN, J ; INGHAM, K

The Journal of biological chemistry, 1992-02, Vol.267 (6), p.3878-3885 [Periódico revisado por pares]

BETHESDA: American Society for Biochemistry and Molecular Biology

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9
Tissue-type plasminogen activator (tPA) interacts with urokinase-type plasminogen activator (uPA) via tPA's lysine binding site. An explanation of the poor fibrin affinity of recombinant tPA/uPA chimeric molecules
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Tissue-type plasminogen activator (tPA) interacts with urokinase-type plasminogen activator (uPA) via tPA's lysine binding site. An explanation of the poor fibrin affinity of recombinant tPA/uPA chimeric molecules

Novokhatny, V ; Medved, L ; Lijnen, H R ; Ingham, K

The Journal of biological chemistry, 1995-04, Vol.270 (15), p.8680 [Periódico revisado por pares]

United States

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10
Nonclottable fibrin obtained from partially reduced fibrinogen: characterization and tissue plasminogen activator stimulation
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Nonclottable fibrin obtained from partially reduced fibrinogen: characterization and tissue plasminogen activator stimulation

Procyk, Roman ; Medved, L. V ; Engelke, Kory J ; Kudryk, Bohdan ; Blombaeck, Birger

Biochemistry (Easton), 1992-03, Vol.31 (8), p.2273-2278 [Periódico revisado por pares]

WASHINGTON: American Chemical Society

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