Metabolism and expression of RNA polymerase II transcripts in influenza virus-infected cells.

Por Katze, M G, Krug, R M
Publicado em 1984

Control of adenovirus early gene expression: accumulation of viral mRNA after infection of transformed cells.

Por Persson, H, Katze, M G, Philipson, L
Publicado em 1981

Purification of a native membrane-associated adenovirus tumor antigen.

Por Persson, H, Katze, M G, Philipson, L
Publicado em 1982

Control of adenovirus early gene expression: posttranscriptional control mediated by both viral and cellular gene products.

Por Katze, M G, Persson, H, Philipson, L
Publicado em 1981

A novel mRNA and a low molecular weight polypeptide encoded in the transforming region of adenovirus DNA.

Por Katze, M G, Persson, H, Philipson, L
Publicado em 1982

Degradation of the interferon-induced 68,000-M(r) protein kinase by poliovirus requires RNA.

Por Black, T L, Barber, G N, Katze, M G
Publicado em 1993

Binding of the adenovirus VAI RNA to the interferon-induced 68-kDa protein kinase correlates with function.

Por Ghadge, G D, Swaminathan, S, Katze, M G, Thimmapaya, B
Publicado em 1991

Interaction of the interferon-induced PKR protein kinase with inhibitory proteins P58IPK and vaccinia virus K3L is mediated by unique domains: implications for kinase regulation.

Por Gale, M, Tan, S L, Wambach, M, Katze, M G
Publicado em 1996

The cellular 68,000-Mr protein kinase is highly autophosphorylated and activated yet significantly degraded during poliovirus infection: implications for translational regulation.

Por Black, T L, Safer, B, Hovanessian, A, Katze, M G
Publicado em 1989

Cellular mRNA translation is blocked at both initiation and elongation after infection by influenza virus or adenovirus.

Por Katze, M G, DeCorato, D, Krug, R M
Publicado em 1986

Purification and partial characterization of a cellular inhibitor of the interferon-induced protein kinase of Mr 68,000 from influenza virus-infected cells.

Por Lee, T G, Tomita, J, Hovanessian, A G, Katze, M G
Publicado em 1990

Efficient transcription, not translation, is dependent on adenovirus tripartite leader sequences at late times of infection.

Por Alonso-Caplen, F V, Katze, M G, Krug, R M
Publicado em 1988

The 58,000-dalton cellular inhibitor of the interferon-induced double-stranded RNA-activated protein kinase (PKR) is a member of the tetratricopeptide repeat family of proteins.

Por Lee, T G, Tang, N, Thompson, S, Miller, J, Katze, M G
Publicado em 1994

Mutants of the RNA-dependent protein kinase (PKR) lacking double-stranded RNA binding domain I can act as transdominant inhibitors and induce malignant transformation.

Por Barber, G N, Wambach, M, Thompson, S, Jagus, R, Katze, M G
Publicado em 1995

The integrity of the stem structure of human immunodeficiency virus type 1 Tat-responsive sequence of RNA is required for interaction with the interferon-induced 68,000-Mr protein...

Por Roy, S, Agy, M, Hovanessian, A G, Sonenberg, N, Katze, M G
Publicado em 1991

An adenovirus agnogene.

Por Virtanen, A, Aleström, P, Persson, H, Katze, M G, Pettersson, U
Publicado em 1982

Translational control by influenza virus: suppression of the kinase that phosphorylates the alpha subunit of initiation factor eIF-2 and selective translation of influenza viral mR...

Por Katze, M G, Detjen, B M, Safer, B, Krug, R M
Publicado em 1986

The three influenza virus polymerase (P) proteins not associated with viral nucleocapsids in the infected cell are in the form of a complex.

Por Detjen, B M, St Angelo, C, Katze, M G, Krug, R M
Publicado em 1987

Influenza virus regulates protein synthesis during infection by repressing autophosphorylation and activity of the cellular 68,000-Mr protein kinase.

Por Katze, M G, Tomita, J, Black, T, Krug, R M, Safer, B, Hovanessian, A
Publicado em 1988

Adenovirus VAI RNA complexes with the 68 000 Mr protein kinase to regulate its autophosphorylation and activity.

Por Katze, M G, DeCorato, D, Safer, B, Galabru, J, Hovanessian, A G
Publicado em 1987