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Selection of homeotic proteins for binding to a human DNA replication origin.
de Stanchina E, Gabellini D, Norio P, Giacca M, Peverali FA, Riva S, Falaschi A, Biamonti G. de Stanchina E, et al. J Mol Biol. 2000 Jun 9;299(3):667-80. doi: 10.1006/jmbi.2000.3782. J Mol Biol. 2000. PMID: 10835276
A novel hnRNP protein (HAP/SAF-B) enters a subset of hnRNP complexes and relocates in nuclear granules in response to heat shock.
Weighardt F, Cobianchi F, Cartegni L, Chiodi I, Villa A, Riva S, Biamonti G. Weighardt F, et al. J Cell Sci. 1999 May;112 ( Pt 10):1465-76. J Cell Sci. 1999. PMID: 10212141
HAP contains an RNA binding domain (RBD) flanked by a negatively charged domain and by an S/K-R/E-rich region. In in vitro pull-down assays, HAP interacts with hnRNP A1, through its S/K-R/E-rich region, and with several other hnRNPs. ...
HAP contains an RNA binding domain (RBD) flanked by a negatively charged domain and by an S/K-R/E-rich region. In in vitro pull-down …
Phosphorylation of human hnRNP protein A1 abrogates in vitro strand annealing activity.
Cobianchi F, Calvio C, Stoppini M, Buvoli M, Riva S. Cobianchi F, et al. Nucleic Acids Res. 1993 Feb 25;21(4):949-55. doi: 10.1093/nar/21.4.949. Nucleic Acids Res. 1993. PMID: 8451194 Free PMC article.
V8 phosphopeptide maps revealed that the target site(s) of in vitro phosphorylation are located in the C-terminal region of A1. ...
V8 phosphopeptide maps revealed that the target site(s) of in vitro phosphorylation are located in the C-terminal region of A1. ...
A simple procedure for enhancing PCR specificity.
Weighardt F, Biamonti G, Riva S. Weighardt F, et al. PCR Methods Appl. 1993 Aug;3(1):77-80. doi: 10.1101/gr.3.1.77. PCR Methods Appl. 1993. PMID: 8220192 No abstract available.
Two homologous genes, originated by duplication, encode the human hnRNP proteins A2 and A1.
Biamonti G, Ruggiu M, Saccone S, Della Valle G, Riva S. Biamonti G, et al. Nucleic Acids Res. 1994 Jun 11;22(11):1996-2002. doi: 10.1093/nar/22.11.1996. Nucleic Acids Res. 1994. PMID: 8029005 Free PMC article.
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