Výsledky vyhledávání - "H.A.A.M. van Teeffelen"

Islet amyloid polypeptide: structure and upstream sequences of the IAPP gene in rat and man

Autor: J. Zandberg, H.A.A.M. van Teeffelen, A.D.M. van Mansfeld, S. Mosselman, H.S. Jansz, Cornelis J.M. Lips, P.D. Baas, Jwm Hoppener

Publikováno v: Biochimica et biophysica acta. 1087(2)

Islet amyloid polypeptide (IAPP) or amylin is a pancreatic islet hormone which was first found in amyloid in insulinomas and in pancreases of patients with type 2 diabetes. In rat a similar polypeptide occurs; however, pancreatic amyloid in this spec

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb73312e9157506627f5f0801c19fbaf
https://pubmed.ncbi.nlm.nih.gov/2223885

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Restoration of the biological activity of in vitro synthesized øX DNA by transfection of ung - spheroplasts or dUTPase treatment

Autor: G. H. Veeneman, H.A.A.M. van Teeffelen, P.D. Baas, J. H. Van Boom, Wieke R. Teertstra, G. A. Van Der Marel, H.S. Jansz

Publikováno v: FEBS Letters, 110(1), 15. Elsevier

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6532dea54d7ceaf174c63c5cb5f6e434
https://doi.org/10.1016/0014-5793(80)80012-3

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Two juxtaposed tyrosyl-OH groups participate in 0X174 gene A protein catalysed cleavage and ligation of DNA

Autor: A.D.M. van Mansfeld, H.A.A.M. van Teeffelen, P.D. Baas, H.S. Jansz

Publikováno v: Nucleic Acids Research. 14:4229-4238

Bacteriophage phi X174 encoded gene A protein is an enzyme required for initiation and termination of successive rounds of rolling circle phi X DNA replication. This enzyme catalyses cleavage and ligation of a phosphodiester bond between nucleotide r

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::7a183661be90d1fad2a463559ebb4104
https://doi.org/10.1093/nar/14.10.4229

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The bond in the bacteriophage øX174 gene A protein-DNA complex is a tyrosyl-5'-phosphate ester

Autor: H.S. Jansz, G. H. Veeneman, J. H. Van Boom, H.A.A.M. van Teeffelen, P.D. Baas, A.D.M. van Mansfeld

Publikováno v: FEBS Letters. (2):351-356

The bacteriophage øX174 gene A protein cleaves the viral strand of the double-stranded replicative form (RF) DNA of the phage at a specific site, the origin. It leaves a free 3'-OH at nucleotide 4305 (G) of the øx DNA sequence and binds covalently

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0dcd4a64ac98d90c7e517aae169f193

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A* protein of bacteriophage φX174 carries an oligonucleotide which it can transfer to the 3−OH of a DNA chain

Autor: H.A.A.M. van Teeffelen, J. Zandberg, A.D.M. van Mansfeld, H.S. Jansz, G. H. Veeneman, J. H. Van Boom, P.D. Baas

Publikováno v: FEBS Letters. (1):103-108

The bacteriophage φX174 gene A encodes two proteins: gene A protein and A* protein. Purified A* protein acts as a single-stranded, DNA-specific endonuclease which remains covalently attached to the 5′-end of the cleavage site. Incubation of A* pro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e418f1b375e47966fd943022c369c4e4

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Alteration of the ATG start codon of the A* protein of bacteriophage [phi]X174 into an ATT codon yields a viable phage indicating that A* protein is not essential for [phi]X174 reproduction

Autor: H.A.A.M. van Teeffelen, A.D.M. van Mansfeld, H. Liewerink, J. H. Van Boom, H.S. Jansz, P.D. Baas

Publikováno v: FEBS Letters, 218(1), 119. Elsevier

Bacteriophage phi X174 gene A encodes two proteins: the gene A protein and the smaller A protein, which is synthesized from a translational start signal within the A gene in the same reading frame as the gene A protein. The gene A protein is involved

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::634907ab8ed190c6870f99a65c43c8f1
https://dspace.library.uu.nl/handle/1874/17233

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Effect of SSB protein on cleavage of single-stranded DNA by phi X gene A protein and A* protein

Autor: A.C. Fluit, H.A.A.M. van Teeffelen, A.D.M. van Mansfeld, H.S. Jansz, P.D. Baas

Gene A protein of bacteriophage phi X174 plays a role as a site-specific endonuclease in the initiation and termination of phi X rolling circle DNA replication. To clarify the sequence requirements of this protein we have studied the cleavage of sing

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e30e56065a5a04a6b4f86c14c46aa037
https://europepmc.org/articles/PMC339577/

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