Výsledky vyhledávání - "H C, Thøgersen"

Recombinant alpha 2M receptor binding domain binds to the alpha 2M receptor with high affinity

Autor: T L, Holtet, K L, Nielsen, M, Etzerodt, S K, Moestrup, J, Gliemann, L, Sottrup-Jensen, H C, Thøgersen

Publikováno v: Annals of the New York Academy of Sciences. 737

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6e40f7d5c665ae6647d33d6d3b21b530
https://pubmed.ncbi.nlm.nih.gov/7524425

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Dissection of the DNA-binding domain of Xenopus laevis TFIIIA. Quantitative DNase I footprinting analysis of specific complexes between a 5 S RNA gene fragment and N-terminal fragments of TFIIIA containing three, four or five zinc-finger domains

Autor: P K, Hansen, J H, Christensen, J, Nyborg, O, Lillelund, H C, Thøgersen

Publikováno v: Journal of molecular biology. 233(2)

Recombinant zinc finger proteins corresponding to N-terminal fragments of Xenopus laevis transcription factor IIIA (TFIIIA) comprising three, four and five fingers produced in Escherichia coli as cleavable hybrid proteins were shown to form specific

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::bf6fd8c2bc390fea949e9d75e87f5057
https://pubmed.ncbi.nlm.nih.gov/8377197

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Human C.hivin.1 inhibitor: primary structure, cDNA cloning, and chromosomal localization

Autor: Karen Skriver, Elzbieta Radziejewska, Jean A. Marrinan, Susan Clark Bock, B Wiman, R L Eddy, E Nielsen, Robert Huber, V H Donaldson, H C Thøgersen

Publikováno v: Biochemistry. 25:4292-4301

The primary structure of human C1 inhibitor was determined by peptide and DNA sequencing. The single-chain polypeptide moiety of the intact inhibitor is 478 residues (52,869 Da), accounting for only 51% of the apparent molecular mass of the circulati

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25b9c413c37f6e0d5f52f80c37cd0fa6
https://doi.org/10.1021/bi00363a018

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Synthesis and sequence-specific proteolysis of hybrid proteins produced in Escherichia coli

Autor: K, Nagai, H C, Thøgersen

Publikováno v: Methods in enzymology. 153

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c5eeecac57f72b6ab11f44768f09d56d
https://pubmed.ncbi.nlm.nih.gov/3323806

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Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease

Autor: H C Thøgersen, Aaron Klug, Michael J. Runswick, Michal Novak, Ross Jakes, John E. Walker, Patricia C. Edwards, M Roth, Claude Michel Wischik, Cesar Milstein

A substantially enriched preparation of Alzheimer paired helical filaments (PHFs) has been used as a starting point for biochemical studies. Pronase treatment, which strips off adhering proteins, leaves a resistant core that is structurally intact. T

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92538ff3b7c64a1d52067e3159b07342
https://europepmc.org/articles/PMC280459/

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Cloning and sequencing of the immunoglobulin A1 protease gene (iga) of Haemophilus influenzae serotype b

Autor: Knud Poulsen, H C Thøgersen, Mogens Kilian, J P Hjorth, J Brandt

Publikováno v: Europe PubMed Central

Secretion of immunoglobulin A1 (IgA1) proteases is a characteristic of Haemophilus influenzae and several other bacterial pathogens causing infectious diseases, including meningitis. Indirect evidence suggests that the proteases are important virulen

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::741968318c059a8b82dddff559f720b5
http://europepmc.org/abstract/med/2506130

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