G J Steffens
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Explore the profile of G J Steffens including associated specialties, affiliations and a list of published articles.
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27
Citations
367
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Recent Articles
1.
Wnendt S, Janocha E, Steffens G, Strassburger W
Protein Eng
. 1997 Feb;
10(2):169-73.
PMID: 9089816
In order to design plasminogen activators with improved thrombolytic properties, bifunctional proteins with both plasminogen-activating and anticoagulative activity were constructed by fusing a thrombin-inhibitory moiety itself comprises four elements: linker...
2.
Hiemstra P, Maassen R, Stolk J, Heinzel-Wieland R, Steffens G, Dijkman J
Infect Immun
. 1996 Nov;
64(11):4520-4.
PMID: 8890201
Antileukoprotease (ALP), or secretory leukocyte proteinase inhibitor, is an endogenous inhibitor of serine proteinases that is present in various external secretions. ALP, one of the major inhibitors of serine proteinases...
3.
Wnendt S, Janocha E, Schneider J, Steffens G
Protein Eng
. 1996 Feb;
9(2):213-23.
PMID: 9005443
The blood clotting enzyme thrombin plays a central role in the aetiology of occlusive disorders such as stroke and acute myocardial infarction. During fibrinolytic therapy with plasminogen activators, thrombin is...
4.
Lijnen H, Wnendt S, Schneider J, Janocha E, Van Hoef B, Collen D, et al.
Eur J Biochem
. 1995 Nov;
234(1):350-7.
PMID: 8529664
A chimeric protein (rscu-PA-40-kDa/Hir), consisting of the C-terminal amino acids 53-65 of hirudin (Hir), fused via a 14-amino-acid linker sequence to the C-terminal of a 40-kDa fragment (Ser47-Leu411) of recombinant...
5.
Steffens G, Heinzel-Wieland R, Saunders D, Wolf B, Rudolphus A, Stolk J, et al.
Agents Actions Suppl
. 1993 Jan;
42:111-21.
PMID: 8356918
Native antileukoproteinase (ALP) and two oxidant resistant mutants ALP 242 and ALP 231 were synthesized by means of recombinant DNA technology. In the ALP 242 molecule the methionine residue located...
6.
Rudolphus A, Heinzel-Wieland R, Vincent V, Saunders D, Steffens G, Dijkman J, et al.
Clin Sci (Lond)
. 1991 Dec;
81(6):777-84.
PMID: 1662584
1. Antileucoprotease, being sensitive to oxidative inactivation, can be produced by recombinant techniques. Via site-directed mutagenesis, two mutants of recombinant antileucoprotease were produced in which one or more of the...
7.
Heinzel-Wieland R, Steffens G, Flohe L
Biomed Biochim Acta
. 1991 Jan;
50(4-6):677-81.
PMID: 1801742
Tandem gene plasmids were constructed and used to express inactive proteins equivalent to human antileukoproteinase (ALP) and the variants [Leu73]-ALP and [Leu73, 82, 94, 96]-ALP in E. coli K12. After...
8.
Reinecke K, Wolf B, MICHELSON A, Puget K, Steffens G, Flohe L
Biol Chem Hoppe Seyler
. 1988 Aug;
369(8):715-25.
PMID: 3214553
The primary structure of Cu-Zn superoxide dismutase from rabbit liver was investigated. The reduced and S-carboxymethylated enzyme was treated with cyanogen bromide, trypsin or Staphylococcus aureus proteinase V8. The resulting...
9.
Steffens G, MICHELSON A, Puget K, Flohe L
Biol Chem Hoppe Seyler
. 1986 Oct;
367(10):1017-24.
PMID: 3790250
The primary structure of Cu-Zn superoxide dismutase isolated from rat liver was determined. The enzyme was reduced, carboxymethylated and fragmented by treatment with cyanogen bromide, trypsin or Staphylococcus aureus proteinase...
10.
Steffens G, MICHELSON A, Otting F, Puget K, Strassburger W, Flohe L
Biol Chem Hoppe Seyler
. 1986 Oct;
367(10):1007-16.
PMID: 3790249
The complete amino-acid sequence of Cu-Zn superoxide dismutase from white cabbage (Brassica oleracea) is reported. The polypeptide chain consists of 151 amino acids and has a molecular mass of 15,604...