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Structural Studies of Human Hemopexin

1984
Abstract The primary structure of human hemopexin (Hpx) is being deduced from sequence analysis of a series of peptides obtained from chemical and enzymatic digests of the protein. Human Hpx consists of about 440 amino acid residues. It has five sites of attachment of GlcN oligosaccharides at the signal sequence of Asn-X-Thr/Ser.
NOBUHIRO TAKAHASHI   +2 more
openaire   +1 more source

Genetic control of serum hemopexin.

Annals of clinical research, 1977
Serum hemopexin was studied in a sample of twin pairs. Among monozygotic twin pairs a high concordance was found for serum hemopexin. This zygosity group analysis of variance also showed a significantly lower variance within than between pairs. The results indicate that the concentration of serum hemopexin is strongly influenced by genetic factors.
M, Myrhed   +2 more
openaire   +1 more source

Hemopexin in cord blood

Clinica Chimica Acta, 1970
G, Weippl   +2 more
openaire   +2 more sources

Hemopexin

New England Journal of Medicine, 1970
openaire   +3 more sources

Matrix Metalloproteinase-9 Promotes Chronic Lymphocytic Leukemia B Cell Survival through Its Hemopexin Domain

Cancer Cell, 2010
Philippe E Van Den Steen   +2 more
exaly  

Hemopexin and haptoglobin: allies against heme toxicity from hemoglobin not contenders

Frontiers in Physiology, 2015
Ann Smith, Russell J Mcculloh
exaly  

Evidence of Reciprocal Reorientation of the Catalytic and Hemopexin-Like Domains of Full-Length MMP-12

Journal of the American Chemical Society, 2008
Vito Calderone   +2 more
exaly  

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