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- Publications
- Influence
Tissue transglutaminase selectively modifies gliadin peptides that are recognized by gut-derived T cells in celiac disease
- Ø. Molberg, S. Mcadam, +10 authors Ludvig M. Sollid
- Biology, Medicine
- Nature Medicine
- 1 June 1998
The action of tissue Transglutaminase1 (TGase) on specific protein-bound glutamine residues plays a critical role in numerous biological processes2–5. Here we provide evidence for a new role of this… Expand
Determinants essential for the transmissible gastroenteritis virus-receptor interaction reside within a domain of aminopeptidase-N that is distinct from the enzymatic site.
- B. Delmas, J. Gelfi, E. Kut, H. Sjöström, O. Norén, H. Laude
- Biology, Medicine
- Journal of virology
- 1 August 1994
The swine-specific coronavirus transmissible gastroenteritis virus (TGEV) uses pig aminopeptidase-N (pAPN) as a cellular receptor. We showed that the human aminopeptidase-N (hAPN) cannot substitute… Expand
Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA
- J. Olsen, Gillian M. Cowell, +10 authors O. Norén
- Biology, Medicine
- FEBS letters
- 10 October 1988
The complete primary structure (967 amino acids) of an intestinal human aminopeptidase N (EC 3.4.11.2) was deduced from the sequence of a cDNA clone. Aminopeptidase N is anchored to the microvillar… Expand
Regulation of lactase-phlorizin hydrolase gene expression by the caudal-related homoeodomain protein Cdx-2.
- J. Troelsen, C. Mitchelmore, N. Spodsberg, A. Jensen, O. Norén, H. Sjöström
- Biology, Medicine
- The Biochemical journal
- 15 March 1997
Lactase-phlorizin hydrolase is exclusively expressed in the small intestine and is often used as a marker for the differentiation of enterocytes. The cis-element CE-LPH1 found in the… Expand
Transcriptional regulation of pig lactase-phlorizin hydrolase: involvement of HNF-1 and FREACs.
- N. Spodsberg, J. Troelsen, P. Carlsson, S. Enerbäck, H. Sjöström, O. Norén
- Biology, Medicine
- Gastroenterology
- 1 April 1999
BACKGROUND & AIMS
One-kilobase sequence of the upstream fragment of the pig lactase-phlorizin hydrolase gene has been shown to control small intestinal-specific expression and postweaning decline of… Expand
Interaction between the homeodomain proteins Cdx2 and HNF1alpha mediates expression of the lactase-phlorizin hydrolase gene.
- C. Mitchelmore, J. Troelsen, N. Spodsberg, H. Sjöström, O. Norén
- Medicine
- The Biochemical journal
- 2000
Lactase-phlorizin hydrolase is a brush-border enzyme which is specifically expressed in the small intestine where it hydrolyses lactose, the main carbohydrate found in milk. We have previously… Expand
Purification and characterisation of amphiphilic lactase/phlorizin hydrolase from human small intestine.
- H. Skovbjerg, H. Sjöström, O. Norén
- Medicine, Chemistry
- European journal of biochemistry
- 1 March 1981
Human intestinal lactase/phlorizin hydrolase (EC 3.2.1.23/62) was purified in its amphiphilic form by immunoadsorbent chromatography. The purification factor was approximately 600 and the recovery… Expand
Human Coronavirus 229E: Receptor Binding Domain and Neutralization by Soluble Receptor at 37°C
- Jamie J. Breslin, Irene Mørk, +7 authors K. Holmes
- Biology
- Journal of Virology
- 1 April 2003
ABSTRACT Truncated human coronavirus HCoV-229E spike glycoproteins containing amino acids 407 to 547 bound to purified, soluble virus receptor, human aminopeptidase N (hAPN). Soluble hAPN neutralized… Expand
The Coronavirus Transmissible Gastroenteritis Virus Causes Infection after Receptor-Mediated Endocytosis and Acid-Dependent Fusion with an Intracellular Compartment
ABSTRACT Aminopeptidase N is a species-specific receptor for transmissible gastroenteritis virus (TGEV), which infects piglets, and for the 229E virus, which infects humans. It is not known whether… Expand