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Structure of human POFUT2: insights into thrombospondin type 1 repeat fold and O-fucosylation.

Chen C.I., Keusch J.J., Klein D., Hess D., Hofsteenge J., Gut H.

EMBO J. 31:3183-3197(2012) · UniProtKB (1) · Mapped (3)

Copine-III interacts with ErbB2 and promotes tumor cell migration.

Heinrich C., Keller C., Boulay A., Vecchi M., Bianchi M., Sack R., Lienhard S., Duss S., Hofsteenge J., Hynes N.E.

Oncogene 29:1598-1610(2010) · Mapped (11)

Deficiency of Dol-P-Man synthase subunit DPM3 bridges the congenital disorders of glycosylation with the dystroglycanopathies.

Lefeber D.J., Schonberger J., Morava E., Guillard M., Huyben K.M., Verrijp K., Grafakou O., Evangeliou A., Preijers F.W., Manta P. et al.

Am. J. Hum. Genet. 85:76-86(2009) · UniProtKB (1)

Peters Plus syndrome is a new congenital disorder of glycosylation and involves defective Omicron-glycosylation of thrombospondin type 1 repeats.

Hess D., Keusch J.J., Oberstein S.A., Hennekam R.C., Hofsteenge J.

J. Biol. Chem. 283:7354-7360(2008) · Mapped (1)

Identification and characterization of abeta1,3-glucosyltransferase that synthesizes the Glc-beta1,3-Fuc disaccharide on thrombospondin type 1 repeats.

Kozma K., Keusch J.J., Hegemann B., Luther K.B., Klein D., Hess D., Haltiwanger R.S., Hofsteenge J.

J. Biol. Chem. 281:36742-36751(2006) · Mapped (3)

Evidence for N- and C-terminal processing of a plant defence-related enzyme: the primary structure of tobacco pre-pro-beta-1,3-glucanase.

Shinshi H., Wenzler H., Neuhaus J.-M., Felix G., Hofsteenge J., Meins F. Jr.

Proc. Natl. Acad. Sci. U.S.A. 85:5541-5545(1988) · UniProtKB (1)

The WSAWS motif is C-hexosylated in a soluble form of the erythropoietin receptor.

Furmanek A., Hess D., Rogniaux H., Hofsteenge J.

Biochemistry 42:8452-8458(2003) · UniProtKB (1) · Mapped (1)

C-mannosylation and O-fucosylation of thrombospondin type 1 repeats.

Gonzalez de Peredo A., Klein D., Macek B., Hess D., Peter-Katalinic J., Hofsteenge J.

Mol. Cell. Proteomics 1:11-18(2002) · UniProtKB (2)

Identification of tyrosine phosphorylation sites on 3-phosphoinositide-dependent protein kinase-1 (PDK1) and their role in regulating kinase activity.

Park J., Hill M.M., Hess D., Brazil D.P., Hofsteenge J., Hemmings B.A.

J. Biol. Chem. 276:37459-37471(2001) · UniProtKB (1) · Mapped (4)

Requirement of the Lec35 gene for all known classes of monosaccharide-P-dolichol-dependent glycosyltransferase reactions in mammals.

Anand M., Rush J.S., Ray S., Doucey M.A., Weik J., Ware F.E., Hofsteenge J., Waechter C.J., Lehrman M.A.

Mol. Biol. Cell 12:487-501(2001) · UniProtKB (2)

C-mannosylation and O-fucosylation of the thrombospondin type 1 module.

Hofsteenge J., Huwiler K.G., Macek B., Hess D., Lawler J., Mosher D.F., Peter-Katalinic J.

J. Biol. Chem. 276:6485-6498(2001) · UniProtKB (2)

Properdin, the positive regulator of complement, is highly C-mannosylated.

Hartmann S., Hofsteenge J.

J. Biol. Chem. 275:28569-28574(2000) · UniProtKB (1)

The four terminal components of the complement system are C-mannosylated on multiple tryptophan residues.

Hofsteenge J., Blommers M., Hess D., Furmanek A., Miroshnichenko O.

J. Biol. Chem. 274:32786-32794(1999) · UniProtKB (5)

Functional expression of human PP2Ac in yeast permits the identification of novel C-terminal and dominant-negative mutant forms.

Evans D.R., Myles T., Hofsteenge J., Hemmings B.A.

J. Biol. Chem. 274:24038-24046(1999) · Mapped (1)

Recombinant human interleukin-12 is the second example of a C-mannosylated protein.

Doucey M.A., Hess D., Blommers M.J., Hofsteenge J.

Glycobiology 9:435-441(1999) · UniProtKB (1)

Ribonucleases from rat and bovine liver: purification, specificity and structural characterization.

Zhao W., Kote-Jarai Z., van Santen Y., Hofsteenge J., Beintema J.J.

Biochim. Biophys. Acta 1384:55-65(1998) · UniProtKB (1)

Recognition signal for C-mannosylation of Trp-7 in RNase 2 consists of sequence Trp-x-x-Trp.

Krieg J., Hartmann S., Vicentini A., Glasner W., Hess D., Hofsteenge J.

Mol. Biol. Cell 9:301-309(1998) · UniProtKB (1)

Structure and expression of a 72-kDa regulatory subunit of protein phosphatase 2A. Evidence for different size forms produced by alternative splicing.

Hendrix P., Mayer-Jaekel R.E., Cron P., Goris J., Hofsteenge J., Merlevede W., Hemmings B.A.

J. Biol. Chem. 268:15267-15276(1993) · UniProtKB (1)

Purification and cDNA cloning of a transcription factor which functionally cooperates within a cAMP regulatory unit in the porcine uPA gene.

Menoud P.-A., Matthies R., Hofsteenge J., Nagamine Y.

Nucleic Acids Res. 21:1845-1852(1993) · UniProtKB (1)

The amino acid sequence of iguana (Iguana iguana) pancreatic ribonuclease.

Zhao W., Beintema J.J., Hofsteenge J.

Eur. J. Biochem. 219:641-646(1994) · UniProtKB (1)

Residues 36-42 of liver RNase PL3 contribute to its uridine-preferring substrate specificity. Cloning of the cDNA and site-directed mutagenesis studies.

Vicentini A.M., Hemmings B.A., Hofsteenge J.

Protein Sci. 3:459-466(1994) · UniProtKB (1)

Demonstration by mass spectrometry that pseudo-hevein and hevein have ragged C-terminal sequences.

Soedjanaatmadja U.M.S., Hofsteenge J., Jeronimus-Stratingh C.M., Bruins A.P., Beintema J.J.

Biochim. Biophys. Acta 1209:144-148(1994) · UniProtKB (1)

New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us.

Hofsteenge J., Mueller D.R., de Beer T., Loeffler A., Richter W.J., Vliegenthart J.F.G.

Biochemistry 33:13524-13530(1994) · UniProtKB (1)

AUH, a gene encoding an AU-specific RNA binding protein with intrinsic enoyl-CoA hydratase activity.

Nakagawa J., Waldner H.P., Meyer-Monard S., Hofsteenge J., Jenoe P., Moroni C.

Proc. Natl. Acad. Sci. U.S.A. 92:2051-2055(1995) · UniProtKB (1)

Purification and primary structure of a porcine kidney non-secretory ribonuclease.

Iwama M., Sanda A., Ohgi K., Hofsteenge J., Irie M.

Biosci. Biotechnol. Biochem. 57:2133-2138(1993) · UniProtKB (1)

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