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Items: 1 to 20 of 85

1.

Intact {alpha}-1,2-endomannosidase is a typical type II membrane protein.

Hamilton SR, Li H, Wischnewski H, Prasad A, Kerley-Hamilton JS, Mitchell T, Walling AJ, Davidson RC, Wildt S, Gerngross TU.

Glycobiology. 2005 Jun;15(6):615-24. Epub 2005 Jan 26.

PMID:
15677381
2.
3.

Identification and analysis of a class 2 alpha-mannosidase from Aspergillus nidulans.

Eades CJ, Gilbert AM, Goodman CD, Hintz WE.

Glycobiology. 1998 Jan;8(1):17-33.

PMID:
9451011
4.

A single tryptophan residue of endomannosidase is crucial for Golgi localization and in vivo activity.

Torossi T, Roth J, Ziak M.

Cell Mol Life Sci. 2007 Jul;64(14):1881-9.

PMID:
17593322
5.

Triple arginines in the cytoplasmic tail of endomannosidase are not essential for type II membrane topology and Golgi localization.

Stehli J, Torossi T, Ziak M.

Cell Mol Life Sci. 2008 May;65(10):1609-19. doi: 10.1007/s00018-008-8054-x.

PMID:
18425413
6.

Endomannosidase undergoes phosphorylation in the Golgi apparatus.

Torossi T, Guhl B, Roth J, Ziak M.

Glycobiology. 2010 Jan;20(1):55-61. doi: 10.1093/glycob/cwp142. Epub 2009 Sep 16.

PMID:
19759276
7.

cDNA cloning and expression of UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase T1 from Toxoplasma gondii.

Wojczyk BS, Stwora-Wojczyk MM, Hagen FK, Striepen B, Hang HC, Bertozzi CR, Roos DS, Spitalnik SL.

Mol Biochem Parasitol. 2003 Oct;131(2):93-107.

PMID:
14511808
8.

Cloning and characterization of a type II integral transmembrane protein gene, Itm2c, that is highly expressed in the mouse brain.

Choi SC, Kim J, Kim TH, Cho SY, Park SS, Kim KD, Lee SH.

Mol Cells. 2001 Dec 31;12(3):391-7.

10.

Human endo-alpha1,2-mannosidase is a Golgi-resident type II membrane protein.

Hardt B, Völker C, Mundt S, Salska-Navarro M, Hauptmann M, Bause E.

Biochimie. 2005 Feb;87(2):169-79.

PMID:
15760709
11.

Molecular cloning and characterization of Arabidopsis thaliana Golgi alpha-mannosidase II, a key enzyme in the formation of complex N-glycans in plants.

Strasser R, Schoberer J, Jin C, Glössl J, Mach L, Steinkellner H.

Plant J. 2006 Mar;45(5):789-803. Erratum in: Plant J. 2006 Sep;47(5):827.

12.

Molecular cloning and tissue-specific expression analysis of mouse spinesin, a type II transmembrane serine protease 5.

Watanabe Y, Okui A, Mitsui S, Kawarabuki K, Yamaguchi T, Uemura H, Yamaguchi N.

Biochem Biophys Res Commun. 2004 Nov 5;324(1):333-40.

PMID:
15465023
13.

Identification and characterization of rat Wnt1 and Wnt10b genes in silico.

Katoh Y, Katoh M.

Int J Oncol. 2005 Mar;26(3):841-5.

PMID:
15703844
14.

Endomannosidase processes oligosaccharides of alpha1-antitrypsin and its naturally occurring genetic variants in the Golgi apparatus.

Torossi T, Fan JY, Sauter-Etter K, Roth J, Ziak M.

Cell Mol Life Sci. 2006 Aug;63(16):1923-32.

PMID:
16871372
16.

A cDNA cloned from Physarum polycephalum encodes new type of family 3 beta-glucosidase that is a fusion protein containing a calx-beta motif.

Maekawa A, Hayase M, Yubisui T, Minami Y.

Int J Biochem Cell Biol. 2006;38(12):2164-72. Epub 2006 Jul 12.

PMID:
16914364
17.

Type XIII collagen is identified as a plasma membrane protein.

Hägg P, Rehn M, Huhtala P, Väisänen T, Tamminen M, Pihlajaniemi T.

J Biol Chem. 1998 Jun 19;273(25):15590-7.

18.

Cloning and characterization of the mouse ortholog of mi-er1.

Thorne LB, Grant AL, Paterno GD, Gillespie LL.

DNA Seq. 2005 Jun;16(3):237-40. Erratum in: DNA Seq. 2005 Oct;16(5):402.

PMID:
16147882
19.

Physical and genetic characterization of an outer-membrane protein (OmpM1) containing an N-terminal S-layer-like homology domain from the phylogenetically Gram-positive gut anaerobe Mitsuokella multacida.

Kalmokoff ML, Austin JW, Cyr TD, Hefford MA, Teather RM, Selinger LB.

Anaerobe. 2009 Jun;15(3):74-81. doi: 10.1016/j.anaerobe.2009.01.001. Epub 2009 Jan 20.

PMID:
19344649
20.

Genomic structure and expression of Jmjd6 and evolutionary analysis in the context of related JmjC domain containing proteins.

Hahn P, Böse J, Edler S, Lengeling A.

BMC Genomics. 2008 Jun 18;9:293. doi: 10.1186/1471-2164-9-293.

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