Szkudlinski MW - Search Results

1

The role of the oligosaccharide chains of thyrotropin alpha- and beta-subunits in hormone action.

Thotakura NR, Desai RK, Szkudlinski MW, Weintraub BD. Thotakura NR, et al. Among authors: szkudlinski mw. Endocrinology. 1992 Jul;131(1):82-8. doi: 10.1210/endo.131.1.1377127. Endocrinology. 1992. PMID: 1377127

2

Role of the carboxy-terminal residues of the alpha-subunit in the expression and bioactivity of human thyroid-stimulating hormone.

Grossmann M, Szkudlinski MW, Zeng H, Kraiem Z, Ji I, Tropea JE, Ji TH, Weintraub BD. Grossmann M, et al. Among authors: szkudlinski mw. Mol Endocrinol. 1995 Aug;9(8):948-58. doi: 10.1210/mend.9.8.7476992. Mol Endocrinol. 1995. PMID: 7476992

3

Expression of human thyrotropin in cell lines with different glycosylation patterns combined with mutagenesis of specific glycosylation sites. Characterization of a novel role for the oligosaccharides in the in vitro and in vivo bioactivity.

Grossmann M, Szkudlinski MW, Tropea JE, Bishop LA, Thotakura NR, Schofield PR, Weintraub BD. Grossmann M, et al. Among authors: szkudlinski mw. J Biol Chem. 1995 Dec 8;270(49):29378-85. doi: 10.1074/jbc.270.49.29378. J Biol Chem. 1995. PMID: 7493973 Free article.

4

Recombinant thyrotropin containing a beta-subunit chimera with the human chorionic gonadotropin-beta carboxy-terminus is biologically active, with a prolonged plasma half-life: role of carbohydrate in bioactivity and metabolic clearance.

Joshi L, Murata Y, Wondisford FE, Szkudlinski MW, Desai R, Weintraub BD. Joshi L, et al. Among authors: szkudlinski mw. Endocrinology. 1995 Sep;136(9):3839-48. doi: 10.1210/endo.136.9.7544273. Endocrinology. 1995. PMID: 7544273

5

Subunit-specific functions of N-linked oligosaccharides in human thyrotropin: role of terminal residues of alpha- and beta-subunit oligosaccharides in metabolic clearance and bioactivity.

Szkudlinski MW, Thotakura NR, Weintraub BD. Szkudlinski MW, et al. Proc Natl Acad Sci U S A. 1995 Sep 26;92(20):9062-6. doi: 10.1073/pnas.92.20.9062. Proc Natl Acad Sci U S A. 1995. PMID: 7568073 Free PMC article.

6

Asparagine-linked oligosaccharide structures determine clearance and organ distribution of pituitary and recombinant thyrotropin.

Szkudlinski MW, Thotakura NR, Tropea JE, Grossmann M, Weintraub BD. Szkudlinski MW, et al. Endocrinology. 1995 Aug;136(8):3325-30. doi: 10.1210/endo.136.8.7628367. Endocrinology. 1995. PMID: 7628367

7

Structure-function studies of oligosaccharides of recombinant human thyrotrophin by sequential deglycosylation and resialylation.

Thotakura NR, Szkudlinski MW, Weintraub BD. Thotakura NR, et al. Among authors: szkudlinski mw. Glycobiology. 1994 Aug;4(4):525-33. doi: 10.1093/glycob/4.4.525. Glycobiology. 1994. PMID: 7827414

8

Purification and characterization of recombinant human thyrotropin (TSH) isoforms produced by Chinese hamster ovary cells: the role of sialylation and sulfation in TSH bioactivity.

Szkudlinski MW, Thotakura NR, Bucci I, Joshi LR, Tsai A, East-Palmer J, Shiloach J, Weintraub BD. Szkudlinski MW, et al. Endocrinology. 1993 Oct;133(4):1490-503. doi: 10.1210/endo.133.4.8404588. Endocrinology. 1993. PMID: 8404588

9

Site-directed mutagenesis of amino acids 33-44 of the common alpha-subunit reveals different structural requirements for heterodimer expression among the glycoprotein hormones and suggests that cyclic adenosine 3',5'-monophosphate production and growth promotion are potentially dissociable functions of human thyrotropin.

Grossmann M, Szkudlinski MW, Dias JA, Xia H, Wong R, Puett D, Weintraub BD. Grossmann M, et al. Among authors: szkudlinski mw. Mol Endocrinol. 1996 Jun;10(6):769-79. doi: 10.1210/mend.10.6.8776737. Mol Endocrinol. 1996. PMID: 8776737

10

Expression of biologically active human thyrotropin (hTSH) in a baculovirus system: effect of insect cell glycosylation on hTSH activity in vitro and in vivo.

Grossmann M, Wong R, Teh NG, Tropea JE, East-Palmer J, Weintraub BD, Szkudlinski MW. Grossmann M, et al. Among authors: szkudlinski mw. Endocrinology. 1997 Jan;138(1):92-100. doi: 10.1210/endo.138.1.4897. Endocrinology. 1997. PMID: 8977390

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