n-acetylneuraminic acid and Pituitary Neoplasms

n-acetylneuraminic acid has been researched along with Pituitary Neoplasms in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	1 (50.00)	18.7374
1990's	1 (50.00)	18.2507
2000's	0 (0.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Breen, KC; Coughlan, CM; Georgopoulou, N; Gillian, AM; McFarlane, I	1
Chen, T; Gesundheit, N; Magner, JA; Weintraub, BD	1

Other Studies

2 other study(ies) available for n-acetylneuraminic acid and Pituitary Neoplasms

Article	Year
The role of the protein glycosylation state in the control of cellular transport of the amyloid beta precursor protein. Neuroscience, 1999, Volume: 90, Issue:1 Topics: 1-Deoxynojirimycin; Amyloid beta-Protein Precursor; Animals; beta-D-Galactoside alpha 2-6-Sialyltransferase; Biological Transport; Carbohydrate Sequence; Glycosylation; Golgi Apparatus; Mannosidases; Membrane Proteins; Mice; Molecular Sequence Data; N-Acetylneuraminic Acid; Neuraminidase; Neuroblastoma; Phytohemagglutinins; Pituitary Neoplasms; Polysaccharides; Protein Processing, Post-Translational; Rats; Sialyltransferases; Swainsonine; Tumor Cells, Cultured	1999
Differential sulfation and sialylation of secreted mouse thyrotropin (TSH) subunits: regulation by TSH-releasing hormone. Endocrinology, 1986, Volume: 119, Issue:2 Topics: Animals; Glycoprotein Hormones, alpha Subunit; Hexosamines; Hexosaminidases; Hypothyroidism; Macromolecular Substances; Methionine; Mice; N-Acetylneuraminic Acid; Peptide Fragments; Pituitary Gland; Pituitary Hormones, Anterior; Pituitary Neoplasms; Sialic Acids; Sulfates; Thyrotropin; Thyrotropin-Releasing Hormone	1986

Article

Year

The role of the protein glycosylation state in the control of cellular transport of the amyloid beta precursor protein.

Neuroscience, 1999, Volume: 90, Issue:1

Topics: 1-Deoxynojirimycin; Amyloid beta-Protein Precursor; Animals; beta-D-Galactoside alpha 2-6-Sialyltransferase; Biological Transport; Carbohydrate Sequence; Glycosylation; Golgi Apparatus; Mannosidases; Membrane Proteins; Mice; Molecular Sequence Data; N-Acetylneuraminic Acid; Neuraminidase; Neuroblastoma; Phytohemagglutinins; Pituitary Neoplasms; Polysaccharides; Protein Processing, Post-Translational; Rats; Sialyltransferases; Swainsonine; Tumor Cells, Cultured

1999

Differential sulfation and sialylation of secreted mouse thyrotropin (TSH) subunits: regulation by TSH-releasing hormone.

Endocrinology, 1986, Volume: 119, Issue:2

Topics: Animals; Glycoprotein Hormones, alpha Subunit; Hexosamines; Hexosaminidases; Hypothyroidism; Macromolecular Substances; Methionine; Mice; N-Acetylneuraminic Acid; Peptide Fragments; Pituitary Gland; Pituitary Hormones, Anterior; Pituitary Neoplasms; Sialic Acids; Sulfates; Thyrotropin; Thyrotropin-Releasing Hormone

1986