Page last updated: 2024-11-08

serine and Generalized Resistance to Thyroid Hormone

serine has been researched along with Generalized Resistance to Thyroid Hormone in 4 studies

Serine: A non-essential amino acid occurring in natural form as the L-isomer. It is synthesized from GLYCINE or THREONINE. It is involved in the biosynthesis of PURINES; PYRIMIDINES; and other amino acids.
serine : An alpha-amino acid that is alanine substituted at position 3 by a hydroxy group.

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's4 (100.00)18.2507
2000's0 (0.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Refetoff, S1
Weiss, RE1
Wing, JR1
Sarne, D1
Chyna, B1
Hayashi, Y1
Pohlenz, J1
Wildhardt, G1
Zabel, B1
Willgerodt, H1
Tagami, T1
Gu, WX1
Peairs, PT1
West, BL1
Jameson, JL1
Gurnell, M1
Rajanayagam, O1
Agostini, M1
Clifton-Bligh, RJ1
Wang, T1
Zelissen, PM1
van der Horst, F1
van de Wiel, A1
Macchia, E1
Pinchera, A1
Schwabe, JW1
Chatterjee, VK1

Trials

1 trial available for serine and Generalized Resistance to Thyroid Hormone

ArticleYear
Resistance to thyroid hormone in subjects from two unrelated families is associated with a point mutation in the thyroid hormone receptor beta gene resulting in the replacement of the normal proline 453 with serine.
    Thyroid : official journal of the American Thyroid Association, 1994,Fall, Volume: 4, Issue:3

    Topics: Adult; Base Sequence; DNA; Genotype; Humans; Male; Molecular Sequence Data; Pedigree; Phenotype; Poi

1994

Other Studies

3 other studies available for serine and Generalized Resistance to Thyroid Hormone

ArticleYear
Resistance to thyroid hormone in a family caused by a new point mutation L330S in the thyroid receptor (TR) beta gene.
    Thyroid : official journal of the American Thyroid Association, 1997, Volume: 7, Issue:1

    Topics: Child; DNA; Exons; Humans; Leucine; Male; Multigene Family; Pedigree; Point Mutation; Receptors, Thy

1997
A novel natural mutation in the thyroid hormone receptor defines a dual functional domain that exchanges nuclear receptor corepressors and coactivators.
    Molecular endocrinology (Baltimore, Md.), 1998, Volume: 12, Issue:12

    Topics: Cell Nucleus; Codon; Dimerization; DNA; Female; Histone Acetyltransferases; Humans; Infant; Leucine;

1998
Three novel mutations at serine 314 in the thyroid hormone beta receptor differentially impair ligand binding in the syndrome of resistance to thyroid hormone.
    Endocrinology, 1999, Volume: 140, Issue:12

    Topics: Adolescent; Adult; Aged; Child; Child, Preschool; Crystallization; Dimerization; DNA; Female; Gene E

1999