Substitution of aspartic acid-686 by histidine or asparagine in the human androgen receptor leads to a functionally inactive protein with altered hormone-binding characteristics

scientific article

Substitution of aspartic acid-686 by histidine or asparagine in the human androgen receptor leads to a functionally inactive protein with altered hormone-binding characteristics is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1210/MEND-5-10-1562
P698PubMed publication ID1775137

P2093author name stringKuiper GG
van Rooij HC
Kaufman M
Liao S
Rosenfield RL
Romalo G
Ris-Stalpers C
Trifiro MA
Sai T
Jenster G
P433issue10
P304page(s)1562-1569
P577publication date1991-10-01
P1433published inMolecular EndocrinologyQ3319475
P1476titleSubstitution of aspartic acid-686 by histidine or asparagine in the human androgen receptor leads to a functionally inactive protein with altered hormone-binding characteristics
P478volume5

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cites work (P2860)
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Q36210938Evidence for DNA-binding domain--ligand-binding domain communications in the androgen receptor
Q41585204Exon skipping gives rise to alternatively spliced forms of the estrogen receptor in breast tumor cells
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Q35196168Replacement of arginine 773 by cysteine or histidine in the human androgen receptor causes complete androgen insensitivity with different receptor phenotypes
Q73428632Somatic mosaicism and variable expressivity
Q34228679Substitution of arginine-839 by cysteine or histidine in the androgen receptor causes different receptor phenotypes in cultured cells and coordinate degrees of clinical androgen resistance
Q33851820Syndromes associated with Homo sapiens pol II regulatory genes
Q40829543The androgen resistance syndromes: clinical and biochemical aspects
Q35064774Trinucleotide repeat polymorphism in the androgen receptor gene (AR).
Q33943733Variable expressivity and mutation databases: The androgen receptor gene mutations database

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