Skip to search form
Skip to main content
Skip to account menu
Semantic Scholar
Semantic Scholar's Logo
Search 227,741,290 papers from all fields of science
Search
Sign In
Create Free Account
Gene Product Variation Site
Known as:
AMINO ACID SUBSTITUTION POINT
, Protein Substitution Site
, Substituted Amino Acid
The amino acid position that is substituted in a gene product variant.
National Institutes of Health
Create Alert
Alert
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
2007
2007
Identification of amino acid residues at the active site of endosialidase that dissociate the polysialic acid binding and cleaving activities in Escherichia coli K1 bacteriophages.
Elina Jakobsson
,
A. Jokilammi
,
+4 authors
J. Finne
Biochemical Journal
2007
Corpus ID: 10876459
Endosialidase (endo-N-acetylneuraminidase) is a tailspike enzyme of bacteriophages specific for human pathogenic Escherichia coli…
Expand
2003
2003
A de novo R589C mutation of anion exchanger 1 causing distal renal tubular acidosis
S. Sritippayawan
,
S. Kirdpon
,
+6 authors
P. Yenchitsomanus
Pediatric nephrology (Berlin, West)
2003
Corpus ID: 705355
Anion exchanger 1 (AE1 or SLC4A1) mutations have been reported to cause distal renal tubular acidosis (dRTA), a disease…
Expand
Highly Cited
2001
Highly Cited
2001
Probing the Mechanism of Inactivation of Human Pyruvate Dehydrogenase by Phosphorylation of Three Sites*
L. Korotchkina
,
M. Patel
Journal of Biological Chemistry
2001
Corpus ID: 42726534
Activity of the mammalian pyruvate dehydrogenase complex (PDC) is regulated by phosphorylation-dephosphorylation of three serine…
Expand
Highly Cited
1997
Highly Cited
1997
Design, synthesis, and biological activities of four angiotensin II receptor ligands with gamma-turn mimetics replacing amino acid residues 3-5.
Boris Schmidt
,
S. Lindman
,
+12 authors
Anders Hallberg
Journal of Medicinal Chemistry
1997
Corpus ID: 22350693
Disulfide cyclization is a powerful method for reducing the conformational space of a peptide. This in turn may enable the study…
Expand
1995
1995
Functional consequences of proline mutations in the putative transmembrane segments 6 and 10 of the glucose transporter GLUT1.
M. Wellner
,
I. Monden
,
M. Mueckler
,
K. Keller
European Journal of Biochemistry
1995
Corpus ID: 12240419
Proline residues are thought to play a characteristic structural and/or dynamic role in various membrane proteins [Williams, K.A…
Expand
Highly Cited
1994
Highly Cited
1994
Antigenic alteration of an anomalous human luteinizing hormone caused by two chorionic gonadotropin-type amino-acid substitutions.
K. Okuda
,
T. Yamada
,
Hirosumi Imoto
,
H. Komatsubara
,
O. Sugimoto
Biochemical and Biophysical Research…
1994
Corpus ID: 12396331
We analyzed the nucleotide sequence of the luteinizing hormone beta subunit (LH beta) in a patient with an anomalous LH. This…
Expand
Highly Cited
1993
Highly Cited
1993
Thermostabilization of firefly luciferase by a single amino acid substitution at position 217.
N. Kajiyama
,
E. Nakano
Biochemistry
1993
Corpus ID: 36074580
Random mutagenesis of the luciferase cDNA from "Genji" firefly, Luciola cruciata, was induced by hydroxylamine in an attempt to…
Expand
1992
1992
Studies on the role of amino acids 38-45 in the expression of a functional thyrotropin receptor.
H. Wadsworth
,
D. Russo
,
Y. Nagayama
,
G. Chazenbalk
,
B. Rapoport
Molecular Endocrinology
1992
Corpus ID: 32536281
We previously reported that deletion or substitution of a unique eight-amino acid tract (residues 38-45) in the extracellular…
Expand
1988
1988
Resolution of alpha-substituted amino acid enantiomers by high-performance liquid chromatography after derivatization with a chiral adduct of o-phthalaldehyde. Application to glutamic acid analogues.
M. Maurs
,
F. Trigalo
,
R. Azerad
Journal of Chromatography A
1988
Corpus ID: 39895036
Highly Cited
1965
Highly Cited
1965
Map positions and specificities of suppressor mutations in Escherichia coli K-12.
G. Eggertsson
,
E. Adelberg
Genetics
1965
Corpus ID: 46073852
suppressor mutation (“suppressor”) can be defined as a mutation which A reverses the phenotypic effects of a second (“primary…
Expand
By clicking accept or continuing to use the site, you agree to the terms outlined in our
Privacy Policy
(opens in a new tab)
,
Terms of Service
(opens in a new tab)
, and
Dataset License
(opens in a new tab)
ACCEPT & CONTINUE