Skip to search form
Skip to main content
Skip to account menu
Semantic Scholar
Semantic Scholar's Logo
Search 227,346,942 papers from all fields of science
Search
Sign In
Create Free Account
Hydroxymethylbilane Synthase
Known as:
Ammonia-Lyase, Porphobilinogen
, Hydroxymethylbilane Synthetase
, Porphobilinogen Ammonia Lyase
Expand
An enzyme that catalyzes the tetrapolymerization of the monopyrrole PORPHOBILINOGEN into the hydroxymethylbilane preuroporphyrinogen…
Expand
National Institutes of Health
Create Alert
Alert
Related topics
Related topics
14 relations
Acute intermittent porphyria
Disorders of Porphyrin Metabolism
HMBS gene
In Blood
Expand
Narrower (1)
hemC protein, E coli
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Review
1994
Review
1994
Highlights in haem biosynthesis.
P. M. Jordan
Current Opinion in Structural Biology
1994
Corpus ID: 8541015
Highly Cited
1994
Highly Cited
1994
Leaf Developmental Age Controls Expression of Genes Encoding Enzymes of Chlorophyll and Heme Biosynthesis in Pea (Pisum sativum L.)
Zheng-Hui He
,
Jianming Li
,
C. Sundqvist
,
M. Timko
Plant Physiology
1994
Corpus ID: 36523807
The effects of leaf developmental age on the expression of three nuclear gene families in pea (Pisum sativum L.) coding for…
Expand
Highly Cited
1990
Highly Cited
1990
Molecular basis of hereditary C3 deficiency.
M. Botto
,
K. Fong
,
A. So
,
A. Rudge
,
M. Walport
Journal of Clinical Investigation
1990
Corpus ID: 12620590
Hereditary deficiency of complement component C3 in a 10-yr-old boy was studied. C3 could not be detected by RIA of serum from…
Expand
Highly Cited
1989
Highly Cited
1989
GATAAG; a cis-control region binding an erythroid-specific nuclear factor with a role in globin and non-globin gene expression.
M. Plumb
,
J. Frampton
,
+4 authors
P. Harrison
Nucleic Acids Research
1989
Corpus ID: 39440314
An erythroid-specific nuclear protein factor binds to a sequence motif (GATAAG) which is present in the promoter region of the…
Expand
Highly Cited
1989
Highly Cited
1989
The mouse porphobilinogen deaminase gene. Structural organization, sequence, and transcriptional analysis.
C. Beaumont
,
C. Porcher
,
C. Picat
,
Y. Nordmann
,
B. Grandchamp
Journal of Biological Chemistry
1989
Corpus ID: 24857743
The porphobilinogen deaminase gene encodes the third enzyme of the heme biosynthetic pathway. This gene is expressed in a tissue…
Expand
Highly Cited
1988
Highly Cited
1988
Activity of porphobilinogen deaminase in peripheral blood mononuclear cells of patients with metastatic cancer
L. Leibovici
,
N. Schoenfeld
,
+4 authors
A. Atsmon
Cancer
1988
Corpus ID: 28071817
Porphobilinogen deaminase (PBGD), one of the enzymes in the pathway of heme synthesis, was found to be elevated in peripheral…
Expand
Highly Cited
1986
Highly Cited
1986
Nucleotide sequence of the hemC locus encoding porphobilinogen deaminase of Escherichia coli K12.
S. Thomas
,
P. Jordan
Nucleic Acids Research
1986
Corpus ID: 28363687
Porphobilinogen deaminase, the product of the hemC locus in Escherichia coli K12, catalyses the tetrapolymerisation of…
Expand
Highly Cited
1978
Highly Cited
1978
Inhibition of dimethyl sulfoxide-stimulated Friend cell erythrodifferentiation by hydrocortisone and other steroids.
W. Scher
,
D. Tsuei
,
S. Sassa
,
P. Price
,
N. Gabelman
,
C. Friend
Proceedings of the National Academy of Sciences…
1978
Corpus ID: 27961418
Erythrodifferentiation and hemoglobin synthesis in dimethyl sulfoxide-stimulated Friend erythroleukemia cells were inhibited by…
Expand
Highly Cited
1971
Highly Cited
1971
The serum porphobilinogen and hepatic porphobilinogen deaminase in normal and porphyric individuals.
K. Miyagi
,
R. Cardinal
,
I. Bossenmaier
,
C. J. Watson
Journal of Laboratory and Clinical Medicine
1971
Corpus ID: 45224688
Abstract Methods are described for quantitative determination of serum PBG and ALA, and for hepatic PBG-D activity. The former…
Expand
Highly Cited
1966
Highly Cited
1966
Activity of Amino-laevulinic Acid Synthetase in Normal and Porphyric Human Livers
K. Nakao
,
O. Wada
,
T. Kitamura
,
K. Uono
,
G. Urata
Nature
1966
Corpus ID: 4270479
ACUTE intermittent porphyria (AIP) is well known as an inborn error of porphyrin metabolism, clinically characterized by attacks…
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