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CTRB1 gene
Known as:
CHYMOTRYPSINOGEN B
, CTRB
, CTRB1
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This gene plays a role in gastrointestinal proteolysis.
National Institutes of Health
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Related topics
Related topics
7 relations
Alpha-Chymotrypsinogen
CTRB1 protein, human
Chymotrypsinogen
Chymotrypsinogen A
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Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
2018
2018
Differences in CTRB1 and CTRB2 promotor activities imply new pathomechanism of associated pancreatitis risk
S. Beer
,
A. Demcsák
,
K. Seltsam
,
J. Mössner
,
J. Rosendahl
Pancreatology (Print)
2018
Corpus ID: 80634378
2018
2018
Characterization of centriole duplication in human epidermis, Bowen's disease, and squamous cell carcinoma.
Saori Watanuki
,
Harumi Fujita
,
K. Kouyama
,
M. Amagai
,
A. Kubo
Journal of dermatological science (Amsterdam)
2018
Corpus ID: 4590267
1982
1982
Stability of acetylated and superguanidinated chymotrypsinogens.
P. Cupo
,
W. El-Deiry
,
P. Whitney
,
W. M. Awad
Archives of Biochemistry and Biophysics
1982
Corpus ID: 39482882
1980
1980
Effect of diet composition on the protein synthetic pattern of the rat pancreas after a feeding period of five days.
S. Poort
,
C. Poort
Biochimica et Biophysica Acta
1980
Corpus ID: 22632736
1973
1973
Calorimetric characterization of ligand binding on trypsinogen and chymotrypsinogen A, with evidence for two binding sites on alpha-chymotrypsin.
E. J. East
,
C. G. Trowbridge
Journal of Biological Chemistry
1973
Corpus ID: 13567861
1972
1972
Modification of protein properties by change in charge. Succinylated chymotrypsinogen.
D. Shiao
,
R. Lumry
,
S. Rajender
European Journal of Biochemistry
1972
Corpus ID: 20599535
Succinylated derivatives of bovine chymotrypsinogen A and α-chymotrypsin were prepared by treatment of the native proteins with…
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1969
1969
Heat capacities from 11 to 305 degrees K and entropies of hydrated and anhydrous bovine zinc insulin and bovine chymotrypsinogen A. Entropy change for formation of peptide bonds.
J. O. Hutchens
,
A. G. Cole
,
J. W. Stout
Journal of Biological Chemistry
1969
Corpus ID: 41890232
Abstract 1. Heat capacities from 11–305°K have been measured for crystalline bovine zinc insulin containing 4% water and for…
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Review
1968
Review
1968
Sedimentation behavior of chymotrypsinogen A in the vicinity of the isoelectric point.
J. Nichol
Journal of Biological Chemistry
1968
Corpus ID: 18236436
1961
1961
The amino acid composition of chymotrypsinogen B.
B. Kassell
,
M. Laskowski
Journal of Biological Chemistry
1961
Corpus ID: 27063810
Highly Cited
1951
Highly Cited
1951
THE REVERSIBLE HEAT DENATURATION OF CHYMOTRYPSINOGEN
M. Eisenberg
,
G. Schwert
The Journal of General Physiology
1951
Corpus ID: 2467857
Within a restricted range of pH and protein concentration crystalline chymotrypsinogen undergoes thermal denaturation which is…
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