Skip to search form
Skip to main content
Skip to account menu
Semantic Scholar
Semantic Scholar's Logo
Search 210,104,081 papers from all fields of science
Search
Sign In
Create Free Account
Isomerase
Known as:
EC 5
, Isomerases
, Isomerases [Chemical/Ingredient]
A class of enzymes that catalyze geometric or structural changes within a molecule to form a single product. The reactions do not involve a net…
Expand
National Institutes of Health
Create Alert
Alert
Related topics
Related topics
49 relations
Narrower (35)
4-oxalocrotonate tautomerase
4S-limonene synthase
Carbohydrate Epimerases
Chalcone isomerase
Expand
Aldose 1-epimerase
Enzyme Gene
GPI Ser-cCnc
Glucose phosphate isomerase:CCnc:Pt:RBC:Qn
Expand
Broader (1)
Enzymes
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Review
2009
Review
2009
Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation.
Feras Hatahet
,
L. Ruddock
Antioxidants and Redox Signaling
2009
Corpus ID: 11414827
Disulfide bond formation is probably involved in the biogenesis of approximately one third of human proteins. A central player in…
Expand
Highly Cited
2009
Highly Cited
2009
Hidden alternate structures of proline isomerase essential for catalysis
J. Fraser
,
M. Clarkson
,
Sheena C. Degnan
,
R. Erion
,
D. Kern
,
T. Alber
Nature
2009
Corpus ID: 4354655
A long-standing challenge is to understand at the atomic level how protein dynamics contribute to enzyme catalysis. X-ray…
Expand
Highly Cited
2008
Highly Cited
2008
Human gene therapy for RPE65 isomerase deficiency activates the retinoid cycle of vision but with slow rod kinetics
A. V. Cideciyan
,
T. Aleman
,
+14 authors
W. Hauswirth
Proceedings of the National Academy of Sciences
2008
Corpus ID: 15503420
The RPE65 gene encodes the isomerase of the retinoid cycle, the enzymatic pathway that underlies mammalian vision. Mutations in…
Expand
Highly Cited
2007
Highly Cited
2007
Disulphide-isomerase-enabled shedding of tumour-associated NKG2D ligands
B. Kaiser
,
D. Yim
,
+6 authors
T. Spies
Nature
2007
Corpus ID: 4430131
Tumour-associated ligands of the activating NKG2D (natural killer group 2, member D; also called KLRK1) receptor—which are…
Expand
Review
2002
Review
2002
Orchestrating the unfolded protein response in health and disease.
R. Kaufman
Journal of Clinical Investigation
2002
Corpus ID: 9892553
A variety of approaches have been employed to identify the UPR signaling components, their function, and their physiological role…
Expand
Highly Cited
2001
Highly Cited
2001
Overexpression of petunia chalcone isomerase in tomato results in fruit containing increased levels of flavonols
S. Muir
,
G. Collins
,
+5 authors
M. Verhoeyen
Nature Biotechnology
2001
Corpus ID: 19063041
Tomatoes are an excellent source of the carotenoid lycopene, a compound that is thought to be protective against prostate cancer…
Expand
Review
1999
Review
1999
The protein disulphide-isomerase family: unravelling a string of folds.
D. Ferrari
,
H. Söling
Biochemical Journal
1999
Corpus ID: 16673250
The mammalian protein disulphide-isomerase (PDI) family encompasses several highly divergent proteins that are involved in the…
Expand
Review
1996
Review
1996
Molecular and industrial aspects of glucose isomerase.
S. Bhosale
,
M. Rao
,
V. Deshpande
Microbiological reviews
1996
Corpus ID: 19337021
Glucose isomerase (GI) (D-xylose ketol-isomerase; EC. 5.3.1.5) catalyzes the reversible isomerization of D-glucose and D-xylose…
Expand
Review
1994
Review
1994
Protein disulphide isomerase: building bridges in protein folding.
R. Freedman
,
T. Hirst
,
M. Tuite
TIBS -Trends in Biochemical Sciences. Regular ed
1994
Corpus ID: 33180256
Highly Cited
1989
Highly Cited
1989
Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin
N. Takahashi
,
T. Hayano
,
Masanori Suzuki
Nature
1989
Corpus ID: 4275952
Peptidyl-prolyl cis-trans isomerase (PPIase) catalyses the cis-trans isomerization of proline imidic peptide bonds in…
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