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Peptidyl‐Prolyl Isomerase Activity of Immunophilins Could Be the Mere Consequence of Protein Complex Organization
Author(s) -
Galigniana Mario D.
Publication year - 2020
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.202000073
Subject(s) - fkbp , peptidylprolyl isomerase , cis trans isomerases , cyclophilin , prolyl isomerase , isomerase , foldase , cypa , cyclophilin a , chemistry , mutant , biochemistry , protein folding , protein disulfide isomerase , chaperone (clinical) , biology , pin1 , enzyme , microbiology and biotechnology , medicine , escherichia coli , pathology , groel , gene
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