Results 161 to 170 of about 93,555 (212)

Molecular Association Assay Systems for Imaging Protein-Protein Interactions in Mammalian Cells. [PDF]

Biosensors (Basel)
Kim SB, Furuta T, Thangudu S, Natarajan A, Paulmurugan R.   +4 more
europepmc   +1 more source

A First-in-Class Chemical-Induced Proximity System Achieves Dose-Dependent Control of Tumor Protein P53 Gene Activation in Preclinical Models of Gastric Cancer. [PDF]

ACS Pharmacol Transl Sci
Nelson TJ, Kemper RM, Chiarella AM, Gonzalez Tineo S, Carroll M, Tripathi S, Clarke BJ, Yu X, Hu X, Cooke AJ, Chirumamilla BC, Chandler A, McGilvary E, Pattenden SG, Jin J, Crona DJ, Hathaway NA.   +16 more
europepmc   +1 more source

Tubulin glutamylation: a key regulator of flagella, cilia, centrosomes, and disease pathways. [PDF]

J Biomed Sci
Chen SC, Chuang YC, Lin YC.
europepmc   +1 more source

Conformation of two non-immunosuppressive FK506 analogs when bound to FKBP by isotope-filtered NMR

FEBS Letters, 1992
The 3D structure of two unlabeled FK506 analogs, (R)- and (S)-[18-OH]ascomycin, when bound to [U-13C,14N]FKBP were determined by isotope-filtered 2D NMR experiments.
Megumi Kawai, Jay R Luly, Stephen W Fesik   +2 more
exaly   +2 more sources

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Functions of the Hsp90-Binding FKBP Immunophilins

2022
The Hsp90 chaperone is known to interact with a diverse array of client proteins. However, in every case examined, Hsp90 is also accompanied by a single or several co-chaperone proteins. One class of co-chaperone contains a tetratricopeptide repeat (TPR) domain that targets the co-chaperone to the C-terminal region of Hsp90. Within this class are Hsp90-
Nina R, Ortiz, Naihsuan, Guy, Yenni A, Garcia, Jeffrey C, Sivils, Mario D, Galigniana, Marc B, Cox   +5 more
openaire   +2 more sources

FKBPs: at the crossroads of folding and transduction

Trends in Plant Science, 2001
FK506-binding proteins (FKBPs) belong to the large family of peptidyl-prolyl cis-trans isomerases, which are known to be involved in many cellular processes, such as cell signalling, protein trafficking and transcription. FKBPs associate into protein complexes, although the involvement and precise role of their foldase activity remain to be elucidated.
Harrar, Y., Bellini, Catherine, Faure, Jean Denis   +2 more
openaire   +3 more sources

FKBP immunophilin patents for neurological disorders

Expert Opinion on Therapeutic Patents, 2005
Immunophilins are a family of binding proteins that are highly conserved in nature and mediate the actions of immunosuppressant drugs. The FK-506-binding protein (FKBP) subclass of immunophilin bind FK-506 and rapamycin and are of particular interest due to their potent neurotrophic activity. Here, the patent literature covering the structures of novel
Robert E Babine, Bruce G Gold
exaly   +2 more sources

Mammalian FKBP-25 and Its Associated Proteins

Archives of Biochemistry and Biophysics, 2000
Soluble proteins from porcine brain were divided into two packs: (1) proteins which pass freely through CM52-cellulose, and (2) proteins retained on CM52. Each of these two packs of proteins was fractionated on preparative flat-bed isoelectrofocusing gel in the range of pH 2-12.
Andrzej Galat
exaly   +3 more sources

Stereospecific assignments and χ1 rotamers for FKBP when bound to ascomycin from 3 J H α,H β and 3 J N,H β coupling constants

FEBS Letters, 1992
3JHα,Hβ and 3JN,Hβ coupling constants were measured for isotopically labeled FKBP when bound to the immunosuppressant, ascomycin, using a 1H-coupled 3D HCCH-TOCSY and 15N-coupled 3D HSQC-TOCSY experiment, respectively.
Robert X Xu, Edward T Olejniczak, Stephen W Fesik   +2 more
exaly   +2 more sources