Results 181 to 190 of about 93,555 (212)

FKBP family proteins as promising new biomarkers for cancer

Current Opinion in Pharmacology, 2011
FK506-binding proteins (FKBPs) belong to the immunophilin family and bind immunosuppressive drugs, such as FK506 and rapamycin. These proteins, through interactions with steroid hormone receptors, kinases, or other cellular factors, play important roles in various physiological processes and, more interestingly, in pathological processes in mammals ...
Jérôme, Solassol, Alain, Mange, Thierry, Maudelonde   +2 more
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Conformational sensitivity analysis of FKBP–FK506/rapamycin complexes

Journal of Computational Chemistry, 1994
AbstractSensitivity analysis techniques are applied to the FKBP–FK506 and FKBP–rapamycin complexes to quantify the conformational relationships between FKBP and its ligands. Crystal structures of the two FKBP complexes are energy minimized in the Amber force field using a continuum solvent model, and derived Green's function sensitivity coefficients ...
Roberta Susnow, Nancie Senko, Timothy Ocain   +2 more
openaire   +1 more source

Atomic Structure of FKBP-FK506, an Immunophilin-Immunosuppressant Complex

Science, 1991
The structure of the human FK506 binding protein (FKBP), complexed with the immunosuppressant FK506, has been determined to 1.7 angstroms resolution by x-ray crystallography. The conformation of the protein changes little upon complexation, but the conformation of FK506 is markedly different in the bound and unbound forms.
G D, Van Duyne, R F, Standaert, P A, Karplus, S L, Schreiber, J, Clardy   +4 more
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Pleiotropic roles in cancer biology for multifaceted proteins FKBPs

Biochimica et Biophysica Acta (BBA) - General Subjects, 2015
FK506 binding proteins (FKBP) are multifunctional proteins highly conserved across the species and abundantly expressed in the cell. In addition to a well-established role in immunosuppression, FKBPs modulate several signal transduction pathways in the cell, due to their isomerase activity and the capability to interact with other proteins, inducing ...
ROMANO, SIMONA, D'ANGELILLO, ANNA, ROMANO, MARIA FIAMMETTA   +2 more
openaire   +3 more sources

High brain densities of the immunophilin FKBP colocalized with calcineurin

Nature, 1992
The immunophilins cyclophilin and FK506 binding protein (FKBP) are small, predominantly soluble proteins that bind the immunosuppressant drugs cyclosporin A and FK506, respectively, with high affinity, and which seem to mediate their pharmacological actions.
J P, Steiner, T M, Dawson, M, Fotuhi, C E, Glatt, A M, Snowman, N, Cohen, S H, Snyder   +6 more
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A Nonimmunosuppressant FKBP-12 Ligand Increases Nerve Regeneration

Experimental Neurology, 1997
The immunosuppressant drugs FK506 and cyclosporin A inhibit T-cell proliferation via a common mechanism: calcineurin inhibition following binding to their respective binding proteins, the peptidyl prolyl isomerases FKBP-12 and cyclophilin A. In contrast, FK506, but not cyclosporin A, accelerates nerve regeneration.
B G, Gold, M, Zeleny-Pooley, M S, Wang, P, Chaturvedi, D M, Armistead   +4 more
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Interaction of Tacrolimus (FK506) and Its Metabolites with FKBP and Calcineurin

Biochemical and Biophysical Research Communications, 1994
Tacrolimus(FK506) is a strong immuno-suppressant and shows its activity through inhibiting IL-2 mRNA transcription by forming pentameric complex with intracellular receptor(FK506 binding protein 12 kDa or FKBP12), Ca2+, calmodulin, and calcineurin.
K, Tamura, T, Fujimura, K, Iwasaki, S, Sakuma, T, Fujitsu, K, Nakamura, K, Shimomura, T, Kuno, C, Tanaka, M, Kobayashi   +9 more
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A mechanism for rotamase catalysis by the FK506 binding protein (FKBP)

Biochemistry, 1993
A detailed mechanism for the catalysis of prolyl isomerization by the rotamase enzyme FKBP is proposed on the basis of a model constructed from the known structure of the FK506/FKBP complex. The model substrate is bound as a type VIa proline turn with the ends exposed to permit longer polypeptide chains (e.g., protein loops) to act as substrates. An ab
S, Fischer, S, Michnick, M, Karplus
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The role of PASTICCINO1, an FKBP-like protein, in plant development

1999
The pasticcino (pas) mutants of Arabidopsis thaliana were identified due to their abnormal response to cytokinins. These mutants fall into 3 complementation groups: pas1 (2 alleles), pas2 (1 allele) and pas3 (4 alleles). The mutants all have excessive and disorganised cell divisions leading to extra cell layers in the hypocotyl, abnormal apical ...
Cowling, R., Vittorioso, P., Faure, Jean Denis, Caboche, Michel, Bellini, Catherine   +4 more
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Neurospora crassa FKBPs

1997
Abstract FK506-binding proteins; rapamycin-binding proteins; peptidyl-prolyl cis-trans isomerases (PPIase, EC no. 5.2.1.8.); rotamases, immunophilins (Schreiber, 1992). Neurospora crassa is sensitive against the immunosuppressants FK506 and rapamycin, which originally were isolated as antifungal agents.
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