Results 121 to 130 of about 7,517 (194)

The FK506-binding protein 25 functionally associates with histone deacetylases and transcription factor YY1

, 2012
[[abstract]]FK506-binding proteins (FKBPs) are cellular receptors for immunosuppressants that belong to a subgroup of proteins, known as immunophilins, with peptidylprolyl cis–trans isomerase (PPIase) activity.
姚雅莉;Yao, Ya-Li
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Molecular cloning, expression, purification and characterization of a recombinant FKBP family member from Pseudomonas aeruginosa.

, 2010
The FK-506 binding proteins (FKBPs) are a family of proteins with characterised molecular functions such as peptidylprolyl cis-trans isomerase activity and chaperone activity.
Tay, Shawn Wei Liang.
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PCR Primer set sequences.

, 2013
aIL-6, interleukin 6;bLIF, Leukemia Inhibitory Factor;cPpia, peptidylprolyl isomerase A (cyclophilin A);dRpl32, ribosomal protein L32;emyc, myelocytomatosis oncogene;fCcnd1, CyclinD1;gSocs3, suppressor of cytokine signaling 3;hMyf5, myogenic factor 5 ...
Bernadette Rossano (381523), Gwénaëlle Begue (381520), Aymeric Douillard (381521), Barbara Vernus (381524), Guillaume Py (381526), Olivier Galbes (381522), Robin Candau (381525)   +6 more
core   +1 more source

The FK506-binding protein 25 functionally associates with histone deacetylases and with transcription factor YY1

, 2010
[[abstract]]FK506-binding proteins (FKBPs) are cellular receptors for immunosuppressants that belong to a subgroup of proteins, known as immunophilins, with peptidylprolyl cis–trans isomerase (PPIase) activity.
Yang WM; Yao YL; Seto E
core   +1 more source

Synthesis and Biological Evaluation of Non-Peptidic Cyclophilin Ligands

, 2016
Peptidylprolyl isomerase cyclophilins play critical roles in a variety of biological processes. Recent findings that cyclophilins are present at high levels in the CNS and that cyclosporin A may possess neuroprotective/neurotrophic effects have prompted ...
Thomas (3209193), Maureen Connolly (3017715), Tim Moeller (3238299), Sergei Belyakov (3238296), Jocelyn McCormick (3238278), Douglas E. Wilkinson (3238287), David Limburg (3238302), Chi Choi (3238290), Mike Fuller (3238284), Ling Wei (205472), Joseph Steiner (3238281), Mark Vaal (3238293), Gregory S. Hamilton (2680738), Yong-Qian Wu (2680744), Agnes Holmes (3084384)   +14 more
core   +1 more source

Cyclophilin D (CYPD; peptidylprolyl isomerase D; PPID) [PDF]

Science-Business eXchange, 2008
openaire   +1 more source

1433 Targeting peptidyl-prolyl isomerase Pin1 to modulate cancer-associated fibroblast phenotype and TGF-beta signaling

Journal for ImmunoTherapy of Cancer, 2023
Krista Goodman, Emily Corse, Catherine Sabatos-Peyton, Hanna Starobinets, Melvyn Chow, Morgan O’Shea, Doga Tasdemir, Kristin Brown, Sebastian Hayes   +8 more
doaj   +1 more source

An internal FK506-binding domain is the catalytic core of the prolyl isomerase activity associated with the Bacillus subtilis trigger factor

, 1997
Two major families of peptidylprolyl cis-trans-isomerases, the cyclophilins and the structurally unrelated FK506-binding proteins (FKBPs), have been identified as cellular factors involved in protein folding in vitro.
Schmid R, Wipat A, Emmerson PT, Carter NM, Marahiel MA, Gothel SF, Harwood CR   +6 more
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Editorial: Phosphorylation-dependent peptidyl-prolyl cis/trans isomerase PIN1 - volume II

Frontiers in Cell and Developmental Biology
Futoshi Suizu
doaj   +1 more source

Chicken FK506-binding protein, FKBP65, a member of the FKBP family of peptidylprolyl cis-trans isomerases, is only partially inhibited by FK506

, 1998
The chicken FK506-binding protein FKBP65, a peptidylprolyl cis-trans isomerase, is a rough endoplasmic reticulum protein that contains four domains homologous to FKBP13, another rough endoplasmic reticulum PPIase.
Zeng, B., MacDonald, J. R., Beck, Konrad, Bann, J. G., Gambee, J. E., Bächinger, H. P., Boswell, B. A.   +6 more
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