Results 11 to 20 of about 98,169 (229)

Basic surface features of nuclear FKBPs facilitate chromatin binding [PDF]

open access: yesScientific Reports, 2017
The nucleoplasmin family of histone chaperones is identified by a pentamer-forming domain and multiple acidic tracts that mediate histone binding and chaperone activity.
Andrew Leung   +10 more
doaj   +4 more sources

FKBP Ligands—Where We Are and Where to Go? [PDF]

open access: yesFrontiers in Pharmacology, 2018
In recent years, many members of the FK506-binding protein (FKBP) family were increasingly linked to various diseases. The binding domain of FKBPs differs only in a few amino acid residues, but their biological roles are versatile.
Jürgen M. Kolos   +3 more
doaj   +4 more sources

FKBPs and the Akt/mTOR pathway [PDF]

open access: yesCell Cycle, 2013
FK506-binding proteins (FKBP) belong to the immunophilin family and are best known for their ability to enable the immunosuppressive properties of FK506 and rapamycin. For rapamycin, this is achieved by inducing inhibitory ternary complexes with the kinase mTOR. The essential accessory protein for this gain-of-function was thought to be FKBP12.
Hausch, F.   +3 more
openaire   +3 more sources

CAQ Corner: Basic concepts of transplant immunology

open access: yes, 2022
Liver Transplantation, EarlyView.
Amanda Cheung, Josh Levitsky
wiley   +1 more source

FKBP-related ncRNA-mRNA axis in breast cancer [PDF]

open access: yesGenomics, 2020
Breast cancer (BC) is a disease with morbidity ranking the first of women worldwidely. In current study, 11 DE-miRNAs, consisting of four FKBP4 related DE-miRNAs and seven FKBP5 related DE-miRNAs, were screened. Four hundred and eighty two predicted lncRNAs were found for DE-miRNAs.
Hanchu, Xiong   +5 more
openaire   +3 more sources

FKBPs in bacterial infections

open access: yesBiochimica et Biophysica Acta (BBA) - General Subjects, 2015
FK506-binding proteins (FKBPs) contain a domain with peptidyl-prolyl-cis/trans-isomerase (PPIase) activity and bind the immunosuppressive drugs FK506 and rapamycin. FKBPs belong to the immunophilin family and are found in eukaryotes and bacteria.In this review we describe two major groups of bacterial virulence-associated FKBPs, the trigger factor and ...
Unal, Can M., Steinert, Michael
openaire   +4 more sources

Peptidyl-prolyl cis-trans isomerases (immunophilins) and their roles in parasite biochemistry, host-parasite interaction and antiparasitic drug action. [PDF]

open access: yes, 2006
Immunophilin is the collective name given to the cyclophilin and FK506-binding protein (FKBP) families. As the name suggests, these include the major binding proteins of certain immunosuppressive drugs: cyclophilins for the cyclic peptide cyclosporin A ...
Adams   +101 more
core   +1 more source

Bioinformatic Analysis Reveals Conservation of Intrinsic Disorder in the Linker Sequences of Prokaryotic Dual-family Immunophilin Chaperones

open access: yesComputational and Structural Biotechnology Journal, 2018
The two classical immunophilin families, found essentially in all living cells, are: cyclophilin (CYN) and FK506-binding protein (FKBP). We previously reported a novel class of immunophilins that are natural chimera of these two, which we named dual ...
Sailen Barik
doaj   +1 more source

An essential function for the ATR-Activation-Domain (AAD) of TopBP1 in mouse development and cellular senescence [PDF]

open access: yes, 2013
ATR activation is dependent on temporal and spatial interactions with partner proteins. In the budding yeast model, three proteins – Dpb11TopBP1, Ddc1Rad9 and Dna2 - all interact with and activate Mec1ATR.
A Aguilera   +67 more
core   +3 more sources

Dual-Family Peptidylprolyl Isomerases (Immunophilins) of Select Monocellular Organisms

open access: yesBiomolecules, 2018
The dual-family peptidylprolyl cis-trans isomerases (immunophilins) represent a naturally occurring chimera of the classical FK506-binding protein (FKBP) and cyclophilin (CYN), connected by a flexible linker.
Sailen Barik
doaj   +1 more source

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