Results 171 to 180 of about 28,299 (224)

TLR-7 Stress Signaling in Differentiating and Mature Eosinophils Is Mediated by the Prolyl Isomerase Pin1. [PDF]

J Immunol, 2018
Shen ZJ, Hu J, Kashi V, Bochkov YA, Gern JE, Malter JS.   +5 more
europepmc   +1 more source

Role of the peptidyl-prolyl cis/trans isomerase Pin1 in the ubiquitin proteasome system (UPS) [PDF]

, 2009
Siepe, Dirk
core  

Editorial: Phosphorylation-dependent peptidyl-prolyl cis/trans isomerase PIN1 - volume II

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

Some of the next articles are maybe not open access.

Related searches:

Prolyl isomerases in yeast

Frontiers in Bioscience, 2004
Prolyl isomerases are enzymes that catalyze cis-trans isomerization of peptidyl-prolyl bonds and span three structurally unrelated protein families: the cyclophilins, FKBPs, and parvulins. The genome of the budding yeast Saccharomyces cerevisiae encodes eight different cyclophilins (Cpr1 to Cpr8), four FKBPs (Fpr1 to Fpr4), and a single parvulin (Ess1).
Miguel, Arevalo-Rodriguez, Xiaoyun, Wu, Steven D, Hanes, Joseph, Heitman   +3 more
openaire   +2 more sources

Peptidyl‐prolyl isomerase inhibitors

Peptide Science, 2005
AbstractDesigned peptidyl‐prolyl isomerase (PPIase) inhibitors of Pin1, cyclophilin (CyP), and FK506 binding protein (FKBP) are reviewed. Emphasis is placed on the design, structure, and biological activity of the inhibitors. While CyP and FKBP inhibitors have been explored fairly thoroughly, inhibitors of the relatively new Pin1 cell cycle regulator ...
Xiaodong J, Wang, Felicia A, Etzkorn
openaire   +2 more sources

Periplasmic Chaperones and Prolyl Isomerases

EcoSal Plus, 2018
The biogenesis of periplasmic and outer membrane proteins (OMPs) in Escherichia coli is assisted by a variety of processes that help with their folding and transport to their final destination in the cellular envelope.
Stull, Frederick, Betton, Jean-Michel, Bardwell, James C.A.   +2 more
openaire   +3 more sources

Archaeal peptidyl prolyl cis-trans isomerases (PPIases)

Frontiers in Bioscience, 2000
PPIases are ubiquitous in living organisms. While 3 families of PPIases, cyclophilin (CyP), FK506 binding protein (FKBP) and parvulin (Pvn), have been studied in detail in Eukarya and Bacteria (eubacteria), little is known about archaeal PPIases. Among 2 cyclophilins found in Archaea, only Halobacterium cyclophilin (HcCyP19) has been characterized.
T, Maruyama, M, Furutani
openaire   +2 more sources

Prolyl Isomerases: Role in Protein Folding

1993
Publisher Summary This chapter discusses the function of prolyl isomerases in protein folding. The importance of prolyl isomerization reactions as slow, rate-limiting steps of folding, and their interdependence with other events in protein folding are described.
F X, Schmid, L M, Mayr, M, Mücke, E R, Schönbrunner   +3 more
openaire   +2 more sources

Characterization of folding intermediates using prolyl isomerase

Biochemistry, 1994
Structure-reactivity relationships of human peptidyl prolyl cis-trans isomerase (PPI) toward the two slow folding reactions of yeast iso-2 cytochrome c have been used to characterize the structure of folding intermediates in the vicinity of critical prolines. We propose that the relative catalytic efficiency of PPI for the protein substrate relative to
S, Veeraraghavan, B T, Nall
openaire   +2 more sources