Results 101 to 110 of about 7,127 (231)
Molecular mechanism of MLL PHD3 and RNA recognition by the Cyp33 RRM domain [PDF]
The nuclear protein cyclophilin 33 (Cyp33) is a peptidyl-prolyl cis-trans isomerase that catalyzes cis-trans isomerization of the peptide bond preceding a proline and promotes folding and conformational changes in folded and unfolded proteins.
Chang, Pei-Yun +9 more
core +2 more sources
Abstract The activities of [NiFe]‐hydrogenase enzymes, which are critical to many microbes, require insertion of a Ni(II) ion into the bimetallic catalytic center. Delivery of Ni(II) to [NiFe]‐hydrogenases depends, in part, on the metallochaperone HypB, which lies at the center of a Ni(II) transfer pathway that includes the metal storage protein SlyD ...
Wayne W. H. Law +4 more
wiley +1 more source
A Family of Novel Cyclophilins, Conserved in the Mimivirus Genus of the Giant DNA Viruses
The cyclophilin (abbreviated here as CYN) family represents a large group of protein prolyl isomerase (PPIase), many of which are also chaperones that promote proper folding of a large variety of client proteins. Over the past few years, megaviruses with
Sailen Barik
doaj +1 more source
Rrd1 isomerizes RNA polymerase II in response to rapamycin [PDF]
International audienceBACKGROUND: In Saccharomyces cerevisiae, the immunosuppressant rapamycin engenders a profound modification in the transcriptional profile leading to growth arrest.
Nathalie Jouvet +4 more
core +1 more source
Phytophthora Avr3a‐like effectors target the conserved immune regulator CAD5 in host plants, suppressing its enzymatic activity to disrupt PTI and ETI responses. ABSTRACT Phytophthora species are oomycetes that cause significant losses in agricultural production and damages to natural ecosystems.
Licai Li +10 more
wiley +1 more source
The Multiple Roles of Peptidyl Prolyl Isomerases in Brain Cancer
Peptidyl prolyl isomerases (PPIases) are broadly expressed enzymes that accelerate the cis-trans isomerization of proline peptide bonds. The most extensively studied PPIase family member is protein interacting with never in mitosis A1 (PIN1), which ...
Stefano Stifani
doaj +1 more source
Native State Proline Isomerization: An Intrinsic Molecular Switch [PDF]
Exquisite control of biological function is achieved via tight regulation of the catalytic and binding activities of cellular proteins. The mechanistic details of protein regulation vary from targeted chemical modification of amino acid side chains (1 ...
Andreotti, Amy, Andreotti, Amy
core +3 more sources
ABSTRACT Peptidyl‐prolyl isomerase, NIMA‐interacting protein 1‐(Pin1) catalyses the cis–trans interconversion of the inflexible bond between serine or threonine residues and proline at the +1 position (pSer/pThr‐Pro). Although initially discovered as an essential regulator of cell division, Pin1 has since been identified as a regulator of many ...
Scott E. Roffey +5 more
wiley +1 more source
Human cyclophilin 40 unravels neurotoxic amyloids.
The accumulation of amyloidogenic proteins is a pathological hallmark of neurodegenerative disorders. The aberrant accumulation of the microtubule associating protein tau (MAPT, tau) into toxic oligomers and amyloid deposits is a primary pathology in ...
Jeremy D Baker +18 more
doaj +1 more source
A serine/arginine-rich nuclear matrix cyclophilin interacts with the C-terminal domain of RNA polymerase II [PDF]
The largest subunit of RNA polymerase II shows a striking difference in the degree of phosphorylation, depending on its functional state: initiating and elongating polymerases are unphosphorylated and highly phosphorylated respectively.
Baechi, Thomas +7 more
core

