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PYCR1 encodes an enzyme that catalyzes the NAD(P)H-dependent conversion of pyrroline-5-carboxylate to proline. Additionally we are shipping Pyrroline-5-Carboxylate Reductase 1 Proteins (14) and Pyrroline-5-Carboxylate Reductase 1 Kits (3) and many more products for this protein.
Showing 10 out of 56 products:
Human Polyclonal PYCR1 Primary Antibody for FACS, IHC (p) - ABIN954393
Reversade, Escande-Beillard, Dimopoulou, Fischer, Chng, Li, Shboul, Tham, Kayserili, Al-Gazali, Shahwan, Brancati, Lee, OConnor, Schmidt-von Kegler, Merriman, Nelson, Masri, Alkazaleh, Guerra et al.: Mutations in PYCR1 cause cutis laxa with progeroid features. ... in Nature genetics 2009
Show all 3 references for ABIN954393
Cow (Bovine) Polyclonal PYCR1 Primary Antibody for WB - ABIN2787369
Meng, Lou, Liu, Li, Zhao, Bartlam, Rao: Crystal structure of human pyrroline-5-carboxylate reductase. in Journal of molecular biology 2006
Human Polyclonal PYCR1 Primary Antibody for IF, WB - ABIN519565
De Ingeniis, Ratnikov, Richardson, Scott, Aza-Blanc, De, Kazanov, Pellecchia, Ronai, Osterman, Smith: Functional specialization in proline biosynthesis of melanoma. in PLoS ONE 2012
Silencing of both PYCR1 and PYCR2 (show PYCR2 Antibodies) completely abolished anti-oxidation activity of RRM2B (show RRM2B Antibodies), demonstrating a functional collaboration of these metabolic enzymes in response to oxidative stress.
confirming that indeed PYCR1 generates L-pipecolic acid from Delta(1)-piperideine-6-carboxylate
our current study presents the second largest group of patients with PYCR1-related ARCL (show ATP6V0A2 Antibodies) and expands the clinical and genetic spectrum.
Identification of two new mutations in the PYCR1 gene in patients with autosomal recessive cutis laxa, type 2.
Data suggest that DJ-1 (show PARK7 Antibodies) and PYCR1 are on the same pathway of anti-oxidative stress protection of the cells.
The findings presented here suggest a mutation screening of PYCR1 and cardiovascular survey in patients with De Barsy syndrome (DBS (show MCF2L Antibodies)).
Mutation analysis revealed the presence of disease-causing variants in PYCR1, including a novel deletion of the entire PYCR1 gene in one family, and in each of the other patients the homozygous missense mutations.
A novel mutation in PYCR1 causes an autosomal recessive cutis laxa with premature aging features in a family.
The phenotype caused by PYCR1 mutations corresponds to geroderma osteodysplasticum rather than ARCL2B.
Mutagenesis and kinetic studies reveal the pivotal roles of the dinucleotide-binding Rossmann motif and residue Glu221 in the human enzyme Pyrroline-5-carboxylate reductase (show PYCR2 Antibodies)(P5CR).
This gene encodes an enzyme that catalyzes the NAD(P)H-dependent conversion of pyrroline-5-carboxylate to proline. This enzyme may also play a physiologic role in the generation of NADP(+) in some cell types. The protein forms a homopolymer and localizes to the mitochondrion. Alternate splicing results in two transcript variants encoding different isoforms.
P5C reductase 1
, mitochondrial pyrroline-5-carboxylate reductase 1
, proliferation-inducing protein 45
, pyrroline-5-carboxylate reductase 1, mitochondrial
, P5CR 1