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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Cysteine-rich PDZ-binding protein

postsynaptic protein that binds to PSD-95; may regulate PSD-95 interaction with a tubulin-based cytoskeleton [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: PSD-95, CAN, V1a, AGE, GluR6
Papers on CRIPT
Genome-wide association studies identified novel loci for non-high-density lipoprotein cholesterol and its postprandial lipemic response.
Borecki et al., Saint Louis, United States. In Hum Genet, 2014
The best association signal was found in a tri-genic region at RHOQ-PIGF-CRIPT for baseline NHDL (lead SNP rs6544903, discovery p = 7e-7, MAF = 2 %; validation p = 6e-4 at 0.1 kb upstream neighboring SNP rs3768725, and 5e-4 at 0.7 kb downstream neighboring SNP rs6733143, MAF = 10 %).
Genomic analysis of primordial dwarfism reveals novel disease genes.
Alkuraya et al., Riyadh, Saudi Arabia. In Genome Res, 2014
We report a novel PD syndrome with distinct facies in two unrelated patients, each with a different homozygous truncating mutation in CRIPT.
The evolution and diversification of plant microtubule-associated proteins.
Gardiner, Sydney, Australia. In Plant J, 2013
The families of MAPs examined are AIR9, CLASP, CRIPT, MAP18, MOR1, TON, EB1, AtMAP70, SPR2, SPR1, WVD2 and MAP65 families (abbreviations are defined in the footnote to Table 1).
Genetic analysis of 16 NMR-lipoprotein fractions in humans, the GOLDN study.
Arnett et al., Saint Louis, United States. In Lipids, 2013
CRIPT (2p21), ACOXL (2q13), BCL2L11 (2q13), PCDH10 (4q28.3),
Gene-alcohol interactions identify several novel blood pressure loci including a promising locus near SLC16A9.
Rao et al., Saint Louis, United States. In Front Genet, 2012
Index SNPs in 20 other loci exhibited suggestive (p-value ≤ 1E-06) associations with BP traits by the 1 df interaction test or joint 2 df test, including 3 rare variants, one low-frequency variant, and SNPs near/in genes ESRRG, FAM179A, CRIPT-SOCS5, KAT2B, ADCY2, GLI3, ZNF716, SLIT1, PDE3A, KERA-LUM, RNF219-AS1, CLEC3A, FBXO15, and IGSF5.
Interactions outside the boundaries of the canonical binding groove of a PDZ domain influence ligand binding.
Jemth et al., Uppsala, Sweden. In Biochemistry, 2012
We have investigated such interactions beyond the binding groove for PDZ3 from PSD-95 and a peptide derived from the C-terminus of the natural ligand CRIPT.
Beyond the binding site: the role of the β₂-β₃ loop and extra-domain structures in PDZ domains.
Rao et al., Freiburg, Germany. In Plos Comput Biol, 2011
Using the CRIPT peptide as a prototypical ligand, our simulations suggest that a network of salt-bridges between the ligand and this loop is necessary for binding.
Arabidopsis thaliana, a plant model organism for the neuronal microtubule cytoskeleton?
Marc et al., Sydney, Australia. In J Exp Bot, 2011
A number of microtubule-associated proteins (MAPs) are conserved, including katanin, EB1, CLASP, spastin, gephyrin, CRIPT, Atlastin/RHD3, and ELP3.
T7 phage display as a method of peptide ligand discovery for PDZ domain proteins.
Spaller et al., Detroit, United States. In Biopolymers, 2008
In the case of PSD-95 PDZ3, peptides were found that possessed low-micromolar dissociation constants, as well as those that rediscovered the C-terminal sequence (KQTSV) of the protein CRIPT, a known natural binding protein of PDZ3.
A thermodynamic ligand binding study of the third PDZ domain (PDZ3) from the mammalian neuronal protein PSD-95.
Spaller et al., Detroit, United States. In Biochemistry, 2007
Two strategies were pursued in developing these binding ligands: (1) systematic N-terminal truncation of sequences derived from the C-terminal regions of identified PDZ3-binding proteins (CRIPT, neuroligin-1, and citron) and (2) selective mutation of specific positions within a consensus hexapeptide (KKETEV) known to bind PDZ3.
Targeting the PDZ domains of molecular scaffolds of transmembrane ion channels.
Mierke et al., Providence, United States. In Aaps J, 2005
The structural features of the PDZ domains with the C-termini of different receptors (GluR6), channels (Kv1.4), and cytoskeletal proteins (CRIPT) provide insight into targeting these regions.
Direct NMR observation of a substrate protein bound to the chaperonin GroEL.
Wüthrich et al., Zürich, Switzerland. In Proc Natl Acad Sci U S A, 2005
By using the NMR techniques of transverse relaxation-optimized spectroscopy (TROSY), cross-correlated relaxation-induced polarization transfer (CRIPT), and cross-correlated relaxation-enhanced polarization transfer (CRINEPT), bound hDHFR could be observed directly.
The interaction between PSD-95 and Ca2+/calmodulin is enhanced by PDZ-binding proteins.
Miyazawa et al., Japan. In J Biochem, 2005
We also found that C-terminal peptides from proteins such as CRIPT and the N-methyl-d-aspartate receptor NR2B subunit, which associate with the PDZ domain of PSD-95, enhanced the affinity of PSD-95 for calmodulin.
Sensitivity enhancement in NMR of macromolecules by application of optimal control theory.
Khaneja et al., Boston, United States. In J Biomol Nmr, 2005
For this system, the 1H-15N coherence transfer module presented here yields an average sensitivity enhancement of 20-25% for cross-correlated relaxation induced polarization transfer (CRIPT) experiments.
NMR techniques used with very large biological macromolecules in solution.
Wider, Zürich, Switzerland. In Methods Enzymol, 2004
Novel techniques optimize transverse relaxation based on cross-correlated relaxation between dipole-dipole interactions and chemical shift anisotropy (CSA), and include transverse relaxation-optimized spectroscopy (TROSY), cross-correlated relaxation-enhanced polarization transfer (CRINEPT), and cross-correlated relaxation-induced polarization transfer (CRIPT).
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