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

Tetratricopeptide repeat domain 1

TPR1, TPRI
Top mentioned proteins: Hsp90, HSP70, ACID, CAN, V1a
Papers on TPR1
Structure of RagB, a major immunodominant outer-membrane surface receptor antigen of Porphyromonas gingivalis.
New
Gomis-Rüth et al., Barcelona, Spain. In Mol Oral Microbiol, Nov 2015
It consists of four tetratrico peptide repeats (TPR1-4), each arranged as two helices connected by a linker, plus two extra downstream capping helices.
Bipartite Topology of Treponema pallidum Repeat Proteins C/D and I: OUTER MEMBRANE INSERTION, TRIMERIZATION, AND PORIN FUNCTION REQUIRE A C-TERMINAL β-BARREL DOMAIN.
New
Radolf et al., Farmington, United States. In J Biol Chem, Jun 2015
We previously identified Treponema pallidum repeat proteins TprC/D, TprF, and TprI as candidate outer membrane proteins (OMPs) and subsequently demonstrated that TprC is not only a rare OMP but also forms trimers and has porin activity.
Structural basis for the recognition of the scaffold protein Frmpd4/Preso1 by the TPR domain of the adaptor protein LGN.
New
Sumimoto et al., Fukuoka, Japan. In Acta Crystallogr Sect F Struct Biol Commun, Feb 2015
Comparison with the previously determined structures of the LGN-Frmpd1, LGN-mInsc and LGN-NuMA complexes reveals that these partner proteins interact with LGN TPR1-6 via a common core binding region with consensus sequence (E/Q)XEX4-5(E/D/Q)X1-2(K/R)X0-1(V/I).
A Faster Triphosphorylation Ribozyme.
Müller et al., San Diego, United States. In Plos One, 2014
One ribozyme (TPR1) was analyzed in more detail.
Plasmodium falciparum Hop (PfHop) Interacts with the Hsp70 Chaperone in a Nucleotide-Dependent Fashion and Exhibits Ligand Selectivity.
Shonhai et al., Thohoyandou, South Africa. In Plos One, 2014
This method allowed us to observe that TPR1 and TPR2B subdomains of PfHop bind preferentially to the C-terminus of PfHsp70-1 compared to PfHsp90.
Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules.
Buchner et al., Garching bei München, Germany. In Nat Commun, 2014
The protein exhibits one binding site for Hsp90 (TPR2A) and two binding sites for Hsp70 (TPR1 and TPR2B).
Role of VPAC2 receptor in monocrotaline-induced pulmonary hypertension in rats.
Goto et al., Yokohama, Japan. In J Appl Physiol, 2014
We examined hemodynamic changes in right ventricular systolic pressure (RVSP), systemic blood pressure (SBP), total pulmonary resistance index (TPRI), total systemic resistance index, and cardiac index (CI) in response to their agonists with monocrotaline (MCT)-induced PH and explored involvement of VIP/PACAP expression and receptors in PH.
NLR-associating transcription factor bHLH84 and its paralogs function redundantly in plant immunity.
Li et al., Vancouver, Canada. In Plos Pathog, 2014
Together with previous finding that SNC1 associates with repressor TPR1 to repress negative regulators, we hypothesize that nuclear NLR proteins may interact with both transcriptional repressors and activators during immune responses, enabling potentially faster and more robust transcriptional reprogramming upon pathogen recognition.
The hop-like stress-induced protein 1 cochaperone is a novel cell-intrinsic restriction factor for mitochondrial tombusvirus replication.
Nagy et al., Lexington, United States. In J Virol, 2014
Overexpression of Sti1p derivatives in yeast reveals that the inhibitory function depends on the TPR1 domain known to interact with heat shock protein 70 (Hsp70), but not on the TPR2 domain interacting with Hsp90.
The assembly and intermolecular properties of the Hsp70-Tomm34-Hsp90 molecular chaperone complex.
Vojtesek et al., Brno, Czech Republic. In J Biol Chem, 2014
We found that Tomm34 TPR1 domain specifically binds Hsp70.
ATPase activity and ATP-dependent conformational change in the co-chaperone HSP70/HSP90-organizing protein (HOP).
Itoh et al., Akita, Japan. In J Biol Chem, 2014
Analysis of deletion mutants revealed that the ATPase domain of HOP is in the N-terminal TPR1-DP1-TPR2A segment.
TOPLESS mediates brassinosteroid-induced transcriptional repression through interaction with BZR1.
Wang et al., Stanford, United States. In Nat Commun, 2013
A triple tpl mutant (tpl;tpr1;tpr4) shows reduced BR sensitivity and suppresses the gain-of-function bzr1-1D mutant phenotype.
A pollen-specific calmodulin-binding protein, NPG1, interacts with putative pectate lyases.
Reddy et al., Fort Collins, United States. In Sci Rep, 2013
A truncated form of AtNPG1 lacking the N-terminal tetratricopeptide repeat 1 (TPR1) failed to interact with PLLs, suggesting that it is essential for NPG1 interaction with PLLs.
Molecular evolution of NASP and conserved histone H3/H4 transport pathway.
Fillingham et al., Toronto, Canada. In Bmc Evol Biol, 2013
Our data indicate that TPR1 and TPR4 constitute the most rapidly evolving functional units of NASP and may account for the functional diversity observed among well characterized family members.
Gα16 interacts with tetratricopeptide repeat 1 (TPR1) through its β3 region to activate Ras independently of phospholipase Cβ signaling.
GeneRIF
Wong et al., Hong Kong, Hong Kong. In Bmc Struct Biol, 2010
beta3 region of Galpha16 is essential for interaction with TPR1 and the subsequent activation of Ras
Cooperative interaction of Hsp40 and TPR1 with Hsp70 reverses Hsp70-HspBp1 complex formation.
GeneRIF
Song et al., Suwŏn, South Korea. In Mol Cells, 2003
Results report cooperative interactions involving Hsp70, Hsp40, and TPR1 that enhance Hsp70-dependent folding of chemically denatured substrates.
Identification of tetratricopeptide repeat 1 as an adaptor protein that interacts with heterotrimeric G proteins and the small GTPase Ras.
GeneRIF
Ye et al., Chicago, United States. In Mol Cell Biol, 2003
Data show that tetratricopeptide repeat 1 is a novel adaptor protein for Ras and selected Galpha proteins that may be involved in protein-protein interaction relating to G-protein signaling.
Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine.
Impact
Moarefi et al., Martinsried, Germany. In Cell, 2000
The TPR1 domain of Hop specifically recognizes the C-terminal heptapeptide of Hsp70 while the TPR2A domain binds the C-terminal pentapeptide of Hsp90.
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