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RBCC specifications

Information


Unique identifier OMICS_21331
Name RBCC
Alternative name Red Blood Cell Collection
Restrictions to use None
Database management system MySQL
Community driven No
Data access Browse
User data submission Not allowed
Maintained Yes

Maintainers


  • person_outline Tamas Hegedus
  • person_outline Bruno Stieger

Publication for Red Blood Cell Collection

RBCC citations

 (8)
library_books

Cyclophilin A potentiates TRIM5α inhibition of HIV 1 nuclear import without promoting TRIM5α binding to the viral capsid

2017
PLoS One
PMCID: 5540582
PMID: 28767697
DOI: 10.1371/journal.pone.0182298

[…] TRIMCyp is a closely related family member of TRIM5α []. TRIMCyp, which consists of the RBCC domains of TRIM5α, but has CypA in place of the SPRY domain, was first identified in an owl monkey kidney cell line (OMK) but was later detected in some rhesus monkey subspecies, suggesting that […]

call_split

Functional role of TRIM E3 ligase oligomerization and regulation of catalytic activity

2016
PMCID: 4864278
PMID: 27154206
DOI: 10.15252/embj.201593741
call_split See protocol

[…] ns in the concentration range that gave a monodisperse molecular weight according to SEC‐MALLS. The data at SOLEIL were recorded over a momentum transfer range of 0.01–0.43 Å−1. The two purified TRIM RBCC constructs (2.5 mg/ml TRIM25 and 6 mg/ml TRIM32) were injected onto an SEC‐3 300 Å Agilent column and eluted at a flow rate of 0.2 mg/ml at 15°C. Frames were collected continuously during the fra […]

library_books

Mechanism of B box 2 domain mediated higher order assembly of the retroviral restriction factor TRIM5α

2016
eLife
PMCID: 4936894
PMID: 27253059
DOI: 10.7554/eLife.16309.031

[…] l capsids is reported to enhance E3 ligase activity (). The RING domain dimerizes to bind E2-Ub conjugates and catalyze Ub transfer (). So far, we have been unable to solve a crystal structure of the RBcc miniTRIM, but structures of monomeric (inactive) and dimeric (active) forms of the TRIM5α RING domain are both known (; ), and so we used molecular modeling to determine possible configurations o […]

library_books

An Evolutionary Screen Highlights Canonical and Noncanonical Candidate Antiviral Genes within the Primate TRIM Gene Family

2013
Genome Biol Evol
PMCID: 3845644
PMID: 24158625
DOI: 10.1093/gbe/evt163

[…] 2 (). TRIML2 is a highly unusual TRIM-like gene. It lacks canonical RING and B-box domains, being solely composed of Coiled-Coil and B30.2 domains. Formally, it does not meet the criteria of being an RBCC-type TRIM gene. However, given the propensity of TRIM proteins to homo- and heterodimerize, we also included such noncanonical genes within our analysis. We find a single site of positive selecti […]

library_books

Apparent effect of rabbit endogenous lentivirus type K acquisition on retrovirus restriction by lagomorph Trim5αs

2013
PMCID: 3758185
PMID: 23938750
DOI: 10.1098/rstb.2012.0498

[…] able to us, so the pika construct was prepared by amplifying exon8, containing the primary specificity determinants for retroviral restriction by TRIM5α [], from pika genomic DNA and fusing it to the RBCC domain of the European rabbit TRIM5α cDNA. Figure 2.These four clones were sequenced and compared with one another and other lagomorph TRIM5α sequences deposited in the NCBI and EBI databases. Th […]

library_books

Origin and Diversification of TRIM Ubiquitin Ligases

2012
PLoS One
PMCID: 3503706
PMID: 23185523
DOI: 10.1371/journal.pone.0050030

[…] ction; 3) A final type of discrepancy was the finding of proteins with very high similarity to TRIMs but that could not be classified as bona fide TRIM proteins, given that they did not have complete RBCC supradomains. These TRIM-like proteins are also discussed in detail in the next section.At this point, the diversity of TRIM sequences in human, mouse, Drosophila melanogaster and Caenorhabditis […]

Citations

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RBCC institution(s)
MTA-SE Molecular Biophysics Research Group, Hungarian Academy of Sciences, Budapest, Hungary; Department of Biophysics and Radiation Biology, Semmelweis University, Budapest, Hungary; Department of Clinical Pharmacology and Toxicology, University Hospital Zurich, Zurich, Switzerland; Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary; Functional Genomics Center Zurich, University of Zurich, ETH Zurich, Zurich, Switzerland
RBCC funding source(s)
Supported by the OTKA 83533, KTIA-AIK-12-2012-0025, OTKA K111678, and Bolyai Fellowship of the Hungarian Academy of Sciences; Grant 310030_144195 from the Swiss National Science Foundation.

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