8u2c: Difference between revisions

No edit summary
No edit summary
 
Line 7: Line 7:
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8u2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8u2c OCA], [https://pdbe.org/8u2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8u2c RCSB], [https://www.ebi.ac.uk/pdbsum/8u2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8u2c ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8u2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8u2c OCA], [https://pdbe.org/8u2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8u2c RCSB], [https://www.ebi.ac.uk/pdbsum/8u2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8u2c ProSAT]</span></td></tr>
</table>
</table>
== Function ==
<div style="background-color:#fffaf0;">
[https://www.uniprot.org/uniprot/ABCG2_HUMAN ABCG2_HUMAN] High-capacity urate exporter functioning in both renal and extrarenal urate excretion. Plays a role in porphyrin homeostasis as it is able to mediates the export of protoporhyrin IX (PPIX) both from mitochondria to cytosol and from cytosol to extracellular space, and cellular export of hemin, and heme. Xenobiotic transporter that may play an important role in the exclusion of xenobiotics from the brain. Appears to play a major role in the multidrug resistance phenotype of several cancer cell lines. Implicated in the efflux of numerous drugs and xenobiotics: mitoxantrone, the photosensitizer pheophorbide, camptothecin, methotrexate, azidothymidine (AZT), and the anthracyclines daunorubicin and doxorubicin.<ref>PMID:12958161</ref> <ref>PMID:20705604</ref> <ref>PMID:22132962</ref> <ref>PMID:23189181</ref>  
== Publication Abstract from PubMed ==
Cryogenic electron microscopy is widely used in structural biology, but its resolution is often limited by the dynamics of the macromolecule. Here we developed a refinement protocol based on Gaussian mixture models that integrates particle orientation and conformation estimation and improves the alignment for flexible domains of protein structures. We demonstrated this protocol on multiple datasets, resulting in improved resolution and resolvability, locally and globally, by visual and quantitative measures.
 
Improving resolution and resolvability of single-particle cryoEM structures using Gaussian mixture models.,Chen M, Schmid MF, Chiu W Nat Methods. 2024 Jan;21(1):37-40. doi: 10.1038/s41592-023-02082-9. Epub 2023 Nov , 16. PMID:37973972<ref>PMID:37973972</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8u2c" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA