| scholarly article | Q13442814 |
| P5530 | Altmetric DOI | 10.1107/S0907444913012687 |
| P6179 | Dimensions Publication ID | 1047170956 |
| P356 | DOI | 10.1107/S0907444913012687 |
| P953 | full work available at URL | http://eprints.whiterose.ac.uk/79623/ |
| https://doi.org/10.1107/S0907444913012687 | ||
| P3181 | OpenCitations bibliographic resource ID | 4823046 |
| P698 | PubMed publication ID | 23999291 |
| P1154 | Scopus EID | 2-s2.0-84883577909 |
| P50 | author | Mark Alexander Stead | Q42551707 |
| Stephen Carr | Q73227445 | ||
| P2093 | author name string | Stephanie C Wright | |
| Gareth O Rosbrook | |||
| Helen J Close | |||
| Simon D Connell | |||
| Christopher M Harrison | |||
| Laura K van Geersdaele | |||
| P2860 | cites work | Drug discovery in the ubiquitin-proteasome system. | Q36525810 |
| Analysis of Drosophila segmentation network identifies a JNK pathway factor overexpressed in kidney cancer. | Q37373844 | ||
| Multiple Ser/Thr-rich degrons mediate the degradation of Ci/Gli by the Cul3-HIB/SPOP E3 ubiquitin ligase | Q37482039 | ||
| ARP/wARP and molecular replacement: the next generation | Q38606646 | ||
| Evolutionary expansion of SPOP and associated TD/POZ gene family: impact of evolutionary route on gene expression pattern | Q39713863 | ||
| The N-terminal POZ domain of GAGA mediates the formation of oligomers that bind DNA with high affinity and specificity | Q47070730 | ||
| BTB domain-containing speckle-type POZ protein (SPOP) serves as an adaptor of Daxx for ubiquitination by Cul3-based ubiquitin ligase | Q53633362 | ||
| [4] Combining constraints for electron-density modification | Q56877908 | ||
| Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex | Q24294734 | ||
| Breast cancer metastasis suppressor 1 (BRMS1) is destabilized by the Cul3-SPOP E3 ubiquitin ligase complex | Q24297410 | ||
| Tumor-suppressor role for the SPOP ubiquitin ligase in signal-dependent proteolysis of the oncogenic co-activator SRC-3/AIB1 | Q24303428 | ||
| Adaptor protein self-assembly drives the control of a cullin-RING ubiquitin ligase | Q24336527 | ||
| SuperPose: a simple server for sophisticated structural superposition | Q24562032 | ||
| Exome sequencing identifies recurrent SPOP, FOXA1 and MED12 mutations in prostate cancer | Q24616117 | ||
| MolProbity: all-atom structure validation for macromolecular crystallography | Q24649111 | ||
| Sequence and structural analysis of BTB domain proteins | Q24812693 | ||
| A short history of SHELX | Q25938995 | ||
| Structures of SPOP-Substrate Complexes: Insights into Molecular Architectures of BTB-Cul3 Ubiquitin Ligases | Q27657740 | ||
| Structural Basis of the 9-Fold Symmetry of Centrioles | Q27666762 | ||
| Structural Basis for Cul3 Protein Assembly with the BTB-Kelch Family of E3 Ubiquitin Ligases | Q27675990 | ||
| Inference of macromolecular assemblies from crystalline state | Q27860457 | ||
| XDS | Q27860472 | ||
| Substructure solution with SHELXD | Q27860593 | ||
| REFMAC5 for the refinement of macromolecular crystal structures | Q27860905 | ||
| Phasercrystallographic software | Q27860930 | ||
| Features and development of Coot | Q27861079 | ||
| Scaling and assessment of data quality | Q27861107 | ||
| Identification of a novel nuclear speckle‐type protein, SPOP | Q28118699 | ||
| MacroH2A1.2 binds the nuclear protein Spop | Q28218285 | ||
| The ubiquitin code | Q28265104 | ||
| Presenting your structures: the CCP4mg molecular-graphics software | Q29547443 | ||
| Keap1 is a forked-stem dimer structure with two large spheres enclosing the intervening, double glycine repeat, and C-terminal domains | Q33734064 | ||
| Structural assembly of cullin-RING ubiquitin ligase complexes | Q34762436 | ||
| Cullin-based ubiquitin ligases: Cul3-BTB complexes join the family. | Q35740993 | ||
| The BACK domain in BTB-kelch proteins. | Q35950674 | ||
| P433 | issue | Pt 9 | |
| P304 | page(s) | 1677-1684 | |
| P577 | publication date | 2013-08-15 | |
| P1433 | published in | Acta Crystallographica Section D: Biological Crystallography | Q1933255 |
| P1476 | title | Structural basis of high-order oligomerization of the cullin-3 adaptor SPOP | |
| P478 | volume | 69 |
| Q35080292 | Biophysical studies on interactions and assembly of full-size E3 ubiquitin ligase: suppressor of cytokine signaling 2 (SOCS2)-elongin BC-cullin 5-ring box protein 2 (RBX2). |
| Q57029699 | Cancer Mutations of the Tumor Suppressor SPOP Disrupt the Formation of Active, Phase-Separated Compartments |
| Q47413250 | Functional analysis of Cullin 3 E3 ligases in tumorigenesis. |
| Q37011857 | Higher-order oligomerization promotes localization of SPOP to liquid nuclear speckles |
| Q36782739 | Multiple Weak Linear Motifs Enhance Recruitment and Processivity in SPOP-Mediated Substrate Ubiquitination |
| Q34637940 | Prostate cancer. Ubiquitylome analysis identifies dysregulation of effector substrates in SPOP-mutant prostate cancer |
| Q91713061 | SPOP and cancer: a systematic review |
| Q41836192 | Speckle-type POZ protein, SPOP, is involved in the DNA damage response. |
| Q34043797 | Targeting Cullin-RING E3 ubiquitin ligases for drug discovery: structure, assembly and small-molecule modulation |
| Q92413024 | The emerging role of SPOP protein in tumorigenesis and cancer therapy |
| Q34430637 | The emerging role of speckle-type POZ protein (SPOP) in cancer development |
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