Ubiquitin (from bovine erythrocytes)
Ubiquitin (from bovine erythrocytes) structure
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Common Name | Ubiquitin (from bovine erythrocytes) | ||
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| CAS Number | 79586-22-4 | Molecular Weight | N/A | |
| Density | N/A | Boiling Point | N/A | |
| Molecular Formula | N/A | Melting Point | N/A | |
| MSDS | USA | Flash Point | N/A | |
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Export-deficient monoubiquitinated PEX5 triggers peroxisome removal in SV40 large T antigen-transformed mouse embryonic fibroblasts.
Autophagy 11 , 1326-40, (2015) Peroxisomes are ubiquitous cell organelles essential for human health. To maintain a healthy cellular environment, dysfunctional and superfluous peroxisomes need to be selectively removed. Although emerging evidence suggests that peroxisomes are mainly degrad... |
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Insights into Ubiquitination from the Unique Clamp-like Binding of the RING E3 AO7 to the E2 UbcH5B.
J. Biol. Chem. 290 , 30225-39, (2015) RING proteins constitute the largest class of E3 ubiquitin ligases. Unlike most RINGs, AO7 (RNF25) binds the E2 ubiquitin-conjugating enzyme, UbcH5B (UBE2D2), with strikingly high affinity. We have defined, by co-crystallization, the distinctive means by whic... |
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Stimulation of ATP-dependent proteolysis requires ubiquitin with the COOH-terminal sequence Arg-Gly-Gly.
J. Biol. Chem. 256 , 9235-9241, (1981) It was previously shown that ubiquitin is very similar to the polypeptide cofactor of the ATP-dependent protein degradation system from rabbit reticulocytes (Wilkinson, K. D., Urban, M. K., and Haas, A. L. (1980) J. Biol. Chem. 255, 7529-7532). We have extend... |
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The ubiquitin system for protein degradation.
Annu. Rev. Biochem. 61 , 761-807, (1992)
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The ubiquitin-proteasome pathway and pathogenesis of human diseases.
Annu. Rev. Med. 50 , 57-74, (1999) The ubiquitin-proteasome pathway plays a pivotal role in the degradation of short-lived and regulatory proteins important in a variety of basic cellular processes, including regulation of the cell cycle, modulation of cell surface receptors and ion channels, ... |
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Structure and functions of the 20S and 26S proteasomes.
Annu. Rev. Biochem. 65 , 801, (1996) The proteasome is an essential component of the ATP-dependent proteolytic pathway in eukaryotic cells and is responsible for the degradation of most cellular proteins. The 20S (700-kDa) proteasome contains multiple peptidase activities that function through a... |
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Changes in the ratio of free NEDD8 to ubiquitin triggers NEDDylation by ubiquitin enzymes.
Biochem. J. 441 , 927-36, (2012) Ubiquitin and UBL (ubiquitin-like) modifiers are small proteins that covalently modify other proteins to alter their properties or behaviours. Ubiquitin modification (ubiquitylation) targets many substrates, often leading to their proteasomal degradation. NED... |
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The UBAP1 subunit of ESCRT-I interacts with ubiquitin via a SOUBA domain.
Structure 20 , 414-28, (2012) The endosomal sorting complexes required for transport (ESCRTs) facilitate endosomal sorting of ubiquitinated cargo, MVB biogenesis, late stages of cytokinesis, and retroviral budding. Here we show that ubiquitin associated protein 1 (UBAP1), a subunit of hum... |
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Quantitative measurement of intact alpha-synuclein proteoforms from post-mortem control and Parkinson's disease brain tissue by intact protein mass spectrometry.
Sci. Rep. 4 , 5797, (2014) A robust top down proteomics method is presented for profiling alpha-synuclein species from autopsied human frontal cortex brain tissue from Parkinson's cases and controls. The method was used to test the hypothesis that pathology associated brain tissue will... |
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Structural basis for the RING-catalyzed synthesis of K63-linked ubiquitin chains.
Nat. Struct. Mol. Biol. 22 , 597-602, (2015) RING E3 ligase-catalyzed formation of K63-linked ubiquitin chains by the Ube2V2-Ubc13 E2 complex is required in many important biological processes. Here we report the structure of the RING-domain dimer of rat RNF4 in complex with a human Ubc13∼Ub conjugate a... |