| Name | ubiquitin |
|---|---|
| Synonyms | HMG20; RPS27A; UBA80; UBCEP 1; UBCEP1; UBA52; UBCEP 2; UBCEP2… |
| Name | mercuric chloride |
|---|---|
| CAS |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 10748083 | Chen A, Wu K, Fuchs SY, Tan P, Gomez C, Pan ZQ: The conserved RING-H2 finger of ROC1 is required for ubiquitin ligation. J Biol Chem. 2000 May 19;275(20):15432-9. Mercury-containing sulfhydryl modification agents (rho-hydroxymercuribenzoate and mercuric chloride) irreversibly inhibit the ROC1-CUL1 ubiquitin ligase activity without disrupting the complex. |
35(0,1,1,5) | Details |
| 11901211 | Furuchi T, Hwang GW, Naganuma A: Overexpression of the ubiquitin-conjugating enzyme Cdc34 confers resistance to methylmercury in Saccharomyces cerevisiae. Mol Pharmacol. 2002 Apr;61(4):738-41. Yeast strains transformed with the CDC34 gene were resistant not only to methylmercury but also to mercuric chloride and p-chloromercuribenzoate. |
4(0,0,0,4) | Details |
| 8392481 | Buller JR, Rossi ML: Immunocytochemistry on paraffin wax Golgi-Cox impregnated central nervous tissue. Funct Neurol. 1993 Mar-Apr;8(2):135-51. Sections of normal and pathological brain and spinal cord, from both Golgi-Cox impregnated tissue and for comparison saline fixed tissue, were studied with the following antibodies: glial fibrillary acidic protein, myelin basic protein, neurofilament, neurone specific enolase, protein gene product 9.5, ubiquitin and vimentin. |
1(0,0,0,1) | Details |
| 8680303 | Didierjean L, Frendo P, Nasser W, Genot G, Marivet J, Burkard G: Heavy-metal-responsive genes in maize: identification and comparison of their expression upon various forms of abiotic stress. Planta. 1996;199(1):1-8. To identify genes involved in defense against heavy-metal stresses, a cDNA library originating from mercuric chloride-treated maize (Zea mays L. cv. Heat-shock protein was mainly induced by heat and cold, and ubiquitin by wounding. |
1(0,0,0,1) | Details |
| 12388758 | Chen M, Rockel T, Steinweger G, Hemmerich P, Risch J, von Mikecz A: Subcellular recruitment of fibrillarin to nucleoplasmic proteasomes: implications for processing of a nucleolar autoantigen. Mol Biol Cell. 2002 Oct;13(10):3576-87. Because proteasomes are absent from the nucleolus, a recruitment system was used to analyze the molecular fate of nucleolar protein fibrillarin: Subtoxic concentrations of mercuric chloride (HgCl (2)) induce subcellular redistribution of fibrillarin and substantial colocalization (33%) with nucleoplasmic proteasomes in different cell lines and in primary cells isolated from mercury-treated mice. Accumulation of fibrillarin and fibrillarin-ubiquitin conjugates in lactacystin-treated cells suggests that proteasome-dependent processing of this autoantigen occurs upon mercury induction. |
1(0,0,0,1) | Details |