Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P62988 (Ubiquitin)
 4,326 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Ubiquitin is a small, 8 kD protein found in all eukaryotic cells. It is involved in a wide variety of regulatory roles within the cell, including gene expression, ribosome biosynthesis, receptor expression, and the stress response. The best understood of these is that of ubiquitin-mediated proteolysis, in which ubiquitin is covalently attached to specific protein target substrates that are then recognized and degraded by a high molecular weight protease.
 ...
PMID:Ubiquitin-mediated protein modification and degradation. 132 65

Immunohistochemical analysis of constituents of senile plaques and cerebro-vascular amyloid in the brain of aged dogs was performed using antisera against beta protein, cystatin C, ubiquitin, tau, and neurofilament (NF). All types of senile plaques and cerebro-vascular amyloid in aged dogs were labeled by anti-beta protein serum. Cystatin C immunoreactivity was detected in neuronal cell bodies, primitive or classical plaques, and amyloid deposited around cerebral capillaries, but not in diffuse plaques and amyloid deposited in the media tunica of cerebro-meningeal arterioles. Ubiquitin-positive granules distributed widely in both gray and white matter of aged dogs, while they were very small in number in young dogs. Swollen neurites-like materials in primitive plaques or classical plaques were immunoreactive for anti-ubiquitin serum. Tau immunostaining labeled commonly axons and several neuronal or glial cells after hydrate autoclave pretreatment. Tau-positive components were observed very rarely in the corona of classical plaques. Most of swollen neurites-like structures of primitive or classical plaques were not reactive for anti-NF serum, and only a few plaques contained small numbers of NF-positive elements.
 ...
PMID:Immunohistochemical analysis of constituents of senile plaques and cerebro-vascular amyloid in aged dogs. 132 97

We have characterized a second T. brucei polyubiquitin gene (UbB) that is highly similar in the coding and flanking regions to a previously described T. brucei polyubiquitin gene (UbA). However, UbB differs from UbA in 2 respects: (1) the predicted carboxy-terminal amino acid of UbB is methionine, as opposed to leucine in UbA, and (2) UbB contains approximately 13 ubiquitin repeats, as opposed to approximately 30 repeats in UbA. In Southern blots of intact T. brucei DNA separated by pulsed field gel electrophoresis, the polyubiquitin sequences have been shown to reside on band 19, which may contain 3 chromosomes. Three experiments that target a neomycin-resistance gene to the polyubiquitin locus demonstrate a one-to-one ratio of polyubiquitin 3-flanking sequences, which suggests that UbA and UbB are alleles rather than duplications. Four additional strains of T. brucei and one strain of T. equiperdum show variation in their polyubiquitin gene size, suggesting that this is a common polymorphism.
 ...
PMID:Allelic polymorphism of the Trypanosoma brucei polyubiquitin gene. 133 86

Ubiquitin adopts a non-native folded structure in 60% methanol solution at low pH. Two-dimensional nuclear magnetic resonance (2D NMR) was used to measure the hydrogen-exchange rates of backbone amide protons of ubiquitin in both native and methanol forms, and to characterize the structure of ubiquitin in the methanol state. Protection factors (the ratios of experimentally determined exchange rates to the rates calculated for an unfolded polypeptide) for protons in the native form of ubiquitin range from less than 10 to greater than 10(5). Most of the protons that are protected from exchange are located in regions of hydrogen-bonded secondary structure. The most strongly protected backbone amide protons are those of residues comprising the hydrophobic core. Hydrogen exchange from ubiquitin in methanol solution was too rapid to measure directly by 2D NMR, so a labeling scheme was employed, in which exchange with solvent occurred while the protein was in methanol solution. Exchange was quenched by dilution with aqueous buffer after the desired labeling time, and proton occupancies were measured by 1H NMR of the native form of the protein. Protection factors for protons in the methanol form of ubiquitin range from 2.6 to 42, with all protected protons located in hydrogen-bonded structure in the native form. Again, the most strongly protected protons are those of residues in the hydrophobic core. Comparison of the patterns of the hydrogen-exchange rates in the native and methanol forms indicates that almost all of the native secondary structure persists in the methanol form, but that it is almost uniformly destabilized by 4-6 kcal/mol.(ABSTRACT TRUNCATED AT 250 WORDS)
 ...
PMID:Hydrogen exchange in native and alcohol forms of ubiquitin. 133 57

Ubiquitin-positive intraneuronal inclusions were found in the extramotor cortices of ten presenile dementia patients with motor neuron disease. There were inclusions in the hippocampal granular cells and in the small neurons of the superficial layers of the temporal and frontal cortices. Bunina bodies were present in the anterior horn cells in all cases. These results suggest that ubiquitin-related cytoskeletal abnormalities are common in cerebral non-motor small neurons in these patients.
 ...
PMID:Ubiquitin-positive intraneuronal inclusions in the extramotor cortices of presenile dementia patients with motor neuron disease. 133 7

A lambda gt 11 cDNA library, constructed from poly(A)+ mRNA isolated from Avena fatua aleurone layers incubated with 1 microM gibberellin A1 (GA1) for 4 days, was screened with an anti-idiotypic antiserum raised against the GA-specific monoclonal antibody MAC 182. One positive clone was isolated, sequenced and shown to encode a tetraubiquitin based on the deduced amino acid sequence. This polyubiquitin cDNA exhibited a high degree of homology to a cloned wheat hexaubiquitin in its 3'-non-coding region. Analysis of total RNA isolated from A. fatua aleurone layers, treated without or with a range of concentrations of GA1 from 10(-11) to 10(-6) M, by northern blotting using the cDNA probe revealed 8 different ubiquitin-containing transcript classes all of which are constitutively expressed in aleurone and are regulated by GA1.
 ...
PMID:cDNA cloning of a tetraubiquitin gene, and expression of ubiquitin-containing transcripts, in aleurone layers of Avena fatua. 133 96

Western blot analysis, using a polyclonal antibody to the 240-kDa endogenous inhibitor of the 20 S proteasome, revealed that the inhibitor is a component of the 26 S complex. Although isolated inhibitor displayed a single 40-kDa band on SDS-PAGE, the antibody detected a 55-kDa component in the 26 S proteasome complex. Ubiquitin polyclonal antibody recognized the same 55-kDa component but did not react with free 40-kDa inhibitor subunit. Addition of purified 40-kDa inhibitor to a ubiquitin ligating system also generated the 55-kDa species. In crude erythrocyte extracts, most of the inhibitor migrated at 55 kDa in the presence of ATP but shifted to 40 kDa in the absence of ATP, consistent with removal of ubiquitin. It is suggested that ubiquitination of the inhibitor may be involved in regulating assembly and/or activity of the 26 S proteasome complex.
 ...
PMID:Ubiquitinated proteasome inhibitor is a component of the 26 S proteasome complex. 133 90

Young sympathetic neurons die when deprived of nerve growth factor (NGF). Under such circumstances, cell death is appropriate to the developing nervous system and requires RNA and protein synthesis. We have hypothesized the existence of an endogenous death program within neurons that is suppressed by trophic factors. The extent and timing of required changes in the synthetic events that comprise the death program are unknown. In an effort to characterize the biochemical events that mediate the death program further, we performed several experiments on embryonic rat sympathetic neurons in vitro. The death program was blocked with cycloheximide when total protein synthesis was inhibited > or = 80%. When protein synthesis was inhibited within 22 +/- 4 h of NGF deprivation, death was prevented in half the neurons. Hence, we define the commitment point for protein synthesis to be 22 +/- 4 h. Analogously, the commitment point for RNA synthesis was 26 +/- 4 h and that for NGF rescue, 24 +/- 4 h. We tested the ability of a wide variety of chemicals to interfere with the death program. Most compounds tested were unable to prevent neuronal death. Some treatments, however, did save NGF-deprived neurons and were subsequently characterized. These included ultraviolet light and agents that raise intracellular concentrations of cAMP. Finally, we looked for the neuronal expression in vitro and in vivo of genes that have been associated with programmed death in other cell types, including TRPM-2/SGP-2, polyubiquitin, TGF beta-1, c-fos, and c-myc. None of these genes showed significant activation associated with neuronal death.
 ...
PMID:Biochemical characterization of programmed cell death in NGF-deprived sympathetic neurons. 133 32

Ubiquitin, an 8.5 kDa polypeptide found almost universally in plants and animals, is a normal component in the lens. The best documented function for ubiquitin involves its conjugation to proteins as a signal to initiate degradation. Conjugates for ubiquitin-dependent degradation tend to be of very high molecular mass and are rapidly degraded. Another role of ubiquitin conjugation may be as a stabilizer during stress for protection of constituent proteins, resulting in ubiquitin conjugates that are long-lived. Examination of clear and cataractous human lenses of < 1 to > 50 years revealed the dramatic accumulation of ubiquitin and ubiquitin conjugates with age, beginning at approximately 10 years. Epithelial tissue contained predominantly conjugates of > 250 kDa, although ubiquitin conjugates were found at 98 and 40-60 kDa in tissues from older donors. The water-soluble, urea-soluble and urea-insoluble fractions of lens cortex and core also contain ubiquitin conjugates that accrue with age. High molecular mass conjugates (> 250 kDa) are particularly prominent in older lens tissue. Cataractous lenses, as compared with normal lenses of the same age, show more of these high molecular mass conjugates in the urea-soluble and urea-insoluble fractions of cortex and core. Heterogeneous conjugates in the 20-85 kDa range accumulate in an age-related fashion in all lens cortex and core fractions. While levels of free ubiquitin are significant in the epithelium and the water-soluble cortex and core for all ages, there is no detectable free ubiquitin in the urea-soluble and urea-insoluble fraction under conditions used in this study.(ABSTRACT TRUNCATED AT 250 WORDS)
 ...
PMID:Ubiquitin and ubiquitin conjugates in human lens. 133 33

Ubiquitin has been isolated and purified from rabbit brain using gel permeation and reverse-phase high-performance liquid chromatography. The 76-residue protein exhibits one difference towards a murine form, is identical to other characterized vertebrate ubiquitins, and confirms an extensive conservation of the ubiquitin structure. No positional microheterogeneities were detectable between two sub-forms.
 ...
PMID:Structural characterization of rabbit brain ubiquitin. 133 7


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>