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The role of NuMA in the interphase nucleus. Paper-1315363.
The interaction with NuMA persists during interphase. Paper-8882923.
No NuMA-positive neurons were found in the hippocampus. Paper-8563033.
No NuMA staining was detected in enucleated pig oocytes. Paper-11337732.
NuMA is required for the proper completion of mitosis. Paper-82708.
Comprehensive analysis of NuMA variation in breast cancer. Paper-12780471.
Does NuMA have a scaffold function in the interphase nucleus? Paper-2091178.
Cleavage of the nuclear matrix protein NuMA during apoptosis. Paper-1040790.
NuMA, a nuclear protein involved in mitosis and nuclear reformation. Paper-7970256.
NuMA and nuclear lamins behave differently in Fas-mediated apoptosis. Paper-9802270.
NuMA cleavage is likely to be a consequence of the onset of apoptosis. Paper-738826.
Phosphorylation is thought to play a regulatory role in NuMA function. Paper-501467.
In unfertilized porcine oocytes, NuMA is localized to the meiotic spindle. Paper-11337732.
NuMA is an essential protein for the formation of spindle poles in mitosis. Paper-1315363.
Localization of NuMA protein isoforms in the nuclear matrix of mammalian cells. Paper-8169281.
This suggests that NuMA may be a nonessential component of the interphase nucleus. Paper-2196279.
Phosphorylation regulates the assembly of NuMA in a mammalian mitotic extract. Paper-1152259.
In interphase, NuMA behaves solely as a 220 kDa nuclear matrix-associated protein. Paper-738826.
Dynamic changes in NuMA and microtubules in monkey-rabbit nuclear transfer embryos. Paper-11337711.
NuMA influences higher order chromatin organization in human mammary epithelium. Paper-13099338.
Here we have studied the fate of NuMA in Fas-treated apoptotic Jurkat T and HeLa cells. Paper-9802270.
Assignment of the nuclear mitotic apparatus protein NuMA gene to human chromosome 11q13. Paper-7901352.
NuMA is required for the organization of microtubules into aster-like mitotic arrays. Paper-409235.
NuMA: evaluation of a new biomarker for the detection of low stage colorectal cancer. Paper-1987978.
Association of the NuMA region on chromosome 11q13 with breast cancer susceptibility. Paper-11198898.
NuMA also functions during meiotic spindle organization in male and female germ cells. Paper-10564670.
Thus, NuMA is required for persistence of the KSHV episomes in daughter cells. Paper-12826766.
Phosphorylation of NUMA occurs during nuclear breakdown and not mitotic spindle assembly. Paper-501467.
Intermediate filament proteins with nuclear functions: NuMA, lamin-like proteins and MFP1. Paper-10017682.
Similar to NuMA, a significant amount of cohesin was found to associate with the nuclear matrix. Paper-8882923.
Antibodies to Mitotic Spindle Apparatus: Clinical Significance of NuMA and HsEg5 Autoantibodies. Paper-12756978.
The intact 220 kDa NuMA functions in interphase cells to retain the nuclear structural integrity. Paper-738826.
In cell culture, 95% of all cell profiles were human nuclear matrix antigen ( NuMA) positive. Paper-8680906.
NuMA relocalized to foci, which coalesced into larger assemblies as morphogenesis progressed. Paper-1681345.
Our results suggest that NuMA organises the poles by stable crosslinking of the microtubule fibers. Paper-9580774.
During mitosis, NuMA forms aggregates that interact with microtubules and certain motor proteins. Paper-2098106.
NuMA is a nuclear matrix protein in interphase and relocates to the spindle poles in mitotis. Paper-1835865.
Inhibition of NuMA or dynein allows completion of mitosis, despite inducing spindle pole abnormalities. Paper-10426998.
Additionally, NuMA appears to act as a nuclear structural target for a death protease during apoptosis. Paper-738826.
These results together indicate that the NuMA gene is present as a single copy on human chromosome 11q13. Paper-7901352.
Of these 56, NuMA-1 was found in 23, NuMA-2 in 7, CE in 20, CENP-F in 5, and CENP-F/ centrosome in 1 case. Paper-12240188.
CONCLUSION: Our results do not support the role of NuMA variants as breast cancer susceptibility alleles. Paper-12780471.
Experiments on cultured myoblasts indicated that NuMA is degraded during muscle cell differentiation. Paper-1315363.
The protein NuMA localizes to mitotic spindle poles where it contributes to the organization of microtubules. Paper-10426998.
NuMA is a cell cycle-related protein essential for normal mitosis that is degraded in early apoptosis. Paper-11198898.
NuMA is a nuclear matrix protein that has an essential function in the organization of the mitotic spindle. Paper-9802270.
Without centrosomes and NuMA, initial establishment of spindle microtubule focusing completely fails. Paper-13656722.
NuMA is a nuclear matrix protein in interphase and distributes to the spindle poles during mitosis. Paper-12556252.
But, it has also been reported that NuMA can organize microtubules in the absence of centrosomes and dynein. Paper-10564670.
In this study, NuMA phosphorylation was examined through the cell cycle using highly synchronized cells. Paper-501467.
In this study, we demonstrate that NuMA loses its stable association with the spindle poles after anaphase onset. Paper-10426998.
The changes in the spatial distribution of NuMA strongly resembled those described to occur during apoptosis. Paper-8847456.
Nuclear-mitotic apparatus protein: a structural protein interface between the nucleoskeleton and RNA splicing. Paper-7932259.
Caspase-3 cleaves NuMA at sites distinct from caspase-6, and mediates DNA fragmentation and chromatin condensation. Paper-1344543.
NuMA is a approximately 230 kDa structural protein that is present exclusively in the nucleus during interphase. Paper-2098106.
A marker for cell death in human cells is the solubilization and release of nuclear matrix proteins ( Numa). Paper-7914824.
In contrast, transient centrosome markers ( NuMA and centrophilin) were localized to all poles of multipolar spindles. Paper-879236.
During telophase NuMA relocates to electron-dense areas around chromatin and finally to the reconstituted nuclei. Paper-8915170.
Primary structure of NuMA, an intranuclear protein that defines a novel pathway for segregation of proteins at mitosis. Paper-7504935.
The nuclear/ mitotic apparatus protein NuMA is a component of the somatodendritic microtubule arrays of the neuron. Paper-2098106.
NuMA, a 238 kDa protein present in the nucleus during interphase, translocates to the spindle poles in mitosis. Paper-259789.
Results show that NuMA was localized in nuclei of 33.5% (163/456) of the serum-deprived fibroblasts used as donor cells. Paper-11337732.
NuMA is one member of a class of nuclear matrix proteins that resides in both the nucleus and mitotic apparatus. Paper-2138851.
Cleavage of a caspase-6-sensitive site at D(1705) produced the R-form, a major tail-less product of NuMA during apoptosis. Paper-12556252.
Degradation of NuMA results in the breakdown of normal nuclear structure, and has been used as a marker of cell apoptosis. Paper-10564670.
Here, we show that in mammary epithelial cells, NuMA is present in both the nuclear matrix and chromatin compartments. Paper-13099338.
During interphase, NuMA is transported into the nucleus where it resides until prometaphase of the next mitotic cycle. Paper-1315363.
Instead of binding to the mitotic spindle these mutant forms of NuMA concentrate at the plasma membrane of the mitotic cell. Paper-247203.
It is thought that the stable complex of NuMA/dynein/dynactin is needed to focus microtubule minus ends to the spindle poles. Paper-10564670.
In contrast, the 'kinase-dead' mut-Pim-1-GFP fusion protein did not co-localize with NuMA, and appeared to promote apoptosis. Paper-9285382.
The sequence for this protein was shown to be identical to that of NuMA, a 236-kDa nuclear mitotic spindle apparatus protein. Paper-7901352.
The cell-cycle-dependent phosphorylation of NuMA is regulated by the balanced activities of protein kinases and phosphatases. Paper-10564670.
NuMA is a component of the nuclear matrix in interphase cells and translocates to the spindle poles in mitosis. Paper-2091178.
These experiments indicate that microtubule assembly is essential for the NuMA protein to accumulate in the polar region. Paper-5186411.
While the function of NuMA is not known, it has been implicated in spindle organization during mitosis and nuclear reformation. Paper-501467.
RESULTS: Screening of NuMA resulted in identification of 11 exonic variants and 12 variants in introns or untranslated regions. Paper-12780471.
During apoptosis NuMA is redistributed within the nucleus and is proteolysed from a 238-kDa form to a 180- to 200-kDa form. Paper-1040790.
NuMA is a prominent component of interphase cell nuclear matrix but its role during interphase is largely unknown. Paper-2196279.
Thus, NuMA, a long coiled-coil protein, appears to have dual functions in interphase and mitosis during the cell cycle. Paper-8169281.
The nuclear-mitotic apparatus protein is important in the establishment and maintenance of the bipolar mitotic spindle apparatus. Paper-7381654.
We tested the significance of NuMA as tumour marker in colorectal cancer and also the sensitivity/specificity profile in general. Paper-1987979.
NuMA is a component of the nuclear matrix which may play a structural role in the architecture of the interphase nucleus. Paper-1040790.
Mutation of the predicted p34cdc2 phosphorylation sites in NuMA impair the assembly of the mitotic spindle and block mitosis. Paper-247203.
These results show for the first time that NuMA and lamins are specific target proteins during virus-induced programmed cell death. Paper-10402024.
The large coiled-coil protein NuMA plays an essential role in organizing microtubule minus ends at spindle poles in vertebrate cells. Paper-10647729.
So far, it is unclear how NuMA accumulates at the spindle poles following transport and how it remains associated throughout mitosis. Paper-9580774.
A functional relationship between NuMA and kid is involved in both spindle organization and chromosome alignment in vertebrate cells. Paper-9984385.
In mitosis, NuMA localises to spindle poles where it contributes to the formation and maintenance of focussed microtubule arrays. Paper-9580774.
The yeast two-hybrid system was used to identify binding partners of NuMA, a component of the nuclear matrix in interphase cells. Paper-8628564.
Immunofluorescence reveals a diffuse distribution of the animal NuMA homologues in plant nuclear core filaments in interphase. Paper-1752469.
Immunofluorescence studies of this hybrid cell showed that the distribution of NuMA protein is equivalent to that in human cells. Paper-3447376.
CHO3 also revealed extra cytoplasmic foci, whereas the SP-H antigen was additionally localized at one end of the free microtubule bundles. Paper-7145660.
The microtubule-associated SP-H antigen was insensitive to ATP extraction, but was removed from microtubules by treatment with 0.5 M NaCl. Paper-39818.
Essential role for the dimerization domain of NuMA-RARalpha in its oncogenic activities and localization to NuMA sites within the nucleus. Paper-9707885.
At prophase NuMA disperses in the cytoplasm and associates with microtubules while MPM-2 is uniformly distributed in the cytoplasm. Paper-8915170.
However, the NuMA protein is synthesized in a human/ Chinese hamster hybrid cell containing a reduced number of human chromosomes. Paper-3447376.
The NuMA Ala794Gly showed no difference in frequency in the unselected breast cancer case series or familial case series compared to control cases. Paper-12780471.
Mitotic asters assembled in this extract are composed of microtubules arranged in a radial array that contain NuMA concentrated at the central core. Paper-409235.
This occurs at the time of nuclear breakdown and eventually leads to an accumulation of the NuMA protein at the polar region of the mitotic spindle. Paper-5186411.
An enzyme immunoassay for NuMA was evaluated in a retrospective clinical study for its potential utility in the detection of colorectal cancer. Paper-1987978.
The plant nucleoskeleton: ultrastructural organization and identification of NuMA homologues in the nuclear matrix and mitotic spindle of plant cells. Paper-1752469.
NuMA antibody microinjection resulted in spindle disorganization and chromosome misalignment, but did not significantly affect early cleavage. Paper-11337711.
NuMA associates with microtubule motors during mitosis to perform an essential role in organizing microtubule minus ends at spindle poles. Paper-1847159.
NuMA, a coiled-coil protein related to intermediate filaments, found in animal cells, can also be detected in this plant nuclear matrix system. Paper-1752469.
Experiments are described that indicate several difficulties in studying the possible affinity and association of NuMA protein with mitotic chromosomes. Paper-4719073.
We show here that this process depends on directed NuMA transport toward microtubule minus ends powered by cytoplasmic dynein and its activator dynactin. Paper-10583009.
This NuMA-containing material is distinct from the peri-centriolar material and forms a matrix that appears to anchor microtubule ends at the spindle pole. Paper-1847159.
BACKGROUND: A recent genome wide case-control association study identified NuMA region on 11q13 as a candidate locus for breast cancer susceptibility. Paper-12780471.
NuMA seems to be preferentially cleaved by caspase-3 in vivo since it was not cleaved in staurosporine-treated caspase-3-null MCF-7 breast cancer cells. Paper-9802270.
Nuclear proteins of the bovine esophageal epithelium. II. The NuMA gene gives rise to multiple mRNAs and gene products reactive with monoclonal antibody W1. Paper-7788872.
As a result of these interactions, NuMA is thought to draw together the minus-ends of microtubules, thereby helping to organize them into a bipolar spindle. Paper-2098106.
NuMA is a 236 kDa protein that participates in the organization of the mitotic spindle despite its strict localization in the nucleus during interphase. Paper-896401.
Non-neoplastic cells cultured under conditions that prevent the establishment of apical polarity also enter the cell cycle upon NuMA antibody treatment. Paper-13198511.
At the onset of mitosis the NuMA protein redistributes from the nucleus to two centrosomal structures that later will become part of the mitotic spindle pole. Paper-5186411.
Transient overexpression of NuMA in HeLa cells induced the formation of a three-dimensional lattice with a quasihexagonal organization that fills the nucleus. Paper-2091178.
We used herpes simplex virus (HSV), an enveloped DNA virus that replicates in the nucleus, to study the intra-nuclear dynamics of NuMA in infected cells. Paper-12819813.
Kaposi's sarcoma-associated herpesvirus-encoded LANA can interact with the nuclear mitotic apparatus protein to regulate genome maintenance and segregation. Paper-12826766.
Together, these data support a central role for NuMA in both mitotic-spindle dynamics and the reformation of the daughter cell nuclei at the end of mitosis. Paper-7970256.
NuMA resides in the nucleus during interphase and becomes transiently associated with mitotic centrosomes after multiple steps of phosphorylations. Paper-8915170.
In our studies, overexpressed wild-type-Pim-1-GFP (green fluorescent protein) fusion protein was found to co-localize in the spindle pole with NuMA during mitosis. Paper-9285382.
Last, Western blotting analysis revealed that nuclear matrix proteins present in the granules are not proteolytically degraded except for the NuMA polypeptide. Paper-903675.
The sum of these findings demonstrate that NuMA function is required during mitosis for the terminal phases of chromosome separation and/or nuclear reassembly. Paper-82708.
NuMA has been recently characterized by two independent studies, and is thought to be part of a family of proteins that is required for the completion of mitosis. Paper-7901352.
Thus, NuMA is a defining feature of the mammalian spindle pole and functions as an essential tether linking bulk microtubules of the spindle to centrosomes. Paper-13656722.
Conditional expression of NuMA in a mouse myeloid cell line resulted in the induction of aneuploidy, cell cycle arrest in G(2)-M phases, and apoptosis. Paper-10028838.
Perturbation of histone acetylation in the acini by trichostatin A treatment altered chromatin structure, disrupted NuMA foci, and induced cell proliferation. Paper-1681345.
These results indicate that the NuMA proteins may be a structural component of the nucleus and may be involved in the early steps of nuclear reformation during telophase. Paper-7249299.
In intact cells labeled with 32P-orthophosphate, NuMA appeared as a 250 kDa phosphoprotein in interphase that shifted to a higher apparent molecular mass in mitosis. Paper-501467.
The NuMA-dynactin/dynein motor multiprotein complex not only explains the transport of NuMA along spindle fibers but also is linked to the process of microtubule focusing. Paper-9332310.
Fluorescent protein (FP) tagged nuclear matrix component protein ( NuMA), which was colocalized with ERalpha and PR-A/B, showed ATP-dependent rapid exchange in the nucleus. Paper-12668933.
These results show that the donor cell nucleus contains NuMA that is contributed to the reconstructed embryo and possibly activated by mechanisms in the oocyte's cytoplast. Paper-11337732.
The differential diagnosis of anti- NuMA-1-positive patients must include Sjögren's syndrome, while patients with anti-CE antibodies must be observed for HCV infection. Paper-12240188.
Despite the absence of NuMA, nuclei formed without visible changes of the chromatin structure, surrounded by an intact nuclear membrane containing pores and nuclear lamins. Paper-1315363.
NuMA is a 236-kD intranuclear protein that during mitosis is distributed into each daughter cell by association with the pericentrosomal domain of the spindle apparatus. Paper-82708.
The results revealed marked changes in the distribution of the density of NuMA bright features when nonneoplastic cells underwent phenotypically normal acinar morphogenesis. Paper-11369402.
In the pig-mouse interspecies reconstructed embryos, NuMA concentrated between the disarrayed chromosomes soon after activation and translocated to the transient spindle poles. Paper-11141357.
NuMA is removed along with the meiotic spindle during the enucleation process before reconstructing the egg by introducing the donor cell nucleus to produce cloned embryos. Paper-11337732.
The C terminus of the nuclear protein NuMA, NuMA-CT, has a well-known function in mitosis via its proximal segment, but it seems also involved in the control of differentiation. Paper-10614208.
NuMA is a 236 kDa intranuclear protein that is distributed into each daughter cell during mitosis through association with the pericentrosomal region of the mitotic spindle. Paper-247203.
We have developed imaging methods to quantify the distribution of fluorescently stained nuclear protein NuMA in different mammary phenotypes obtained using 3D cell culture. Paper-11369402.
In 30% of BHK cells transfected by the full-length clone, cytoplasmic aggregates of NuMA that colocalize with the centrosomes were documented in addition to the nuclear staining. Paper-551114.
Here we describe the isolation of NuMA protein from HeLa cells under mild conditions as a prerequisite to study its interactions with elements of the RCC1-Ran regulatory pathway. Paper-139629.
Nuclear mitotic apparatus protein-retinoic acid receptor alpha (NuMA-RARalpha) is the fourth of five fusion proteins identified in acute promyelocytic leukemia (APL) patients. Paper-9707885.
In this report we demonstrate that microinjection of anti- NuMA antibodies into interphase and prophase cells results in a failure to form a mitotic spindle apparatus. Paper-7381654.
The Food and Drug Administration approved NMP22 test, which measures the level of nuclear mitotic apparatus protein in urine, has 50% to 100% sensitivity and 60% to 90% specificity. Paper-8798389.
While the function of NuMA remains uncertain, its unusual pattern of segregation at mitosis defines a novel pathway for the segregation of nuclear proteins during cell division. Paper-7504935.
During mitosis, in contrast to the accumulation at the poles in animal cells, NuMA homologues in plant onion cells show a diffuse pattern, which may correspond to the spindle matrix. Paper-1752469.
Perturbation of NuMA alone disrupts spindle pole organization and delays anaphase onset, but does not alter the velocity of oscillatory chromosome movement in prometaphase. Paper-8758456.
Interestingly, we found that cohesin localizes to the spindle poles during mitosis and interacts with NuMA, a spindle pole-associated factor required for mitotic spindle organization. Paper-8882923.
Cells expressing these mutant forms of NuMA have disorganized mitotic spindles, fail to complete cytokinesis normally, and assemble micronuclei in the subsequent interphase. Paper-247203.
Progress on the use of a nuclear matrix protein known as NuMA as a marker for bladder cancer is presented, including results of a recently completed multisite clinical trial. Paper-822535.
MCC is not directly cytotoxic towards these cancer cells, but induces apoptosis as determined by nuclear DNA fragmentation and by the release of nuclear mitotic apparatus protein. Paper-1685602.
Clinical information was available for only 17 of the 30 patients with anti- NuMA-1; of these, 17 (53%) had clinical and lip biopsy findings that met the criteria for Sjögren's syndrome. Paper-703192.
This study shows that NuMA is extensively modified following HSV infection, including phosphorylation of an unidentified site(s), and that it depends to an extent on viral DNA synthesis. Paper-12819813.
To gain insight into the ultrastructure of NuMA, several defined fragments, as well as the full-length recombinant protein, were expressed in Escherichia coli and purified to homogeneity. Paper-259789.
Further evidence for apoptotic cell death was the observed blebbing and fragmentation of the chromosomes and a decrease in the level of NuMA protein detected by confocal microscopy. Paper-9285382.
These observations provide an initial set of clues regarding a potentially important function of NuMA in the organization of microtubules within the somatodendritic compartment of the neuron. Paper-2098106.
In an attempt to discover novel proteins functioning in both interphase nucleus and mitotic spindle as NuMA does, we carried out cDNA library screening with pooled autoimmune antibodies. Paper-12845936.
Other results from this laboratory have shown that transient overexpression of NuMA in HeLa cells induces a nuclear scaffold with a quasi-hexagonal organization that can fill the nuclei. Paper-1835865.
Intracellular dynactin, dynein and nuclear/ mitotic apparatus (NuMA) protein were recruited to multiple foci associated with ectopic cytoplasmic aggregates of Arp1alpha in transfected cells. Paper-2053753.
A nonsynonymous SNP (A794G) in NuMA was identified that showed a stronger association with breast cancer risk than the initial marker SNP (OR=2.8, P=0.005 initial sample; OR=2.1, P=0.002 combined). Paper-11198898.
As mitosis progresses, NuMA reassociates with telophase chromosomes very early during nuclear reformation, before substantial accumulation of lamins on chromosomal surfaces is evident. Paper-7249299.
When microtubules were depolymerized by nocodazole treatment, the SP-H antigen appeared as discrete cytoplasmic foci, suggesting that the antigen may self-associate, forming multimeric structures. Paper-39818.
Both the changes in morphology associated with apoptosis and the cleavage of NuMA were retarded by treatment with TPCK but not by treatment by other protease inhibitors including ICE inhibitor II. Paper-1040790.
Upon alteration of nuclear organization using an antibody against NuMA, differentiated non-neoplastic cells undergo apoptosis, whereas partially differentiated malignant cells enter the cell cycle. Paper-13198511.
In addition, some peri-centrosomal material at the spindle poles becomes fragmented and the distribution of the spindle protein NuMA becomes more concentrated at the minus ends of the spindle microtubules. Paper-1835657.
Regarding T-stages of colorectal cancer no marker detected T1 when regarding 95% specificity-cut-off value but NuMA showed little more sensitivity when based on a 95% specificity cut off value versus healthy. Paper-1987979.
The abundant coiled-coil protein NuMA is located in the nucleus during interphase, but when the nuclear envelope disassembles in prometaphase it rapidly redistributes to the developing spindle poles. Paper-11786171.
NuMA becomes dephosphorylated, loses its association with dynein/dynactin, and releases from spindle poles after anaphase onset to allow spindle disassembly and reformation of interphase daughter nuclei. Paper-10564670.
Immunolocalization of NuMA and phosphorylated proteins during the cell cycle in human breast and prostate cancer cells as analyzed by immunofluorescence and postembedding immunoelectron microscopy. Paper-8915170.
In synchronized cells, NuMA and LANA are colocalized in interphase cells and separate during mitosis at the beginning of prophase, reassociating again at the end of telophase and cytokinesis. Paper-12826766.
We propose that NuMA functions early in mitosis during the formation of spindle poles, but is released from the spindle after anaphase, to allow spindle disassembly and remodelling of the microtubule network. Paper-10426998.
NuMA and nuclear lamins are cleaved during viral infection--inhibition of caspase activity prevents cleavage and rescues HeLa cells from measles virus-induced but not from rhinovirus 1B-induced cell death. Paper-10402024.
The microtubule motor cytoplasmic dynein was a critical part of this coalescing machinery, and in some tumor cells overexpression of the spindle protein NuMA interfered with dynein localization, promoting multipolarity. Paper-10757620.
Although the potential functional relevance of the A794G variation requires further biological validation, we conclude that variations in the NuMA gene are likely responsible for the observed increased breast cancer risk. Paper-11198898.
This interaction between NuMA and LANA is critical for segregation and maintenance of the KSHV episomes through a temporally controlled mechanism of binding and release during specific phases of mitosis. Paper-12826766.
Using fluorescence recovery after photobleaching, we show that an exogenously expressed green-fluorescent-protein/ NuMA fusion undergoes continuous exchange between soluble and spindle-associated pools in living cells. Paper-10647729.
Surprisingly, these K-fibers were oriented away from, and not directly connected to, centrosomes and incorporated into the spindle by the sliding of their distal ends toward centrosomes via a NuMA-dependent mechanism. Paper-9855154.
By screening tissue sections of various organs, absence of NuMA from the nucleus was observed in a number of cell types, including sperm, granulocytes in the blood, and differentiated smooth and skeletal muscle fibers. Paper-1315363.
NuMA positivity associated with a diagnosis of connective tissue disease (CTD) in 18 patients (45%), primary Sj??gren or sicca syndrome and undifferentiated connective tissue disease being the most represented. Paper-12756978.
The impact of poly(ADP-ribosyl)ation on the biochemical function of NuMA remains murky at this time, but these new results represent the first step to clearing the view as to how poly(ADP-ribosyl)ation regulates cell division. Paper-11495124.
Molecular Basis of Ion Channels and Receptors Involved in Nerve Excitation, Synaptic Transmission and Muscle Contraction. Proceedings of a conference in memory of Professor Shosaku Numa. Tokyo, Japan, January 12-15, 1993. Paper-11723591.
Determination of the microtubule polarity demonstrated that the peripheral bundles of microtubules were arranged with their minus ends directed to the cell periphery, and the SP-H antigen was specifically localized at this end. Paper-39818.
A potential role for NuMA in nuclear organization or gene regulation is suggested by the observations that its pattern of nuclear distribution depends upon cell phenotype and that it interacts and/or colocalizes with transcription factors. Paper-13099338.
To determine if NuMA plays an active role in organizing the microtubules at the polar region of the mitotic spindle, we have developed a cell free system for the assembly of mitotic asters derived from synchronized cultured cells. Paper-409235.
Polyclonal antibodies raised against fusion proteins generated from non-overlapping cDNA fragments stained the HeLa SP-H antigen in interphase and mitotic cells, and recognized a single 215 kDa band on immunoblots, as did the original SP-H antibody. Paper-101924.
After induction of a 180 kDa form of NuMA in interphase HeLa cells by 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole, nuclear apoptotic phenomena including chromatin condensation, DNA fragmentation, and micronucleation were observed. Paper-738826.
When HL60 cells were stimulated by diverse apoptosis inducers such as camptothecin, staurosporine, cycloheximide, and A23187, the extent of NuMA cleavage to produce a 180 kDa product was comparable with the degree of oligonucleosomal laddering. Paper-738826.
Therefore, we have compared the textural features observed in G0/G1 nuclei from human leukemic CEM cells and their MDR variant CEM-VLB, after staining of either DNA by Feulgen method or nuclear matrix by immunodetection of NuMA antigen on DNase treated samples. Paper-2083288.
Furthermore, given that NuMA is essential for spindle pole organization in vertebrate systems, it is likely that this insoluble matrix plays an essential structural function in anchoring and/or stabilizing microtubule minus ends at spindle poles in mitotic cells. Paper-1847159.
Its association with the nuclear matrix and its localization during mitosis to the site of nuclear reassembly suggest the interesting possibility that NuMA protein could be representative of a class of proteins involved in the early events of nuclear reassembly. Paper-3447376.
In dividing cells, upon phosphorylation, NuMA disperses into the cytoplasm, associates with cytoplasmic dynein/dynactin to form a complex, and translocates along microtubules to the spindle poles where it organizes and tethers microtubules to spindle poles. Paper-10564670.
These results indicate that several metal ions are powerful stabilizing agents of the nuclear matrix prepared from K562 erythroleukemia cells and also strengthen the concept that NuMA and topoisomerase IIalpha may act as structural components of the nuclear matrix. Paper-1920339.
Additionally, we show that the delocalization of dynein from mitotic spindles by HPV16 E7 and the interaction between HPV16 E7 and NuMA correlate with the induction of defects in chromosome alignment during prometaphase even in cells with normal centrosome numbers. Paper-13521107.
In interphase cells NuMA protein is restricted to the nucleus and is a constituent of isolated nuclear matrices, but in mitotic cells it is observed by indirect immunofluorescence microscopy to be concentrated at the polar regions of the mitotic apparatus. Paper-3447376.
NuMA, a nuclear protein that associates with the mitotic apparatus, was identified in 1980 as a high molecular weight component of the nuclear matrix with the unusual property of associating with the microtubules of the spindle apparatus during mitosis. Paper-7970256.
Using immunogold electron microscopy, we show that NuMA is a component of an electron-dense material concentrated at both mitotic spindle poles in PtK1 cells and the core of microtubule asters formed through a centrosome-independent mechanism in cell-free mitotic extracts. Paper-1847159.
Further analysis of this sequence here has revealed that NuMA will form a two-stranded coiled-coil structure with multiple (18) points at which the conformation is interrupted either by proline-containing segments or by discontinuities in the phasing of the heptad substructure. Paper-8164366.
NuMA is present in the nuclei and mitotic spindle of all types of human cells that have been examined, but proteins of similar molecular weight (300,000 daltons in dissociating solvents) or immunological specificity are not detected in cells of other species (including monkey). Paper-3447376.
The majority of cells were positive for NuMA but a few negative cell types were found, including spermatozoa, superficial keratinocytes, neutrophil granulocytes, syncytiotrophoblasts, and some neurons, fibroblasts, and smooth and skeletal muscle cells. Paper-2196279.
Once cells have passed the metaphase-anaphase transition, the 240 kDa form of NuMA either becomes a 180 kDa truncated form which is fated to be degraded completely before mitotic exit, or returns to the 220 kDa form that relocates to the daughter nuclei and remains throughout interphase. Paper-738826.
The concomitant autoimmune response to a hnRNP component of the pre-mRNA processing machinery and to NuMA, a protein engaged in mitotic events and reported to be associated with mRNA splicing complexes in interphase, may indicate physical and functional association of these antigens. Paper-1316542.
When mitotic NuMA function is disrupted, centrosomes provide initial focusing activity, but continued centrosome attachment to spindle fibers under tension is defective, and the maintenance of focused kinetochore fibers at spindle poles throughout mitosis is prevented. Paper-13656722.
Immediately after nuclear transfer, NuMA staining was absent in all donor cell fibroblast nuclei (0 h) but staining was detected by 6 h within the reconstructed eggs, at which time the transferred somatic cell nucleus swelled in most cells (19/27) and became a pronucleus-like structure. Paper-11337732.
Here we report on nuclear organization of NuMA during the cell cycle in estrogen responsive MCF-7 breast cancer cells and in androgen responsive LNCaP prostate cancer cells using immunoelectron microscopy, and on correlation to MPM-2 monoclonal phosphoprotein antibody. Paper-8915170.
In stark contrast to conventional microtubule-associated proteins whose solubility is directly dependent on microtubules, we find that once NuMA is incorporated into this matrix either in vivo or in vitro, it becomes insoluble and this insolubility is no longer dependent on microtubules. Paper-1847159.
Taken together, these results demonstrate that the unique organization of the minus ends of microtubules and the localization of NuMA at the polar ends of the mammalian mitotic spindle can be accomplished in a centrosome-independent manner by the opposing activities of plus end- and minus end-directed motors. Paper-739071.
Separation of centrosomes at the G2-M transition is also impaired and mitotic spindle morphogenesis is grossly abnormal: although in most spindles chromosomes align in a metaphase plate, the two centrosomes stay most often unseparated at one pole and most of the NuMA protein accumulates at the other. Paper-1234512.
A total of 11 differentially expressed protein spots corresponding to 10 independent proteins were detected, and peptide fingerprinting combined with mass spectrometry of these proteins revealed them to include NuMA (nuclear protein that associates with the mitotic apparatus), heat shock proteins, and redox regulators. Paper-10028838.
This chapter will review the structure, function, and distribution of the protein NuMA ( nuclear matrix mitotic apparatus) and other nuclear matrix proteins that depart the nucleus during the interphase/ mitosis transition to become structural and functional components within specific domains of the mitotic apparatus. Paper-472414.
While none of these specific mutations in the NuMA sequence alters the faithful targeting of the protein into the interphase nucleus, mutation of threonine residue 2040 alone or in combination with mutations in other potential p34cdc2 phosphorylation sites abolishes NuMA's ability to associate normally with the microtubules of the mitotic spindle. Paper-247203.
These synonyms are used for gene NUMA1 (nuclear mitotic apparatus protein 1): SP-H antigen, NuMA protein, NUMA, Nuclear mitotic apparatus protein 1.
These accession numbers are used for gene NUMA1: Q9BTE9 (UNIPROT__AC), Q96HN5 (UNIPROT__AC), CAA77670 (NCBI_GENBANK__AC), CAA77669 (NCBI_GENBANK__AC).
NUMA1 is a homologue of NUMA1 (nuclear mitotic apparatus protein 1) from Bos taurus.
NUMA1 is a homologue of NUMA1 (nuclear mitotic apparatus protein 1) from Pan troglodytes.
NUMA1 is a homologue of NUMA1 (nuclear mitotic apparatus protein 1) from Gallus gallus.
NUMA1 is a homologue of Numa1 (nuclear mitotic apparatus protein 1) from Mus musculus.
NUMA1 is a homologue of Numa1 (nuclear mitotic apparatus protein 1) from Rattus norvegicus.
NUMA1 is a homologue of LOC572344 (similar to nuclear/mitotic apparatus protein) from Danio rerio.
Important links !
iHOP - Information Hyperlinked over Proteins .
Concept & Implementation by Robert Hoffmann.