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Journal articles on the topic 'HECW1'

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Author: Grafiati

Published: 9 March 2023

Last updated: 10 March 2023

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1

Erdman, Vera V., Denis D. Karimov, Ilsia A. Tuktarova, Yanina R. Timasheva, Timur R. Nasibullin, and Gulnaz F. Korytina. "Alu Deletions in LAMA2 and CDH4 Genes Are Key Components of Polygenic Predictors of Longevity." International Journal of Molecular Sciences 23, no. 21 (November 4, 2022): 13492. http://dx.doi.org/10.3390/ijms232113492.

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Longevity is a unique human phenomenon and a highly stable trait, characterized by polygenicity. The longevity phenotype occurs due to the ability to successfully withstand the age-related genomic instability triggered by Alu elements. The purpose of our cross-sectional study was to evaluate the combined contribution of ACE*Ya5ACE, CDH4*Yb8NBC516, COL13A1*Ya5ac1986, HECW1*Ya5NBC182, LAMA2*Ya5-MLS19, PLAT*TPA25, PKHD1L1*Yb8AC702, SEMA6A*Yb8NBC597, STK38L*Ya5ac2145 and TEAD1*Ya5ac2013 Alu elements to longevity. The study group included 2054 unrelated individuals aged from 18 to 113 years who are ethnic Tatars from Russia. We analyzed the dynamics of the allele and genotype frequencies of the studied Alu polymorphic loci in the age groups of young (18–44 years old), middle-aged (45–59 years old), elderly (60–74 years old), old seniors (75–89 years old) and long-livers (90–113 years old). Most significant changes in allele and genotype frequencies were observed between the long-livers and other groups. The search for polygenic predictors of longevity was performed using the APSampler program. Attaining longevity was associated with the combinations LAMA2*ID + CDH4*D (OR = 2.23, PBonf = 1.90 × 10−2) and CDH4*DD + LAMA2*ID + HECW1*D (OR = 4.58, PBonf = 9.00 × 10−3) among persons aged between 18 and 89 years, LAMA2*ID + CDH4*D + SEMA6A*I for individuals below 75 years of age (OR = 3.13, PBonf = 2.00 × 10−2), LAMA2*ID + HECW1*I for elderly people aged 60 and older (OR = 3.13, PBonf = 2.00 × 10−2) and CDH4*DD + LAMA2*D + HECW1*D (OR = 4.21, PBonf = 2.60 × 10−2) and CDH4*DD + LAMA2*D + ACE*I (OR = 3.68, PBonf = 1.90 × 10−2) among old seniors (75–89 years old). The key elements of combinations associated with longevity were the deletion alleles of CDH4 and LAMA2 genes. Our results point to the significance for human longevity of the Alu polymorphic loci in CDH4, LAMA2, HECW1, SEMA6A and ACE genes, involved in the integration systems.

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2

Haouari, Shanez, Christian Robert Andres, Debora Lanznaster, Sylviane Marouillat, Céline Brulard, Audrey Dangoumau, Devina Ung, et al. "Study of Ubiquitin Pathway Genes in a French Population with Amyotrophic Lateral Sclerosis: Focus on HECW1 Encoding the E3 Ligase NEDL1." International Journal of Molecular Sciences 24, no. 2 (January 9, 2023): 1268. http://dx.doi.org/10.3390/ijms24021268.

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The ubiquitin pathway, one of the main actors regulating cell signaling processes and cellular protein homeostasis, is directly involved in the pathophysiology of amyotrophic lateral sclerosis (ALS). We first analyzed, by a next-generation sequencing (NGS) strategy, a series of genes of the ubiquitin pathway in two cohorts of familial and sporadic ALS patients comprising 176 ALS patients. We identified several pathogenic variants in different genes of this ubiquitin pathway already described in ALS, such as FUS, CCNF and UBQLN2. Other variants of interest were discovered in new genes studied in this disease, in particular in the HECW1 gene. We have shown that the HECT E3 ligase called NEDL1, encoded by the HECW1 gene, is expressed in neurons, mainly in their somas. Its overexpression is associated with increased cell death in vitro and, very interestingly, with the cytoplasmic mislocalization of TDP-43, a major protein involved in ALS. These results give new support for the role of the ubiquitin pathway in ALS, and suggest further studies of the HECW1 gene and its protein NEDL1 in the pathophysiology of ALS.

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Liu, Jia, Su Dong, Lian Li, Heather Wang, Jing Zhao, and Yutong Zhao. "The E3 ubiquitin ligase HECW1 targets thyroid transcription factor 1 (TTF1/NKX2.1) for its degradation in the ubiquitin-proteasome system." Cellular Signalling 58 (June 2019): 91–98. http://dx.doi.org/10.1016/j.cellsig.2019.03.005.

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Liu, Jia, Su Dong, Heather Wang, Lian Li, Qinmao Ye, Yanhui Li, Jiaxing Miao, Sissy Jhiang, Jing Zhao, and Yutong Zhao. "Two distinct E3 ligases, SCF FBXL19 and HECW1, degrade thyroid transcription factor 1 in normal thyroid epithelial and follicular thyroid carcinoma cells, respectively." FASEB Journal 33, no. 9 (June 25, 2019): 10538–50. http://dx.doi.org/10.1096/fj.201900415r.

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5

Chen, Yumay, Daniel J. Riley, Lei Zheng, Phang-Lang Chen, and Wen-Hwa Lee. "Phosphorylation of the Mitotic Regulator Protein Hec1 by Nek2 Kinase Is Essential for Faithful Chromosome Segregation." Journal of Biological Chemistry 277, no. 51 (October 16, 2002): 49408–16. http://dx.doi.org/10.1074/jbc.m207069200.

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Hec1 (highlyexpressed incancer) plays essential roles in chromosome segregation by interacting through its coiled-coil domains with several proteins that modulate the G2/M phase. Hec1 localizes to kinetochores, and its inactivation either by genetic deletion or antibody neutralization leads to severe and lethal chromosomal segregation errors, indicating that Hec1 plays a critical role in chromosome segregation. The mechanisms by which Hec1 is regulated, however, are not known. Here we show that human Hec1 is a serine phosphoprotein and that it binds specifically to the mitotic regulatory kinase Nek2 during G2/M. Nek2 phosphorylates Hec1 on serine residue 165, bothin vitroandin vivo. Yeast cells are viable without scNek2/Kin3, a close structural homolog of Nek2 that binds to both human and yeast Hec1. When the same yeasts carry an scNek2/Kin3 (D55G) or Nek2 (E38G) mutation to mimic a similar temperature-sensitivenimamutation inAspergillus, their growth is arrested at the nonpermissive temperature, because the scNek2/Kin3 (D55G) mutant binds to Hec1 but fails to phosphorylate it. Whereas wild-type human Hec1 rescues lethality resulting from deletion of Hec1 inSaccharomyces cerevesiae, a human Hec1 mutant or yeast Hec1 mutant changing Ser165to Ala or yeast Hec1 mutant changing Ser201to Ala does not. Mutations changing the same Ser residues to Glu, to mimic the negative charge created by phosphorylation, partially rescue lethality but result in a high incidence of errors in chromosomal segregation. These results suggest that cell cycle-regulated serine phosphorylation of Hec1 by Nek2 is essential for faithful chromosome segregation.

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6

Wu, Guikai, Randy Wei, Eric Cheng, Bryan Ngo, and Wen-Hwa Lee. "Hec1 Contributes to Mitotic Centrosomal Microtubule Growth for Proper Spindle Assembly through Interaction with Hice1." Molecular Biology of the Cell 20, no. 22 (November 15, 2009): 4686–95. http://dx.doi.org/10.1091/mbc.e08-11-1123.

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Previous studies have stipulated Hec1 as a conserved kinetochore component critical for mitotic control in part by directly binding to kinetochore fibers of the mitotic spindle and by recruiting spindle assembly checkpoint proteins Mad1 and Mad2. Hec1 has also been reported to localize to centrosomes, but its function there has yet to be elucidated. Here, we show that Hec1 specifically colocalizes with Hice1, a previously characterized centrosomal microtubule-binding protein, at the spindle pole region during mitosis. In addition, the C-terminal region of Hec1 directly binds to the coiled-coil domain 1 of Hice1. Depletion of Hice1 by small interfering RNA (siRNA) reduced levels of Hec1 in the cell, preferentially at centrosomes and spindle pole vicinity. Reduction of de novo microtubule nucleation from mitotic centrosomes can be observed in cells treated with Hec1 or Hice1 siRNA. Consistently, neutralization of Hec1 or Hice1 by specific antibodies impaired microtubule aster formation from purified mitotic centrosomes in vitro. Last, disruption of the Hec1/Hice1 interaction by overexpressing Hice1ΔCoil1, a mutant defective in Hec1 interaction, elicited abnormal spindle morphology often detected in Hec1 and Hice1 deficient cells. Together, the results suggest that Hec1, through cooperation with Hice1, contributes to centrosome-directed microtubule growth to facilitate establishing a proper mitotic spindle.

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7

Sundin, Lynsie J. R., Geoffrey J. Guimaraes, and Jennifer G. DeLuca. "The NDC80 complex proteins Nuf2 and Hec1 make distinct contributions to kinetochore–microtubule attachment in mitosis." Molecular Biology of the Cell 22, no. 6 (March 15, 2011): 759–68. http://dx.doi.org/10.1091/mbc.e10-08-0671.

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Successful mitosis requires that kinetochores stably attach to the plus ends of spindle microtubules. Central to generating these attachments is the NDC80 complex, made of the four proteins Spc24, Spc25, Nuf2, and Hec1/Ndc80. Structural studies have revealed that portions of both Hec1 and Nuf2 N termini fold into calponin homology (CH) domains, which are known to mediate microtubule binding in certain proteins. Hec1 also contains a basic, positively charged stretch of amino acids that precedes its CH domain, referred to as the “tail.” Here, using a gene silence and rescue approach in HeLa cells, we show that the CH domain of Hec1, the CH domain of Nuf2, and the Hec1 tail each contributes to kinetochore–microtubule attachment in distinct ways. The most severe defects in kinetochore–microtubule attachment were observed in cells rescued with a Hec1 CH domain mutant, followed by those rescued with a Hec1 tail domain mutant. Cells rescued with Nuf2 CH domain mutants, however, generated stable kinetochore–microtubule attachments but failed to generate wild-type interkinetochore tension and failed to enter anaphase in a timely manner. These data suggest that the CH and tail domains of Hec1 generate essential contacts between kinetochores and microtubules in cells, whereas the Nuf2 CH domain does not.

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8

Wei, Randy, Bryan Ngo, Guikai Wu, and Wen-Hwa Lee. "Phosphorylation of the Ndc80 complex protein, HEC1, by Nek2 kinase modulates chromosome alignment and signaling of the spindle assembly checkpoint." Molecular Biology of the Cell 22, no. 19 (October 2011): 3584–94. http://dx.doi.org/10.1091/mbc.e11-01-0012.

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The spindle assemble checkpoint (SAC) is critical for accurate chromosome segregation. Hec1 contributes to chromosome segregation in part by mediating SAC signaling and chromosome alignment. However, the molecular mechanism by which Hec1 modulates checkpoint signaling and alignment remains poorly understood. We found that Hec1 serine 165 (S165) is preferentially phosphorylated at kinetochores. Phosphorylated Hec1 serine 165 (pS165) specifically localized to kinetochores of misaligned chromosomes, showing a spatiotemporal distribution characteristic of SAC molecules. Expressing an RNA interference (RNAi)-resistant S165A mutant in Hec1-depleted cells permitted normal progression to metaphase, but accelerated the metaphase-to-anaphase transition. The S165A cells were defective in Mad1 and Mad2 localization to kinetochores, regardless of attachment status. These cells often entered anaphase with lagging chromosomes and elicited increased segregation errors and cell death. In contrast, expressing S165E mutant in Hec1-depleted cells triggered defective chromosome alignment and severe mitotic arrest associated with increased Mad1/Mad2 signals at prometaphase kinetochores. A small portion of S165E cells eventually bypassed the SAC but showed severe segregation errors. Nek2 is the primary kinase responsible for kinetochore pS165, while PP1 phosphatase may dephosphorylate pS165 during SAC silencing. Taken together, these results suggest that modifications of Hec1 S165 serve as an important mechanism in modulating SAC signaling and chromosome alignment.

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9

Tooley, John G., Stephanie A. Miller, and P. Todd Stukenberg. "The Ndc80 complex uses a tripartite attachment point to couple microtubule depolymerization to chromosome movement." Molecular Biology of the Cell 22, no. 8 (April 15, 2011): 1217–26. http://dx.doi.org/10.1091/mbc.e10-07-0626.

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In kinetochores, the Ndc80 complex couples the energy in a depolymerizing microtubule to perform the work of moving chromosomes. The complex directly binds microtubules using an unstructured, positively charged N-terminal tail located on Hec1/Ndc80. Hec1/Ndc80 also contains a calponin homology domain (CHD) that increases its affinity for microtubules in vitro, yet whether it is required in cells and how the tail and CHD work together are critical unanswered questions. Human kinetochores containing Hec1/Ndc80 with point mutations in the CHD fail to align chromosomes or form productive microtubule attachments. Kinetochore architecture and spindle checkpoint protein recruitment are unaffected in these mutants, and the loss of CHD function cannot be rescued by removing Aurora B sites from the tail. The interaction between the Hec1/Ndc80 CHD and a microtubule is facilitated by positively charged amino acids on two separate regions of the CHD, and both are required for kinetochores to make stable attachments to microtubules. Chromosome congression in cells also requires positive charge on the Hec1 tail to facilitate microtubule contact. In vitro binding data suggest that charge on the tail regulates attachment by directly increasing microtubule affinity as well as driving cooperative binding of the CHD. These data argue that in vertebrates there is a tripartite attachment point facilitating the interaction between Hec1/Ndc80 and microtubules. We discuss how such a complex microtubule-binding interface may facilitate the coupling of depolymerization to chromosome movement.

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10

DeLuca, Jennifer G., Yimin Dong, Polla Hergert, Joshua Strauss, Jennifer M. Hickey, E. D. Salmon, and Bruce F. McEwen. "Hec1 and Nuf2 Are Core Components of the Kinetochore Outer Plate Essential for Organizing Microtubule Attachment Sites." Molecular Biology of the Cell 16, no. 2 (February 2005): 519–31. http://dx.doi.org/10.1091/mbc.e04-09-0852.

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A major goal in the study of vertebrate mitosis is to identify proteins that create the kinetochore-microtubule attachment site. Attachment sites within the kinetochore outer plate generate microtubule dependent forces for chromosome movement and regulate spindle checkpoint protein assembly at the kinetochore. The Ndc80 complex, comprised of Ndc80 (Hec1), Nuf2, Spc24, and Spc25, is essential for metaphase chromosome alignment and anaphase chromosome segregation. It has also been suggested to have roles in kinetochore microtubule formation, production of kinetochore tension, and the spindle checkpoint. Here we show that Nuf2 and Hec1 localize throughout the outer plate, and not the corona, of the vertebrate kinetochore. They are part of a stable “core” region whose assembly dynamics are distinct from other outer domain spindle checkpoint and motor proteins. Furthermore, Nuf2 and Hec1 are required for formation and/or maintenance of the outer plate structure itself. Fluorescence light microscopy, live cell imaging, and electron microscopy provide quantitative data demonstrating that Nuf2 and Hec1 are essential for normal kinetochore microtubule attachment. Our results indicate that Nuf2 and Hec1 are required for organization of stable microtubule plus-end binding sites in the outer plate that are needed for the sustained poleward forces required for biorientation at kinetochores.

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Wimbish, Robert T., Keith F. DeLuca, Jeanne E. Mick, Jack Himes, Ignacio Jiménez-Sánchez, A. Arockia Jeyaprakash, and Jennifer G. DeLuca. "The Hec1/Ndc80 tail domain is required for force generation at kinetochores, but is dispensable for kinetochore–microtubule attachment formation and Ska complex recruitment." Molecular Biology of the Cell 31, no. 14 (July 1, 2020): 1453–73. http://dx.doi.org/10.1091/mbc.e20-05-0286.

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This study demonstrates that the Ska complex and the Hec1 tail domain contribute to kinetochore–microtubule attachment regulation independently. The Hec1 tail is shown to be dispensable for Ska complex recruitment to kinetochores and for formation of kinetochore–microtubule attachments, but required for wild-type force generation at kinetochores.

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12

DeLuca, Keith F., Amanda Meppelink, Amanda J. Broad, Jeanne E. Mick, Olve B. Peersen, Sibel Pektas, Susanne M. A. Lens, and Jennifer G. DeLuca. "Aurora A kinase phosphorylates Hec1 to regulate metaphase kinetochore–microtubule dynamics." Journal of Cell Biology 217, no. 1 (November 29, 2017): 163–77. http://dx.doi.org/10.1083/jcb.201707160.

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Precise regulation of kinetochore–microtubule attachments is essential for successful chromosome segregation. Central to this regulation is Aurora B kinase, which phosphorylates kinetochore substrates to promote microtubule turnover. A critical target of Aurora B is the N-terminal “tail” domain of Hec1, which is a component of the NDC80 complex, a force-transducing link between kinetochores and microtubules. Although Aurora B is regarded as the “master regulator” of kinetochore–microtubule attachment, other mitotic kinases likely contribute to Hec1 phosphorylation. In this study, we demonstrate that Aurora A kinase regulates kinetochore–microtubule dynamics of metaphase chromosomes, and we identify Hec1 S69, a previously uncharacterized phosphorylation target site in the Hec1 tail, as a critical Aurora A substrate for this regulation. Additionally, we demonstrate that Aurora A kinase associates with inner centromere protein (INCENP) during mitosis and that INCENP is competent to drive accumulation of the kinase to the centromere region of mitotic chromosomes. These findings reveal that both Aurora A and B contribute to kinetochore–microtubule attachment dynamics, and they uncover an unexpected role for Aurora A in late mitosis.

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Zaytsev, Anatoly V., Lynsie J. R. Sundin, Keith F. DeLuca, Ekaterina L. Grishchuk, and Jennifer G. DeLuca. "Accurate phosphoregulation of kinetochore–microtubule affinity requires unconstrained molecular interactions." Journal of Cell Biology 206, no. 1 (June 30, 2014): 45–59. http://dx.doi.org/10.1083/jcb.201312107.

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Accurate chromosome segregation relies on dynamic interactions between microtubules (MTs) and the NDC80 complex, a major kinetochore MT-binding component. Phosphorylation at multiple residues of its Hec1 subunit may tune kinetochore–MT binding affinity for diverse mitotic functions, but molecular details of such phosphoregulation remain elusive. Using quantitative analyses of mitotic progression in mammalian cells, we show that Hec1 phosphorylation provides graded control of kinetochore–MT affinity. In contrast, modeling the kinetochore interface with repetitive MT binding sites predicts a switchlike response. To reconcile these findings, we hypothesize that interactions between NDC80 complexes and MTs are not constrained, i.e., the NDC80 complexes can alternate their binding between adjacent kinetochore MTs. Experiments using cells with phosphomimetic Hec1 mutants corroborate predictions of such a model but not of the repetitive sites model. We propose that accurate regulation of kinetochore–MT affinity is driven by incremental phosphorylation of an NDC80 molecular “lawn,” in which the NDC80–MT bonds reorganize dynamically in response to the number and stability of MT attachments.

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Nijenhuis, Wilco, Eleonore von Castelmur, Dene Littler, Valeria De Marco, Eelco Tromer, Mathijs Vleugel, Maria H. J. van Osch, Berend Snel, Anastassis Perrakis, and Geert J. P. L. Kops. "A TPR domain–containing N-terminal module of MPS1 is required for its kinetochore localization by Aurora B." Journal of Cell Biology 201, no. 2 (April 8, 2013): 217–31. http://dx.doi.org/10.1083/jcb.201210033.

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The mitotic checkpoint ensures correct chromosome segregation by delaying cell cycle progression until all kinetochores have attached to the mitotic spindle. In this paper, we show that the mitotic checkpoint kinase MPS1 contains an N-terminal localization module, organized in an N-terminal extension (NTE) and a tetratricopeptide repeat (TPR) domain, for which we have determined the crystal structure. Although the module was necessary for kinetochore localization of MPS1 and essential for the mitotic checkpoint, the predominant kinetochore binding activity resided within the NTE. MPS1 localization further required HEC1 and Aurora B activity. We show that MPS1 localization to kinetochores depended on the calponin homology domain of HEC1 but not on Aurora B–dependent phosphorylation of the HEC1 tail. Rather, the TPR domain was the critical mediator of Aurora B control over MPS1 localization, as its deletion rendered MPS1 localization insensitive to Aurora B inhibition. These data are consistent with a model in which Aurora B activity relieves a TPR-dependent inhibitory constraint on MPS1 localization.

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Yanagishita, Tomoe, Takuya Hirade, Keiko Shimojima Yamamoto, Makoto Funatsuka, Yusaku Miyamoto, Makiko Maeda, Kumiko Yanagi, et al. "HECW2 ‐related disorder in four Japanese patients." American Journal of Medical Genetics Part A 185, no. 10 (May 28, 2021): 2895–902. http://dx.doi.org/10.1002/ajmg.a.62363.

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Mikami, Yoshikazu, Tetsuya Hori, Hiroshi Kimura, and Tatsuo Fukagawa. "The Functional Region of CENP-H Interacts with the Nuf2 Complex That Localizes to Centromere during Mitosis." Molecular and Cellular Biology 25, no. 5 (March 1, 2005): 1958–70. http://dx.doi.org/10.1128/mcb.25.5.1958-1970.2005.

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ABSTRACT CENP-H is a constitutive centromere component that localizes to the centromere throughout the cell cycle. Because CENP-H is colocalized with CENP-A and CENP-C, it is thought to be an inner centromere protein. We previously generated a conditional loss-of-function mutant of CENP-H and showed that CENP-H is required for targeting of CENP-C to the centromere in chicken DT40 cells. In the present study, we used this mutant to identify the functional region of chicken CENP-H necessary for centromere targeting and cell viability. This region was found by yeast two-hybrid analysis to interact with Hec1, which is a member of the Nuf2 complex that transiently localizes to the centromere during mitosis. Coimmunoprecipitation experiments revealed that CENP-H interacts with the Nuf2 complex in chicken DT40 cells. Photobleaching experiments showed that both Hec1 and CENP-H form stable associations with the centromeres during mitosis, suggesting that Hec1 acts as a structural component of centromeres during mitosis. On the basis of these results and previously published data, we propose that the Nuf2 complex functions as a connector between the inner and outer kinetochores.

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Li, L., Y. Zhou, G. F. Wang, S. C. Liao, Y. B. Ke, W. Wu, X. H. Li, R. L. Zhang, and Y. C. Fu. "Anaphase-promoting complex/cyclosome controls HEC1 stability." Cell Proliferation 44, no. 1 (December 29, 2010): 1–9. http://dx.doi.org/10.1111/j.1365-2184.2010.00712.x.

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18

Krishnamoorthy, Vidhya, Richa Khanna, and Veena K. Parnaik. "E3 ubiquitin ligase HECW2 targets PCNA and lamin B1." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1865, no. 8 (August 2018): 1088–104. http://dx.doi.org/10.1016/j.bbamcr.2018.05.008.

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Zaytsev, Anatoly V., Jeanne E. Mick, Evgeny Maslennikov, Boris Nikashin, Jennifer G. DeLuca, and Ekaterina L. Grishchuk. "Multisite phosphorylation of the NDC80 complex gradually tunes its microtubule-binding affinity." Molecular Biology of the Cell 26, no. 10 (May 15, 2015): 1829–44. http://dx.doi.org/10.1091/mbc.e14-11-1539.

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Microtubule (MT) attachment to kinetochores is vitally important for cell division, but how these interactions are controlled by phosphorylation is not well known. We used quantitative approaches in vitro combined with molecular dynamics simulations to examine phosphoregulation of the NDC80 complex, a core kinetochore component. We show that the outputs from multiple phosphorylation events on the unstructured tail of its Hec1 subunit are additively integrated to elicit gradual tuning of NDC80-MT binding both in vitro and in silico. Conformational plasticity of the Hec1 tail enables it to serve as a phosphorylation-controlled rheostat, providing a new paradigm for regulating the affinity of MT binders. We also show that cooperativity of NDC80 interactions is weak and is unaffected by NDC80 phosphorylation. This in vitro finding strongly supports our model that independent molecular binding events to MTs by individual NDC80 complexes, rather than their structured oligomers, regulate the dynamics and stability of kinetochore-MT attachments in dividing cells.

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Tan, Yi, Chengling Zhang, Ying Zhang, Xueshan Dai, Qinghua Wei, Jiahui Wei, Pingli Xu, and Yi Chen. "Combination of ferulic acid, ligustrazine and tetrahydropalmatine inhibits invasion and metastasis through MMP/TIMP signaling in endometriosis." PeerJ 9 (June 28, 2021): e11664. http://dx.doi.org/10.7717/peerj.11664.

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Background The design of the combination of ferulic acid, ligustrazine and tetrahydropalmatine (FLT) is inspired by the Chinese herbal prescription Foshou San. Previous work has shown that FLT inhibited endometriosis growth in rat autograft models. However, the mechanism behind this is unclear. MMP/TIMP signaling is considered as the vital pathway of metastasis and invasion in endometriosis. In this study, we aim to disclose effects of FLT on MMP/TIMP signaling in invasion and metastasis during endometrial cells and xenograft endometriosis. Methods In vivo, effect of FLT on endometriosis was evaluated in a xenogeneic mice model. In vitro, cell viability assay was performed with an IC50 measurement of FLT in hEM15A and HEC1-B cells. The effect of FLT on invasion and metastasis was analyzed in scratch wound and transwell assay. Gene and protein expression of MMP/TIMP signaling were detected by qPCR and Western blotting. Results In xenograft endometriosis, FLT reduced ectopic volume without effect on weight. FLT inhibitory effects on cell growth exhibited a dose-dependent manner in hEM15A and HEC1-B cells. IC50s of FLT in hEM15A cells were 839.30 ± 121.11 or 483.53 ±156.91 μg·ml−1 after the treatment for 24 or 48 h, respectively. In HEC1-B cells, IC50 values of 24 or 48 h were 625.20 ± 59.52 or 250.30 ± 68.12 μg·ml−1. In addition, FLT significantly inhibited invasion and metastasis in scratch wound and transwell assay. Furthermore, FLT inactivated MMP/TIMP signaling with decreasing expression of MMP-2/9, and an enhancing expression of TIMP-1. Conclusions MMP/TIMP inactivation is a reasonable explanation for the inhibition of FLT on invasion and metastasis in endometriosis. This result reveals a potential mechanism on the role of FLT in endometriosis and may benefit for its further application.

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Wang, Zan-Ying, Wen-Qiong Liu, Si’e Wang, and Zeng-Tao Wei. "Fisetin induces G2/M phase cell cycle arrest by inactivating cdc25C-cdc2 via ATM-Chk1/2 activation in human endometrial cancer cells." Bangladesh Journal of Pharmacology 10, no. 2 (April 3, 2015): 279. http://dx.doi.org/10.3329/bjp.v10i2.21945.

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<p>Endometrial cancer is one of the most prevalent gynaecological malignancies where, currently available therapeutic options remain limited. Recently phytochemicals are exploited for their efficiency in cancer therapy. The present study investigates the anti-proliferative effect of fisetin, a flavonoid on human endometrial cancer cells (KLE and Hec1 A). Fisetin (20-100 µM) effectively reduced the viability of Hec1 A and KLE cells and potentially altered the cell population at G2/M stage. Expression levels of the cell cycle proteins (cyclin B1, p-Cdc2, p-Cdc25C, p-Chk1, Chk2, p-ATM, cyclin B1, H2AX, p21 and p27) were analyzed. Fisetin suppressed cyclin B1 expression and caused inactiva-tion of Cdc25C and Cdc2 by increasing their phosphorylation levels and further activated ATM, Chk1 and Chk2. Increased levels of p21 and p27 were observed as well. These results suggest that fisetin induced G2/M cell cycle arrest via inactivating Cdc25c and Cdc2 through activation of ATM, Chk1 and Chk2.</p><p> </p><p> </p>

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Kuhn, Jonathan, and Sophie Dumont. "Mammalian kinetochores count attached microtubules in a sensitive and switch-like manner." Journal of Cell Biology 218, no. 11 (September 6, 2019): 3583–96. http://dx.doi.org/10.1083/jcb.201902105.

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The spindle assembly checkpoint (SAC) prevents anaphase until all kinetochores attach to the spindle. Each mammalian kinetochore binds many microtubules, but how many attached microtubules are required to turn off the checkpoint, and how the kinetochore monitors microtubule numbers, are not known and are central to understanding SAC mechanisms and function. To address these questions, here we systematically tune and fix the fraction of Hec1 molecules capable of microtubule binding. We show that Hec1 molecules independently bind microtubules within single kinetochores, but that the kinetochore does not independently process attachment information from different molecules. Few attached microtubules (20% occupancy) can trigger complete Mad1 loss, and Mad1 loss is slower in this case. Finally, we show using laser ablation that individual kinetochores detect changes in microtubule binding, not in spindle forces that accompany attachment. Thus, the mammalian kinetochore responds specifically to the binding of each microtubule and counts microtubules as a single unit in a sensitive and switch-like manner. This may allow kinetochores to rapidly react to early attachments and maintain a robust SAC response despite dynamic microtubule numbers.

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Gurzov, E. N., and M. Izquierdo. "RNA interference against Hec1 inhibits tumor growth in vivo." Gene Therapy 13, no. 1 (August 25, 2005): 1–7. http://dx.doi.org/10.1038/sj.gt.3302595.

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Zhu, Z. B., B. Lu, M. Numnum, S. K. Makhija, M. Wang, P. Reynolds, G. P. Siegal, and D. T. Curiel. "227 RNA interference against Hec1 targets malignant mesothelioma (MM)." Lung Cancer 54 (October 2006): S55. http://dx.doi.org/10.1016/s0169-5002(07)70303-3.

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Zihala, David, Tereza Sevcikova, Michal Simicek, Tereza Popkova, Hana Plonkova, Lucie Broskevicova, Jan Vrana, et al. "Identification of Molecular Mechanisms Responsible for the Development of Extramedullary Disease in Myeloma and Potential Novel Therapeutic Targets Using Transcriptomic and Exome Profiling." Blood 136, Supplement 1 (November 5, 2020): 16–17. http://dx.doi.org/10.1182/blood-2020-142300.

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Introduction: Multiple myeloma (MM) is the second most common blood cancer, and despite recent treatment advances, the majority of patients will ultimately die due to progression. Extramedullary disease (EMD) is a less frequent manifestation of MM often occurring during the course of disease where tumor plasma cells become independent of bone marrow microenvironment and infiltrate other tissues and organs. The development of EMD is always considered a high-risk feature with poor prognosis. Aim: To identify molecular mechanisms responsible for the development of EMD using DNA and RNA sequencing and thus reveal potentially novel druggable targets. Currently, available anti-myeloma agents are not effective in patients with EMD. Thus it is critical to perform this kind of translational research that will ultimately lead to discovering new treatment strategies in this prognostically poor subset of MM patients. Methods: We collected a unique set of FACS/MACS sorted aberrant plasma cells from 4 freshly obtained EMD samples from relapse and their respective cryopreserved bone marrow samples from diagnosis (available in 3 cases). In the 3 longitudinal ND and EMD samples we analyzed somatic mutations in the whole-exome sequencing data (Illumina, Sure select V6) using a combination of Mutect2 and Strelka2. To analyze differential gene expression, we used Deseq2 R package and Salmon for read mapping and quantification and Cytospace for the pathway enrichment analysis. Besides, to investigate the effect of cryopreservation on the gene expression in longitudinal samples from diagnosis, we compared all 4 EMD samples with 5 fresh unrelated BM samples from ND patients with PET/CT confirmed lack of EMD. Results: Analysis of somatic mutations revealed an only partial overlap of mutated genes between ND and respective EMD sample (23% on average) and 1.49x increased number of variants in EMD. In our samples (ND and EMD), we identified 11 mutated myeloma drivers (Walker 2018) that mostly affected epigenetic processes and MAPK pathway, with the latter being mutated in all three patients in both stages. Interestingly, we identified two genes, both exclusively mutated only in 2/3 EMD samples and not mutated in any ND sample, DNAJC16 and HERC1. DNAJC16 is a member of heat shock proteins (Hsp40; Kampinga 2009). HERC1 is an E3 ubiquitin ligase that regulates p38 signaling and cell migration (Padrazza 2020), and thus, it represents a potentially interesting target for further analysis of EMD development. Differential expression analysis of 3 paired ND-EMD samples revealed 131 deregulated transcripts with the TNFSF9 (CD137L) ligand, HECW1 ubiquitin ligase, and UNC13C gene being top upregulated genes. Among the top downregulated were immunoglobulin genes and S1PR4 signaling receptor, MPO myeloperoxidase, and SLAMF1 (CD150) signaling lymphocytic activation molecule. Analysis of a larger cohort of fresh unpaired 5 ND and 4 EMD samples resulted in more distinct clusters of ND/EMD samples and the total number of 673 deregulated genes (Fig. 1). EMD downregulated genes mostly belong to cell adhesion, chemokine signaling pathway, and neutrophil activation process. Upregulated genes belong to proliferation, cell cycle, and DNA damage signaling pathways. Evaluation of currently available druggable targets revealed that only LAG3 (lymphocyte activation 3 protein) is significantly downregulated in EMD. For three upregulated genes (FGFR3, NTRK3, EZH2), we found interaction with potential cancer inhibitors (Erdafitinib, Entrectinib, Tazemetostat). Notably, the latter agent targeting EZH2 methyltransferase gene has been recently approved by the FDA for follicular lymphoma treatment, and clinical trials for MM are ongoing. Conclusion: Here, we report the preliminary analysis of the genomic and transcriptomic profile of EMD samples with their respective paired samples from the new diagnosis. The genomic alterations proved to be heterogeneous; though, we were able to identify 2 genes exclusively mutated in EMD samples. Moreover, deregulated transcriptome clearly separated ND and EMD stage in unrelated cohorts and pointed to rapid proliferation and increased DNA damage response pathways and pinpointed several potential drug targets. However, our findings warrant a more in-depth analysis on the bigger patient cohort. Acknowledgement: Work was supported by project ENOCH (No. CZ.02.1.01/0.0/0.0/16_019/0000868) Figure 1 Disclosures No relevant conflicts of interest to declare.

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Lee, Sanghwa, Ling Zhu, and Enamul Huq. "An autoregulatory negative feedback loop controls thermomorphogenesis in Arabidopsis." PLOS Genetics 17, no. 6 (June 1, 2021): e1009595. http://dx.doi.org/10.1371/journal.pgen.1009595.

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Plant growth and development are acutely sensitive to high ambient temperature caused in part due to climate change. However, the mechanism of high ambient temperature signaling is not well defined. Here, we show that HECATEs (HEC1 and HEC2), two helix-loop-helix transcription factors, inhibit thermomorphogenesis. While the expression of HEC1 and HEC2 is increased and HEC2 protein is stabilized at high ambient temperature, hec1hec2 double mutant showed exaggerated thermomorphogenesis. Analyses of the four PHYTOCHROME INTERACTING FACTOR (PIF1, PIF3, PIF4 and PIF5) mutants and overexpression lines showed that they all contribute to promote thermomorphogenesis. Furthermore, genetic analysis showed that pifQ is epistatic to hec1hec2. HECs and PIFs oppositely control the expression of many genes in response to high ambient temperature. PIFs activate the expression of HECs in response to high ambient temperature. HEC2 in turn interacts with PIF4 both in yeast and in vivo. In the absence of HECs, PIF4 binding to its own promoter as well as the target gene promoters was enhanced, indicating that HECs control PIF4 activity via heterodimerization. Overall, these data suggest that PIF4-HEC forms an autoregulatory composite negative feedback loop that controls growth genes to modulate thermomorphogenesis.

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Iemura, Kenji, Yujiro Yoshizaki, Kinue Kuniyasu, and Kozo Tanaka. "Attenuated Chromosome Oscillation as a Cause of Chromosomal Instability in Cancer Cells." Cancers 13, no. 18 (September 9, 2021): 4531. http://dx.doi.org/10.3390/cancers13184531.

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Chromosomal instability (CIN) is commonly seen in cancer cells, and related to tumor progression and poor prognosis. Among the causes of CIN, insufficient correction of erroneous kinetochore (KT)-microtubule (MT) attachments plays pivotal roles in various situations. In this review, we focused on the previously unappreciated role of chromosome oscillation in the correction of erroneous KT-MT attachments, and its relevance to the etiology of CIN. First, we provided an overview of the error correction mechanisms for KT-MT attachments, especially the role of Aurora kinases in error correction by phosphorylating Hec1, which connects MT to KT. Next, we explained chromosome oscillation and its underlying mechanisms. Then we introduced how chromosome oscillation is involved in the error correction of KT-MT attachments, based on recent findings. Chromosome oscillation has been shown to promote Hec1 phosphorylation by Aurora A which localizes to the spindle. Finally, we discussed the link between attenuated chromosome oscillation and CIN in cancer cells. This link underscores the role of chromosome dynamics in mitotic fidelity, and the mutual relationship between defective chromosome dynamics and CIN in cancer cells that can be a target for cancer therapy.

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Mehta, Ajay, Samantha Seymour, William Wilson, and Christina Peroutka. "eP188: Novel HECW2 variant presenting with tachypnea and multisystemic congenital malformations." Genetics in Medicine 24, no. 3 (March 2022): S116. http://dx.doi.org/10.1016/j.gim.2022.01.224.

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Krishnamoorthy, Vidhya, Richa Khanna, and Veena K. Parnaik. "E3 ubiquitin ligase HECW2 mediates the proteasomal degradation of HP1 isoforms." Biochemical and Biophysical Research Communications 503, no. 4 (September 2018): 2478–84. http://dx.doi.org/10.1016/j.bbrc.2018.07.003.

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Diaz-Rodriguez, Elena. "Targeting the Kinetochore in Cancer Therapy: The Ndc80/Hec1 Complex." Current Drug Therapy 5, no. 1 (February 1, 2010): 29–35. http://dx.doi.org/10.2174/1574885511005010029.

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Hua, Shasha, Zhikai Wang, Kai Jiang, Yuejia Huang, Tarsha Ward, Lingli Zhao, Zhen Dou, and Xuebiao Yao. "CENP-U Cooperates with Hec1 to Orchestrate Kinetochore-Microtubule Attachment." Journal of Biological Chemistry 286, no. 2 (November 5, 2010): 1627–38. http://dx.doi.org/10.1074/jbc.m110.174946.

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DeLuca, Jennifer G., Walter E. Gall, Claudio Ciferri, Daniela Cimini, Andrea Musacchio, and E. D. Salmon. "Kinetochore Microtubule Dynamics and Attachment Stability Are Regulated by Hec1." Cell 127, no. 5 (December 2006): 969–82. http://dx.doi.org/10.1016/j.cell.2006.09.047.

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Vincent, Soriano. "Hepatitis B Virus Infection Despite Receiving Lamivudine in One HIV-Infected Person." HIV Clinical Trials 4, no. 1 (February 2003): 77–78. http://dx.doi.org/10.1310/6dmu-hec1-eax7-rlun.

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Wei, Xiaomou, Chunhai Gao, Jia Luo, Wei Zhang, Shuhao Qi, Weijun Liang, and Shengming Dai. "Hec1 inhibition alters spindle morphology and chromosome alignment in porcine oocytes." Molecular Biology Reports 41, no. 8 (April 22, 2014): 5089–95. http://dx.doi.org/10.1007/s11033-014-3374-4.

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35

Wei, Ronnie R., Jawdat Al-Bassam, and Stephen C. Harrison. "The Ndc80/HEC1 complex is a contact point for kinetochore-microtubule attachment." Nature Structural & Molecular Biology 14, no. 1 (December 31, 2006): 54–59. http://dx.doi.org/10.1038/nsmb1186.

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DeLuca, K. F., S. M. A. Lens, and J. G. DeLuca. "Temporal changes in Hec1 phosphorylation control kinetochore-microtubule attachment stability during mitosis." Journal of Cell Science 124, no. 4 (January 25, 2011): 622–34. http://dx.doi.org/10.1242/jcs.072629.

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Diaz-Rodriguez, E., R. Sotillo, J. M. Schvartzman, and R. Benezra. "Hec1 overexpression hyperactivates the mitotic checkpoint and induces tumor formation in vivo." Proceedings of the National Academy of Sciences 105, no. 43 (October 21, 2008): 16719–24. http://dx.doi.org/10.1073/pnas.0803504105.

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38

Qu, Ying, Jianfang Li, Qu Cai, and Bingya Liu. "Hec1/Ndc80 is overexpressed in human gastric cancer and regulates cell growth." Journal of Gastroenterology 49, no. 3 (April 17, 2013): 408–18. http://dx.doi.org/10.1007/s00535-013-0809-y.

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Mattiuzzo, Marta, Giulia Vargiu, Pierangela Totta, Mario Fiore, Claudio Ciferri, Andrea Musacchio, and Francesca Degrassi. "Abnormal Kinetochore-Generated Pulling Forces from Expressing a N-Terminally Modified Hec1." PLoS ONE 6, no. 1 (January 28, 2011): e16307. http://dx.doi.org/10.1371/journal.pone.0016307.

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Nakamura, Haruhiko, Mitsugu Uematsu, Yurika Numata-Uematsu, Yu Abe, Wakaba Endo, Atsuo Kikuchi, Yusuke Takezawa, et al. "Rett-like features and cortical visual impairment in a Japanese patient with HECW2 mutation." Brain and Development 40, no. 5 (May 2018): 410–14. http://dx.doi.org/10.1016/j.braindev.2017.12.015.

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Orticello, M., M. Fiore, P. Totta, M. Desideri, M. Barisic, D. Passeri, J. Lenzi, et al. "N-terminus-modified Hec1 suppresses tumour growth by interfering with kinetochore–microtubule dynamics." Oncogene 34, no. 25 (August 18, 2014): 3325–35. http://dx.doi.org/10.1038/onc.2014.265.

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Zhao, Gangyin, Yubao Cheng, Ping Gui, Meiying Cui, Wei Liu, Wenwen Wang, Xueying Wang, et al. "Dynamic acetylation of the kinetochore-associated protein HEC1 ensures accurate microtubule–kinetochore attachment." Journal of Biological Chemistry 294, no. 2 (November 8, 2018): 576–92. http://dx.doi.org/10.1074/jbc.ra118.003844.

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Martin-Lluesma, S. "Role of Hec1 in Spindle Checkpoint Signaling and Kinetochore Recruitment of Mad1/Mad2." Science 297, no. 5590 (September 27, 2002): 2267–70. http://dx.doi.org/10.1126/science.1075596.

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44

Chang, Howard C., Jennifer Paek, and Dennis H. Kim. "Natural polymorphisms in C. elegans HECW-1 E3 ligase affect pathogen avoidance behaviour." Nature 480, no. 7378 (November 16, 2011): 525–29. http://dx.doi.org/10.1038/nature10643.

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45

Long, Alexandra F., Dylan B. Udy, and Sophie Dumont. "Hec1 Tail Phosphorylation Differentially Regulates Mammalian Kinetochore Coupling to Polymerizing and Depolymerizing Microtubules." Current Biology 27, no. 11 (June 2017): 1692–99. http://dx.doi.org/10.1016/j.cub.2017.04.058.

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Huang, Lynn YL, Chia-chi Chang, Ying-Shuan Lee, Jiann-Jyh Huang, Shih-Hsien Chuang, Jia-Ming Chang, Kuo-Jang Kao, et al. "Inhibition of Hec1 as a novel approach for treatment of primary liver cancer." Cancer Chemotherapy and Pharmacology 74, no. 3 (July 20, 2014): 511–20. http://dx.doi.org/10.1007/s00280-014-2540-7.

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Guimaraes, Geoffrey J., Yimin Dong, Bruce F. McEwen, and Jennifer G. DeLuca. "Kinetochore-Microtubule Attachment Relies on the Disordered N-Terminal Tail Domain of Hec1." Current Biology 18, no. 22 (November 2008): 1778–84. http://dx.doi.org/10.1016/j.cub.2008.08.012.

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Ciferri, Claudio, Jennifer De Luca, Silvia Monzani, Karin J. Ferrari, Dejan Ristic, Claire Wyman, Holger Stark, John Kilmartin, Edward D. Salmon, and Andrea Musacchio. "Architecture of the Human Ndc80-Hec1 Complex, a Critical Constituent of the Outer Kinetochore." Journal of Biological Chemistry 280, no. 32 (June 16, 2005): 29088–95. http://dx.doi.org/10.1074/jbc.m504070200.

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Qiu, Xiao-Long, Guideng Li, Guikai Wu, Jiewen Zhu, Longen Zhou, Phang-Lang Chen, A. Richard Chamberlin, and Wen-Hwa Lee. "Synthesis and Biological Evaluation of a Series of Novel Inhibitor of Nek2/Hec1 Analogues." Journal of Medicinal Chemistry 52, no. 6 (March 26, 2009): 1757–67. http://dx.doi.org/10.1021/jm8015969.

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Mo, Qing-qing, Ping-bo Chen, Xin Jin, Qian Chen, Lan Tang, Bei-bei Wang, Ke-zhen Li, et al. "Inhibition of Hec1 expression enhances the sensitivity of human ovarian cancer cells to paclitaxel." Acta Pharmacologica Sinica 34, no. 4 (March 11, 2013): 541–48. http://dx.doi.org/10.1038/aps.2012.197.

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