CDK5 Antibody

Total Page：16

File Type：pdf, Size：1020Kb

Product Datasheet CDK5 Antibody Catalog No: #31054 Package Size: #31054-1 50ul #31054-2 100ul Orders: [email protected] Support: [email protected] Description Product Name CDK5 Antibody Host Species Rabbit Clonality Polyclonal Applications E WB IHC Species Reactivity Hu Ms Specificity The antibody detects endogenous level of total CDK5 protein. Immunogen Type Recombinant Protein Immunogen Description Full length fusion protein Target Name CDK5 Other Names cyclin-dependent kinase 5, PSSALRE Accession No. Genbank No.: BC005115 Formulation Supplied at 0.8mg/mL in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.3, 0.05% sodium azide and 50% glycerol. Storage Store at -20°C/1 year Application Details Predicted MW: 33kd ELISA: 1:1000-1:2000 Western blotting: 1:200-1:1000 Immunohistochemistry: 1:10-1:50 Images Gel: 12%+10%SDS-PAGE Lysate: 30 µg Hela cell lysate Primary antibody: 1/400 dilution Secondary antibody: Goat anti Rabbit IgG - H&L (HRP) at 1/10000 dilution Exposure time: 1 minute Address: 8400 Baltimore Ave. Suite 302 College Park MD 20740 USA http://www.sabbiotech.com 1 The image on the left is immunohistochemistry of paraffin-embedded Human brain tissue using 31054(CDK5 Antibody) at dilution 1/10, on the right is treated with the fusion protein. Background Cell division protein kinase 5?is an?enzyme?that in humans is encoded by the?CDK5?gene.?The protein encoded by this gene is part of the?cyclin-dependent kinase?family. CDK5 is required for proper development of the brain and to be activated, CDK5 must associate with CDK5R1 or CDK5R2. Cdk5 is involved in the processes of neuronal maturation and migration, phosphorylating the key intracellular adaptor of the reelin signaling chain. Experiments performed on mice lacking p35, a necessary activator of cdk5 in early brain development, showed that the normal layering of neurons was reversed in the cortex. This disrupted lamination again implicated cdk5 in neuronal migration and plasticity. Cdk5 is also involved in the regulation of synaptic vesicle exocytosis via phosphorylation of munc-18. Note: This product is for in vitro research use only and is not intended for use in humans or animals. Address: 8400 Baltimore Ave. Suite 302 College Park MD 20740 USA http://www.sabbiotech.com 2.

Copy Link

Recommended publications

Mutations in CDK5RAP2 Cause Seckel Syndrome Go¨ Khan Yigit1,2,3,A, Karen E
ORIGINAL ARTICLE Mutations in CDK5RAP2 cause Seckel syndrome Go¨ khan Yigit1,2,3,a, Karen E. Brown4,a,Hu¨ lya Kayserili5, Esther Pohl1,2,3, Almuth Caliebe6, Diana Zahnleiter7, Elisabeth Rosser8, Nina Bo¨ gershausen1,2,3, Zehra Oya Uyguner5, Umut Altunoglu5, Gudrun Nu¨ rnberg2,3,9, Peter Nu¨ rnberg2,3,9, Anita Rauch10, Yun Li1,2,3, Christian Thomas Thiel7 & Bernd Wollnik1,2,3 1Institute of Human Genetics, University of Cologne, Cologne, Germany 2Center for Molecular Medicine Cologne (CMMC), University of Cologne, Cologne, Germany 3Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne, Cologne, Germany 4Chromosome Biology Group, MRC Clinical Sciences Centre, Imperial College School of Medicine, Hammersmith Hospital, London, W12 0NN, UK 5Department of Medical Genetics, Istanbul Medical Faculty, Istanbul University, Istanbul, Turkey 6Institute of Human Genetics, Christian-Albrechts-University of Kiel, Kiel, Germany 7Institute of Human Genetics, Friedrich-Alexander University Erlangen-Nuremberg, Erlangen, Germany 8Department of Clinical Genetics, Great Ormond Street Hospital for Children, London, WC1N 3EH, UK 9Cologne Center for Genomics, University of Cologne, Cologne, Germany 10Institute of Medical Genetics, University of Zurich, Schwerzenbach-Zurich, Switzerland Keywords Abstract CDK5RAP2, CEP215, microcephaly, primordial dwarﬁsm, Seckel syndrome Seckel syndrome is a heterogeneous, autosomal recessive disorder marked by pre- natal proportionate short stature, severe microcephaly, intellectual disability, and Correspondence characteristic facial features. Here, we describe the novel homozygous splice-site Bernd Wollnik, Center for Molecular mutations c.383+1G>C and c.4005-9A>GinCDK5RAP2 in two consanguineous Medicine Cologne (CMMC) and Institute of families with Seckel syndrome. CDK5RAP2 (CEP215) encodes a centrosomal pro- Human Genetics, University of Cologne, tein which is known to be essential for centrosomal cohesion and proper spindle Kerpener Str.
[Show full text]
Neuroprotective Role of Intermittent Fasting in Senescence-Accelerated Mice P8 (SAMP8) M
Neuroprotective role of intermittent fasting in senescence-accelerated mice P8 (SAMP8) M. Tajes, J. Gutierrez-Cuesta, J. Folch, D. Ortuño-Sahagun, E. Verdaguer, A. Jiménez, F. Junyent, A. Lau, A. Camins, M. Pallàs To cite this version: M. Tajes, J. Gutierrez-Cuesta, J. Folch, D. Ortuño-Sahagun, E. Verdaguer, et al.. Neuroprotective role of intermittent fasting in senescence-accelerated mice P8 (SAMP8). Experimental Gerontology, Elsevier, 2010, 45 (9), pp.702. 10.1016/j.exger.2010.04.010. hal-00615111 HAL Id: hal-00615111 https://hal.archives-ouvertes.fr/hal-00615111 Submitted on 18 Aug 2011 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. ÔØ ÅÒÙ×Ö ÔØ Neuroprotective role of intermittent fasting in senescence-accelerated mice P8 (SAMP8) M. Tajes, J. Gutierrez-Cuesta, J. Folch, D. Ortuño-Sahagun, E. Verda- guer, A. Jiménez,F. Junyent, A. Lau, A. Camins, M. Pallàs PII: S0531-5565(10)00188-9 DOI: doi: 10.1016/j.exger.2010.04.010 Reference: EXG 8747 To appear in: Experimental Gerontology Received date: 25 December 2009 Revised date: 23 April 2010 Accepted date: 29 April 2010 Please cite this article as: Tajes, M., Gutierrez-Cuesta, J., Folch, J., Ortuño-Sahagun, D., Verdaguer, E., Jiménez, A., Junyent, F., Lau, A., Camins, A., Pallàs, M., Neuroprotec- tive role of intermittent fasting in senescence-accelerated mice P8 (SAMP8), Experimental Gerontology (2010), doi: 10.1016/j.exger.2010.04.010 This is a PDF file of an unedited manuscript that has been accepted for publication.
[Show full text]
Transcriptomic and Open Chromatin Atlas of High-Resolution Anatomical Regions in the Rhesus Macaque Brain
ARTICLE https://doi.org/10.1038/s41467-020-14368-z OPEN Transcriptomic and open chromatin atlas of high-resolution anatomical regions in the rhesus macaque brain Senlin Yin1,7, Keying Lu1,7, Tao Tan2,3,4,7, Jie Tang 1,7, Jingkuan Wei3, Xu Liu5, Xinlei Hu1, Haisu Wan5, Wei Huang6, Yong Fan4*, Dan Xie 1* & Yang Yu 2* 1234567890():,; The rhesus macaque is a prime model animal in neuroscience. A comprehensive tran- scriptomic and open chromatin atlas of the rhesus macaque brain is key to a deeper understanding of the brain. Here we characterize the transcriptome of 416 brain samples from 52 regions of 8 rhesus macaque brains. We identify gene modules associated with specific brain regions like the cerebral cortex, pituitary, and thalamus. In addition, we discover 9703 novel intergenic transcripts, including 1701 coding transcripts and 2845 lncRNAs. Most of the novel transcripts are only expressed in specific brain regions or cortical regions of specific individuals. We further survey the open chromatin regions in the hippocampal CA1 and several cerebral cortical regions of the rhesus macaque brain using ATAC-seq, revealing CA1- and cortex-specific open chromatin regions. Our results add to the growing body of knowledge regarding the baseline transcriptomic and open chromatin profiles in the brain of the rhesus macaque. 1 Frontier Science Center for Disease Molecular Network, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, 610041 Chengdu, China. 2 Department of Obstetrics and Gynecology, Peking University Third Hospital, 100191 Beijing, China. 3 Yunnan Key Laboratory of Primate Biomedical Research, Institute of Primate Translational Medicine, Kunming University of Science and Technology, 650500 Kunming, Yunnan, China.
[Show full text]
1471-2105-8-S9-S6.Pdf
BMC Bioinformatics BioMed Central Proceedings Open Access Extracting unrecognized gene relationships from the biomedical literature via matrix factorizations Hyunsoo Kim, Haesun Park* and Barry L Drake Address: College of Computing, Georgia Institute of Technology, Atlanta, GA 30332, USA Email: Hyunsoo Kim - [email protected]; Haesun Park* - [email protected]; Barry L Drake - [email protected] * Corresponding author from First International Workshop on Text Mining in Bioinformatics (TMBio) 2006 Arlington, VA, USA. 10 November 2006 Published: 27 November 2007 BMC Bioinformatics 2007, 8(Suppl 9):S6 doi:10.1186/1471-2105-8-S9-S6 <supplement> <title> <p>First International Workshop on Text Mining in Bioinformatics (TMBio) 2006</p> </title> <editor>Min Song and Zoran Obradovic</editor> <note>Proceedings</note> </supplement> This article is available from: http://www.biomedcentral.com/1471-2105/8/S9/S6 © 2007 Kim et al; licensee BioMed Central Ltd. Abstract Background: The construction of literature-based networks of gene-gene interactions is one of the most important applications of text mining in bioinformatics. Extracting potential gene relationships from the biomedical literature may be helpful in building biological hypotheses that can be explored further experimentally. Recently, latent semantic indexing based on the singular value decomposition (LSI/SVD) has been applied to gene retrieval. However, the determination of the number of factors k used in the reduced rank matrix is still an open problem. Results: In this paper, we introduce a way to incorporate a priori knowledge of gene relationships into LSI/SVD to determine the number of factors. We also explore the utility of the non-negative matrix factorization (NMF) to extract unrecognized gene relationships from the biomedical literature by taking advantage of known gene relationships.
[Show full text]
Downloaded from in December 2015)
cells Article Proteomic Analysis of Hydromethylthionine in the Line 66 Model of Frontotemporal Dementia Demonstrates Actions on Tau-Dependent and Tau-Independent Networks Karima Schwab 1,2, Valeria Melis 1, Charles R. Harrington 1,3 , Claude M. Wischik 1,3, Mandy Magbagbeolu 2, Franz Theuring 2,† and Gernot Riedel 1,*,† 1 School of Medicine, Medical Sciences and Nutrition, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD, UK; [email protected] (K.S.); [email protected] (V.M.); [email protected] (C.R.H.); [email protected] (C.M.W.) 2 Charité—Universitätsmedizin Berlin, Hessische Str. 3-4, 10115 Berlin, Germany; [email protected] (M.M.); [email protected] (F.T.) 3 TauRx Therapeutics Ltd., 395 King Street, Aberdeen AB24 5RP, UK * Correspondence: [email protected] † Equal contribution (co-last author). Abstract: Abnormal aggregation of tau is the pathological hallmark of tauopathies including fron- totemporal dementia (FTD). We have generated tau-transgenic mice that express the aggregation- prone P301S human tau (line 66). These mice present with early-onset, high tau load in brain and FTD-like behavioural deﬁciencies. Several of these behavioural phenotypes and tau pathology are reversed by treatment with hydromethylthionine but key pathways underlying these corrections Citation: Schwab, K.; Melis, V.; Harrington, C.R.; Wischik, C.M.; remain elusive. In two proteomic experiments, line 66 mice were compared with wild-type mice Magbagbeolu, M.; Theuring, F.; and then vehicle and hydromethylthionine treatments of line 66 mice were compared. The brain Riedel, G. Proteomic Analysis of proteome was investigated using two-dimensional electrophoresis and mass spectrometry to iden- Hydromethylthionine in the Line 66 tify protein networks and pathways that were altered due to tau overexpression or modiﬁed by Model of Frontotemporal Dementia hydromethylthionine treatment.
[Show full text]
CDK5R1(P35) Antibody (C-Term) Purified Rabbit Polyclonal Antibody (Pab) Catalog # Ap7743b
10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 CDK5R1(p35) Antibody (C-term) Purified Rabbit Polyclonal Antibody (Pab) Catalog # AP7743b Specification CDK5R1(p35) Antibody (C-term) - Product Information Application WB, IHC-P,E Primary Accession Q15078 Other Accession P61810, P61809, Q28199 Reactivity Human Predicted Bovine, Mouse, Rat Host Rabbit Clonality Polyclonal Isotype Rabbit Ig Calculated MW 34060 Antigen Region 272-301 CDK5R1 Antibody (C-term) (Cat. #AP7743b) CDK5R1(p35) Antibody (C-term) - Additional western blot analysis in A2058 cell line Information lysates (35ug/lane).This demonstrates the CDK5R1 antibody detected the CDK5R1 Gene ID 8851 protein (arrow). Other Names Cyclin-dependent kinase 5 activator 1, CDK5 activator 1, Cyclin-dependent kinase 5 regulatory subunit 1, TPKII regulatory subunit, Cyclin-dependent kinase 5 activator 1, p35, p35, Cyclin-dependent kinase 5 activator 1, p25, p25, Tau protein kinase II 23 kDa subunit, p23, CDK5R1, CDK5R, NCK5A Target/Specificity This CDK5R1(p35) antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between Formalin-fixed and paraffin-embedded 272-301 amino acids from the C-terminal human brain tissue reacted with region of human CDK5R1(p35). CDK5R1(p35) Antibody (C-term) (Cat.#AP7743b), which was Dilution peroxidase-conjugated to the secondary WB~~1:1000 antibody, followed by DAB staining. This data IHC-P~~1:10~50 demonstrates the use of this antibody for immunohistochemistry; clinical relevance has Format not been evaluated. Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A CDK5R1(p35) Antibody (C-term) - column, followed by peptide affinity Background Page 1/3 10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 purification.
[Show full text]
Extracting Unrecognized Gene Relationships from the Biomedical Literature Via Matrix Factorizations
Extracting Unrecognized Gene Relationships from the Biomedical Literature via Matrix Factorizations Hyunsoo Kim∗1, Haesun Park∗1 and Barry L. Drake1 1 College of Computing, Georgia Institute of Technology, 266 Ferst Drive, Atlanta, GA 30332, USA. Email: H. Kim∗- [email protected]; H. Park∗- [email protected]; B. L. Drake - [email protected]; ∗Corresponding author Abstract Background: The construction of literature-based networks of gene-gene interactions is one of the most important applications of text mining in bioinformatics. Extracting potential gene relationships from the biomedical literature may be helpful in building biological hypotheses that can be explored further experimentally. Recently, latent semantic indexing based on the singular value decomposition (LSI/SVD) has been applied to gene retrieval. However, the determination of the number of factors k used in the reduced rank matrix is still an open problem. Results: In this paper, we introduce a way to incorporate a priori knowledge of gene relationships into LSI/SVD to determine the number of factors. We also explore the utility of the non-negative matrix factorization (NMF) to extract unrecognized gene relationships from the biomedical literature by taking advantage of known gene relationships. A gene retrieval method based on NMF (GR/NMF) showed comparable performance with LSI/SVD. Conclusions: Using known gene relationships of a given gene, we can determine the number of factors used in the reduced rank matrix and retrieve unrecognized genes related with the given gene by LSI/SVD or GR/NMF. 1 Background Latent semantic indexing based on the singular value decomposition (LSI/SVD) [1, 2] uses the truncated singular value decomposition as a low-rank approximation of a term-by-document matrix.
[Show full text]
SUPPLEMENTARY MATERIALS and METHODS PBMC Transcriptomics
BMJ Publishing Group Limited (BMJ) disclaims all liability and responsibility arising from any reliance Supplemental material placed on this supplemental material which has been supplied by the author(s) Gut SUPPLEMENTARY MATERIALS AND METHODS PBMC transcriptomics identifies immune-metabolism disorder during the development of HBV-ACLF Contents l Supplementary methods l Supplementary Figure 1 l Supplementary Figure 2 l Supplementary Figure 3 l Supplementary Figure 4 l Supplementary Figure 5 l Supplementary Table 1 l Supplementary Table 2 l Supplementary Table 3 l Supplementary Table 4 l Supplementary Tables 5-14 l Supplementary Table 15 l Supplementary Table 16 l Supplementary Table 17 Li J, et al. Gut 2021;0:1–13. doi: 10.1136/gutjnl-2020-323395 BMJ Publishing Group Limited (BMJ) disclaims all liability and responsibility arising from any reliance Supplemental material placed on this supplemental material which has been supplied by the author(s) Gut SUPPLEMENTARY METHODS Test for HBV DNA The levels of HBV DNA were detected using real-time PCR with a COBAS® AmpliPrep/COBAS® TaqMan 48 System (Roche, Basel, Switzerland) and HBV Test v2.0. Criteria for diagnosing cirrhosis Pathology The gold standard for the diagnosis of cirrhosis is a liver biopsy obtained through a percutaneous or transjugular approach.1 Ultrasonography was performed 2-4 hours before biopsy. Liver biopsy specimens were obtained by experienced physicians. Percutaneous transthoracic puncture of the liver was performed according to the standard criteria. After biopsy, patients were monitored in the hospital with periodic analyses of haematocrit and other vital signs for 24 hours. Cirrhosis was diagnosed according to the globally agreed upon criteria.2 Cirrhosis is defined based on its pathological features under a microscope: (a) the presence of parenchymal nodules, (b) differences in liver cell size and appearance, (c) fragmentation of the biopsy specimen, (d) fibrous septa, and (d) an altered architecture and vascular relationships.
[Show full text]
Tissue-Type Plasminogen Activator Regulates P35-Mediated Cdk5
© 2019. Published by The Company of Biologists Ltd | Journal of Cell Science (2019) 132, jcs224196. doi:10.1242/jcs.224196 RESEARCH ARTICLE Tissue-type plasminogen activator regulates p35-mediated Cdk5 activation in the postsynaptic terminal Ariel Diaz1,*, Valerie Jeanneret2,*, Paola Merino1, Patrick McCann1 and Manuel Yepes1,2,3,‡ ABSTRACT functional and structural changes in the synapse required for the Neuronal depolarization induces the synaptic release of tissue-type development of long-term potentiation (Qian et al., 1993), learning plasminogen activator (tPA). Cyclin-dependent kinase-5 (Cdk5) is a (Seeds et al., 1995), stress-induced anxiety (Pawlak et al., 2003) and member of the family of cyclin-dependent kinases that regulates cell visual cortex plasticity (Müller and Griesinger, 1998). Interestingly, migration and synaptic function in postmitotic neurons. Cdk5 is activated recent studies indicate that the release of tPA into the synaptic cleft by its binding to p35 (also known as Cdk5r1), a membrane-anchored also modulates the response of the postsynaptic terminal to the protein that is rapidly degraded by the proteasome. Here, we show that presynaptic release of glutamate (Jeanneret et al., 2016), and has a tPA prevents the degradation of p35 in the synapse by a plasminogen- direct effect on the structure and receptor composition of the dependent mechanism that requires open synaptic N-methyl-D- postsynaptic density (PSD) (Jeanneret et al., 2018). aspartate (NMDA) receptors. We show that tPA treatment increases Cyclin-dependent kinase-5 (Cdk5) is a member of the family of the abundance of p35 and its binding to Cdk5 in the postsynaptic density cyclin-dependent kinases found in postmitotic neurons (Dhavan and (PSD).
[Show full text]
Altered Resting-State Functional Connectivity in Hipsc-Derived Neuronal Networks from Schizophrenia Patients
medRxiv preprint doi: https://doi.org/10.1101/2021.08.26.21262277; this version posted August 28, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted medRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license . Manuscript Title: Altered resting-state functional connectivity in hiPSC-derived neuronal networks from schizophrenia patients Short Title: Altered neuronal network dynamics in schizophrenia Authors: Sofía Puvogel1,2,3 a, Kris Blanchard1,2 a, Bárbara S. Casas1, Robyn Miller4,5, Delia Garrido1, Magdalena Sanhueza2#, Verónica Palma1# a These authors contributed equally to this work # Co-Corresponding Authors: Verónica Palma ([email protected]), Phone number (56-2) 2978 7221, Las Encinas 3370. Milenio Building, Floor 3, Ñuñoa, Santiago, Chile. 7800024. Magdalena Sanhueza ([email protected]). Phone number (56-2) 2978 7344. Las Encinas 3370. Milenio Building, Floor 3, Ñuñoa, Santiago, Chile. 7800024 1. Laboratory of Stem Cells and Developmental Biology, Department of Biology, Faculty of Sciences. Universidad de Chile. Santiago, Chile. 2. Cell Physiology Laboratory, Department of Biology, Faculty of Sciences, Universidad de Chile, Santiago, Chile. 3. Current affiliation: Department of Biomedical Sciences of Cells and Systems, University Medical Center Groningen, Groningen, The Netherlands. 4. Georgia State University, Dept of Computer Science, Atlanta GA, USA. 5. Tri-institutional Center for Translational Research in Neuroimaging and Data Science (TReNDS Center), Atlanta, GA, USA 1 NOTE: This preprint reports new research that has not been certified by peer review and should not be used to guide clinical practice.
[Show full text]
Kinome Expression Profiling to Target New Therapeutic Avenues in Multiple Myeloma
Plasma Cell DIsorders SUPPLEMENTARY APPENDIX Kinome expression profiling to target new therapeutic avenues in multiple myeloma Hugues de Boussac, 1 Angélique Bruyer, 1 Michel Jourdan, 1 Anke Maes, 2 Nicolas Robert, 3 Claire Gourzones, 1 Laure Vincent, 4 Anja Seckinger, 5,6 Guillaume Cartron, 4,7,8 Dirk Hose, 5,6 Elke De Bruyne, 2 Alboukadel Kassambara, 1 Philippe Pasero 1 and Jérôme Moreaux 1,3,8 1IGH, CNRS, Université de Montpellier, Montpellier, France; 2Department of Hematology and Immunology, Myeloma Center Brussels, Vrije Universiteit Brussel, Brussels, Belgium; 3CHU Montpellier, Laboratory for Monitoring Innovative Therapies, Department of Biologi - cal Hematology, Montpellier, France; 4CHU Montpellier, Department of Clinical Hematology, Montpellier, France; 5Medizinische Klinik und Poliklinik V, Universitätsklinikum Heidelberg, Heidelberg, Germany; 6Nationales Centrum für Tumorerkrankungen, Heidelberg , Ger - many; 7Université de Montpellier, UMR CNRS 5235, Montpellier, France and 8 Université de Montpellier, UFR de Médecine, Montpel - lier, France ©2020 Ferrata Storti Foundation. This is an open-access paper. doi:10.3324/haematol. 2018.208306 Received: October 5, 2018. Accepted: July 5, 2019. Pre-published: July 9, 2019. Correspondence: JEROME MOREAUX - [email protected] Supplementary experiment procedures Kinome Index A list of 661 genes of kinases or kinases related have been extracted from literature9, and challenged in the HM cohort for OS prognostic values The prognostic value of each of the genes was computed using maximally selected rank test from R package MaxStat. After Benjamini Hochberg multiple testing correction a list of 104 significant prognostic genes has been extracted. This second list has then been challenged for similar prognosis value in the UAMS-TT2 validation cohort.
[Show full text]
Dishevelled Is a NEK2 Kinase Substrate Controlling Dynamics of Centrosomal Linker Proteins
Dishevelled is a NEK2 kinase substrate controlling dynamics of centrosomal linker proteins Igor Cervenkaa, Jana Valnohovaa,1, Ondrej Bernatika,b, Jakub Harnosa, Matej Radsetoulala, Katerina Sedovac, Katerina Hanakovac, David Potesilc, Miroslava Sedlackovad, Alena Salasovaa,e, Zachary Steinhartf, Stephane Angersf, Gunnar Schultea,g, Ales Hampld, Zbynek Zdrahalc,h, and Vitezslav Bryjaa,b,2 aDepartment of Experimental Biology, Faculty of Science, Masaryk University, 61 137 Brno, Czech Republic; bInstitute of Biophysics, Academy of Sciences of Czech Republic, 61 200 Brno, Czech Republic; cResearch Group Proteomics, Central European Institute of Technology, 62 500 Brno, Czech Republic; dDepartment of Histology and Embryology, Faculty of Medicine, Masaryk University, 62 500 Brno, Czech Republic; eDepartment of Biochemistry and Biophysics, Karolinska Institutet Stockholm, 171 77, Sweden; fDepartment of Pharmaceutical Sciences, Leslie Dan Faculty of Pharmacy, University of Toronto, Toronto, ON M5S 3M2, Canada; gReceptor Biology and Signaling, Department of Physiology and Pharmacology, Karolinska Institutet, 17 177 Stockholm, Sweden; and hNational Centre for Biomolecular Research, Faculty of Science, Masaryk University, 625 00 Brno, Czech Republic Edited by Roeland Nusse, Stanford University School of Medicine, Stanford, CA, and approved June 23, 2016 (received for review May 31, 2016) Dishevelled (DVL) is a key scaffolding protein and a branching point cleavage of Rootletin (14) and displacement of C-NAP1 from cen- in Wnt signaling pathways. Here, we present conclusive evidence trosomes (18). Interference with linker proteins or their phosphor- that DVL regulates the centrosomal cycle. We demonstrate that DVL ylation has a drastic effect on cell division (19) and on genome dishevelled and axin (DIX) domain, but not DIX domain-mediated integrity caused by chromosome segregation errors (20).
[Show full text]