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CHF 207.90

The Retinoblastoma Protein

1.Characterization of RB1 Deletions in Interphase and Metaphase by Molecular Cytogenetics Exemplified in Chronic Lymphatic Leukemia Thomas Liehr 2.Detection of RB1 Gene Copy Number Variations using a Multiplex Ligation-Dependent Probe Amplification Method Nejat Dalay 3.A Fluorescent Quantitative Multiplex PCR Method to Detect Copy Number Changes in the RB1 Gene Chitra Kannabiran...

19693616 {"price-changing":0,"image":"https:\/\/image.vergleiche.ch\/small\/aHR0cHM6Ly9pLndlbHRiaWxkLmRlL3AvdGhlLXJldGlub2JsYXN0b21hLXByb3RlaW4tMzQ5NDUzNzA3LmpwZw==!aHR0cHM6Ly9pLndlbHRiaWxkLmRlL3AvdGhlLXJldGlub2JsYXN0b21hLXByb3RlaW4tMzQ5NDUzNzA3LmpwZ3x+fGh0dHBzOi8vb3MxLm1laW5lY2xvdWQuaW8vYjEwMTU4L21lZGlhL2ltYWdlLzJmL2I1L2U0LzY2NDY5NDEwMDAwMDFBXzYwMHg2MDAuanBn","post_title":"The Retinoblastoma Protein","deeplink":"https:\/\/track.adtraction.com\/t\/t?a=1632201226&as=1592767275&t=2&tk=1&url=https:\/\/www.weltbild.ch\/artikel\/x\/_23641054-1","labels":[],"brand_id":440615,"post_content":"1.Characterization of RB1 Deletions in Interphase and Metaphase by Molecular Cytogenetics Exemplified in Chronic Lymphatic Leukemia Thomas Liehr 2.Detection of RB1 Gene Copy Number Variations using a Multiplex Ligation-Dependent Probe Amplification Method Nejat Dalay 3.A Fluorescent Quantitative Multiplex PCR Method to Detect Copy Number Changes in the RB1 Gene Chitra Kannabiran 4. Using\u00a0Methylation-specific PCR to study RB1 Promoter Hypermethylation Tha\u00eds M. McCormick and Maria da Gl\u00f3ria da C. Carvalho 5. Detection of Aberrant DNA Methylation Patterns in the RB1 Gene Sumadi Lukman Anwar and Ulrich Lehmann 6. Detection of Retinoblastoma Protein Phosphorylation by Immunoblot Analysis Pedro G. Santiago-Cardona, Jaileene P\u00e9rez-Morales, and Jonathan Gonz\u00e1lez-Flores 7. Immunohistochemical Detection of the Retinoblastoma Protein Charles A. Ishak, Matthew J. Cecchini, Christopher J. Howlett, and Frederick A. Dick 8. Immunohistochemical Detection of Retinoblastoma Protein Phosphorylation in Human Tumor Samples Jaileene P\u00e9rez-Morales, Angel N\u00fa\u00f1ez-Marrero, and Pedro G. Santiago-Cardona 9. Detection of CCND1 Locus Amplification by Fluorescence in situ Hybridization Margit Bal\u00e1zs, Vikt\u00f3ria Koroknai, Istv\u00e1n Sz\u00e1sz, and Szilvia Ecsedi 10. Detection of CCND1 Gene Copy Number Variations using Multiplex Ligation-dependent Probe Amplification and Fluorescence in situ Hybridization Methods Akishi Ooi and Takeru Oyama 11. Detection of p16 Promoter Hypermethylation by Methylation-specific PCR Javed Hussain Choudhury, Raima Das, Shaheen Laskar, Sharbadeb Kundu, Manish Kumar, Partha Pratim Das, Yashmin Choudhury, Rosy Mondal, and Sankar Kumar Ghosh 12. Immunohistochemical Detection of p16 in Clinical Samples Georgia Karpathiou and Michel Peoc'h\u00a0 13. Detection of E2F-DNA Complexes Using Chromatin Immunoprecipitation Assays Miyoung Lee, Lorraine J. Gudas, and Harold I. Saavedra 14. Detection of E2F-induced Transcriptional Activity Using a Dual Luciferase Reporter Assay Ainhoa Iglesias-Ara, Nerea Osinalde, and Ana M. Zubiaga 15. Detection of HPV E6\/E7 mRNA in Clinical Samples using RNA in situ Hybridization Manishkumar Pandey, Priyanka G. Bhosale, and Manoj B. Mahimkar 16. CRISPR\/Cas9 Mediated Knockout of Rb1 in Xenopus tropicalis Thomas Naert and Kris Vleminckx","merchants_number":2,"ean":9781493975648,"category_id":1,"size":null,"min_price":118,"low_price_merchant_id":27291482,"ID":19693616,"merchants":["weltbild","euniverse"],"brand":"Springer Berlin,Springer New York,Humana Press,Humana","slug":"the-retinoblastoma-protein-1","url":"\/produkt\/the-retinoblastoma-protein-1\/","low_price_merchant_name":"Weltbild"}

CHF 178.00

Protein Misfolding Diseases

Part I: Protein Biophysics Assays 1. Biophysical and Spectroscopic Methods for Monitoring Protein Misfolding and Amyloid Aggregation Joana S. Cristóvão, Bárbara J. Henriques, and Cláudio M. Gomes 2. Ultrasensitive RT-QuIC Seed Amplification Assays for Disease-Associated Tau, -Synuclein, and Prion Aggregates Eri Saijo, Bradley R. Groveman, Allison Kraus, Michael ...

11492198 {"price-changing":0,"image":"https:\/\/image.vergleiche.ch\/small\/aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvYjMvZTEvMzgvODAzOTYyODYwMDAwMUFfNjAweDYwMC5qcGc=!aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvYjMvZTEvMzgvODAzOTYyODYwMDAwMUFfNjAweDYwMC5qcGd8fnxodHRwczovL2kud2VsdGJpbGQuZGUvcC9wcm90ZWluLW1pc2ZvbGRpbmctZGlzZWFzZXMtMzEwODQ3MTcxLmpwZw==","post_title":"Protein Misfolding Diseases","deeplink":"https:\/\/cct.connects.ch\/tc.php?t=116298C1969900829T&subid=9781493993963&deepurl=https%3A%2F%2Feuniverse.ch%2Fbuecher%2Fmathematik-naturwissenschaft-technik%2Fbiologie%2F379026%2Fprotein-misfolding-diseases-methods-and-protocols%3FsPartner%3Dtoppreise","labels":[],"brand_id":1,"post_content":"Part I: Protein Biophysics Assays\u00a01. Biophysical and Spectroscopic Methods for Monitoring Protein Misfolding and Amyloid Aggregation\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Joana S. Crist\u00f3v\u00e3o, B\u00e1rbara J. Henriques, and Cl\u00e1udio M. Gomes\u00a02. Ultrasensitive RT-QuIC Seed Amplification Assays for Disease-Associated Tau, -Synuclein, and Prion Aggregates\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Eri Saijo, Bradley R. Groveman, Allison Kraus, Michael Metrick, Christina D. Orr\u00f9, Andrew G. Hughson, and Byron Caughey\u00a03. Vesicle-Based Assays to Study Membrane Interactions of Amyloid Peptides\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Ravit Malishev, Sofiya Kolusheva, and Raz Jelinek\u00a04. Differential Scanning Fluorimetry and Hydrogen Deuterium Exchange Mass Spectrometry to Monitor the Conformational Dynamics of NBD1 in Cystic Fibrosis\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Naoto Soya, Ariel Roldan, and Gergely L. Lukacs\u00a05. A Multipronged Method for Unveiling Subtle Structural-Functional Defects of Mutant Chaperone Molecules Causing Human Chaperonopathies\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Donatella Bulone, Pier Luigi San Biagio, Tatiana Qui\u00f1ones-Ruiz, Manuel Rosario-Alomar, Igor K. Lednev, Frank T. Robb,Everly Conway de Macario, and Alberto J.L. Macario\u00a06. High-Throughput Microplate-Based Fluorescence Assays for Studying Stochastic Aggregation of Superoxide Dismutase-1\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Alireza Abdolvahabi, Sanaz Rasouli, Corbin M. Croom, and Devon L. Plewman\u00a07. Methods for Structural Analysis of Amyloid Fibrils in Misfolding Diseases\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Devkee M. Vadukul, Youssra K. Al-Hilaly, and Louise C. Serpell\u00a08. Assays for Light Chain Amyloidosis Formation and Cytotoxicity\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Luis M. Blancas-Mejia, Pinaki Misra, Christopher J. Dick, Marta Marin Argany, Keely R. Redhage, Shawna A. Cooper, and Marina Ramirez-Alvarado\u00a0Part II: Cellular And Proteostasis Assays\u00a09. Monitoring Aggregate Clearance and Formation in Cell-Based Assays\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Evelien Eenjes, Young Joo Yang-Klingler, and Ai Yamamoto\u00a010. Monitoring Proteome Stress in Live Cells Using HaloTag-Based Fluorogenic Sensor\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Yu Liu, Matthew Fares, and Xin Zhang\u00a011. Quantification of Protein Aggregates Using Bimolecular Fluorescence Complementation\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Vibha Prasad and Aaron Voigt\u00a012. Screening Protein Aggregation in Cells Using Fluorescent Labels Coupled to Flow Cytometry\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Salvador Ventura and Susanna Navarro\u00a013. Induction of Cu\/Zn Superoxide Dismutase (SOD1) Aggregation in Living Cells\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Edward Pokrishevsky, Jeremy Nan, and Neil R. Cashman\u00a014. A Cell Model for HSP60 Deficiencies: Modeling Different Levels of Chaperonopathies Leading to Oxidative Stress and Mitochondrial Dysfunction\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Cagla C\u00f6mert, Paula Fernandez Guerra, and Peter Bross\u00a015. Super-Resolution Fluorescence Imaging of Mutant Huntingtin Aggregation in Cells\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Steffen J. Sahl and Willianne I.M. Vonk\u00a0Part III: Protein Folding Recovery and Correction Assays\u00a016. Thermal Shift and Stability Assays of Disease-Related Misfolded Proteins Using Differential Scanning Fluorimetry\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 T\u00e2nia G. Lucas, Cl\u00e1udio M. Gomes, and B\u00e1rbara J. Henriques\u00a017. Methods to Screen Compounds against Mutant p53 Misfolding and Aggregation for Cancer Therapeutics\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Giulia Diniz da Silva Ferretti, Danielly Ferraz da Costa, Jerson Lima da Silva, and Luciana Pereira Rangel\u00a018. Early Stage Discovery and Validation of Pharmacological Chaperones for the Correction of Protein Misfolding Diseases\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Oscar Aubi, Per M. Knappskog, and Aurora Martinez\u00a019. Constructing Kinetically Controlled Denaturation Isotherms of Folded Proteins Using Denaturant-Pulse Chaperonin Binding\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Pierce T. O'Neil, Alexandra J. Machen, Jackie A. Thompson, Wei Wang, Quyen Q. Hoang, Michael R. Baldwin, Karen R. Khar, John Karanicolas, and Mark T. Fisher\u00a020. In Vitro Prion Amplification Methodology for Inhibitor Screening\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Tuane Cristine R.G. Vieira and Jerson L. Silva\u00a021. SolubiS: Optimizing Protein Solubility by Minimal Point Mutations\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Rob van der Kant, Joost van Durme, Frederic Rousseau, and Joost Schymkowitz","merchants_number":2,"ean":9781493993963,"category_id":1,"size":null,"min_price":178,"low_price_merchant_id":70255345,"ID":11492198,"merchants":["euniverse","weltbild"],"brand":"undefined","slug":"protein-misfolding-diseases-3","url":"\/produkt\/protein-misfolding-diseases-3\/","low_price_merchant_name":"eUniverse"}

CHF 12.00

Protein-Power-Smoothies

CHF 177.00

Protein Targeting Protocols

CHF 27.25

Protein Muskel Fit

Nahrungsergänzungsmittel sind kein Ersatz für eine ausgewogene und abwechslungsreiche Ernährung und eine gesunde Lebensweise. Protein Muskel Fit Kapseln tragen bei mit Magensium zur Erhaltung einer normalen Muskelmasse und Muskelfunktion. Zutaten: pro Kapsel: Erbsenprotein Pulver, Magnesiumcitrat Kapselhülle: Hydroxypropylmethylcellulose pflanzlich Nährwerte: Tagesdosis: 100 % veganes...