Clinical Proteomics: From Diagnosis to Therapy

Unprecedented in its scope and intensity, this booklet brings jointly proteomic ways in prognosis and therapy from all medical fields, together with medical toxicology. the result's a brand new self-discipline in molecular drugs that might revolutionize the remedy and prevention of melanoma, stroke and different serious diseases.
Following an summary of scientific proteomics, the authors examine the applied sciences on hand, prior to relocating directly to melanoma, cardiopulmonary affliction, diabetes and stroke. an entire part is dedicated to toxicity and the paintings is rounded off with a dialogue of the way forward for scientific proteomics.Content:
Chapter 1 Preanalytical matters in medical Proteomic reports (pages 1–12): Roisean E. Ferguson and Rosamonde E. Banks
Chapter 2 Protein Separation via Two?Dimensional Electrophoresis (pages 13–29): Pamela M. Donoghue, Miroslava Stastna and Prof. Dr. Michael J. Dunn
Chapter three Protein Separation: Liquid Chromatography (pages 31–51): Miroslava Stastna and Dr. Jennifer Van Eyk
Chapter four HPLC in Protein Discovery (pages 53–60): Timothy J. Barder
Chapter five IEF research of Peptides for Biomarkers Discovery (pages 61–71): Ali R. Vaezzadeh, Catherine G. Zimmermann?Ivol, Jacques Deshusses, Alexander Scherl and Denis F. Hochstrasser
Chapter 6 Capillary Electrophoretic Separations for medical Proteomics (pages 73–88): Brian M. Balgley, Weijie Wang, Xueping Fang, Don L. DeVoe and Cheng S. Lee
Chapter 7 Quantitative Proteomics utilizing Nano?LC with excessive Accuracy Mass Spectrometry (pages 89–100): Ljiljana Pasa?Tolic, Jon M. Jacobs, Wei?Jun Qian and Richard D. Smith
Chapter eight Antibody Microarrays for Protein and Glycan Detection (pages 101–111): Songming Chen and Brian B. Haab
Chapter nine Biomarker identity: The function of Experimental layout, information, and knowledge Sharing (pages 113–120): Marc R. Wilkins
Chapter 10 purposes of solid Isotope Tagging dependent Quantitative Proteomics in melanoma learn (pages 121–143): Ru Chen, Teresa A. Brentnall and Ruedi Aebersold
Chapter eleven Two?Dimensional Liquid Separations, Protein Microarrays, and Mass Spectrometry in accomplished research of Posttranslational variations and Biomarker Discovery in Cancers (pages 145–164): Tasneem H. Patwa, Jia Zhao, David E. Misek and David M. Lubman
Chapter 12 improvement and Use of Reversed?Phase Protein Microarrays for scientific functions (pages 165–175): Virginia Espina, Julia Wulfkuhle, Valerie S. Calvert, Kirsten H. Edmiston, Lance A. Liotta and Emanuel F. Petricoin
Chapter thirteen Cyclin?Dependent Kinase Inhibitors and melanoma: Usefulness of Proteomic ways in review of the Molecular Mechanisms and Efficacy of Novel Therapeutics (pages 177–202): Marian Hajduch, Helena Skalnikova, Petr Halada, David Vydra, Petr Dzubak, Marta Dziechciarkova, Miroslav Strnad, Danuta Radioch, Suresh Jivan Gadher and Hana Kovarova
Chapter 14 Diagnostic Markers for tracking middle Transplant Rejection (pages 203–215): Dr. Ciara A. McManus, Professor Marlene L. Rose and Prof. Dr. Michael J. Dunn
Chapter 15 The examine of Microheterogeneity in Human Plasma Proteins: software to Acute Myocardial Infarction (pages 217–229): Randall W. Nelson, city A. Kiernan, Dobrin Nedelkov, Kemmons A. Tubbs and Eric E. Niederkofler
Chapter sixteen Discovery of Biomarkers for Cardiovascular illnesses (pages 231–240): Anthony O. Gramolini and Andrew Emili
Chapter 17 improvement of Biomarker improvement Pipeline: look for Myocardial Ischemia Biomarkers (pages 241–261): Qin Fu, Shijun Sheng and Dr. Jennifer E. Van Eyk
Chapter 18 The Albuminome as a device for Biomarker Discovery (pages 263–278): Rebekah L. Gundry and Robert J. Cotter
Chapter 19 software of Metabolomics to Cardiovascular Biomarker and Pathway Discovery (pages 279–293): Gregory D. Lewis and Robert E. Gerszten
Chapter 20 Urinary Biomarkers in Diabetic Nephropathy and different Glomerular illnesses (pages 295–322): John M. Arthur and T. Brian Powell
Chapter 21 Pulmonary Proteomics (pages 323–347): Jan Hirsch, Lorraine B. Ware and Michael A. Matthay
Chapter 22 Proteomics supplying Insights into significant Psychiatric problems (pages 349–377): Melanie Focking, Kyla Pennington, Jane English, Prof. Dr. Michael Dunn and David Cotter
Chapter 23 Redox Proteomics research of Oxidative changed mind Proteins in Alzheimer's ailment and gentle Cognitive Impairment: Insights into the development of This Dementing ailment (pages 379–401): Rukhsana Sultana and D. Allan Butterfield
Chapter 24 Toxicoproteomics: Correlating Tissue and Serum Proteomics in Liver damage (pages 403–433): B. Alex Merrick
Chapter 25 Biomarkers for Renal illness and Uremic pollutants (pages 435–452): Eric Schiffer, Harald Mischak and Raymond C. Vanholder
Chapter 26 HIV and different Viral monitors (pages 453–480): David R. Graham
Chapter 27 software of Fungal Cyclic Peptides and Metabolites (pages 481–509): Jan Nedved, Miroslav Sulc, Alexandr Jegorov, Anastassios Giannakopulos and Vladimir Havlicek
Chapter 28 Microarray ways to Autoantibody Profiling (pages 511–532): John M. Astle and Thomas Kodadek
Chapter 29 id of Tumor Antigen Directed Autoantibodies (pages 533–547): Sandra Faca and Sam Hanash
Chapter 30 Antibody and opposite catch Protein Microarrays for medical Proteomics (pages 549–569): Harvey B. Pollard, Ofer Eidelman, Meera Srivastava, Catherine Joswik, Stephen Rothwell, Gregory P. Mueller, David M. Jacobowitz, William B. Guggino, Jerry Wright, Pamela L. Zeitlin and Cloud P. Paweletz
Chapter 31 Use of Antibody Microarrays within the research of irritation, Autoimmunity, Viral an infection, and melanoma Metastases (pages 571–592): Rodney Lui, Angus Brown, Bosco Wu, Ming?Wei Lin, John Thompson, Filip Braet, Wayne Dyer, JoDee Lattimore, Peter Macdonald, Stephen Adelstein and Cristobal G. dos Remedios
Chapter 32 the longer term: Translation from Discovery to the health facility – Roles of HUPO and in Biomarker Discovery (pages 593–613): Gilbert S. Omenn and Peipei Ping
Chapter 33 requisites of an excellent Biomarker: Translation into the medical Laboratory (pages 615–631): Mario Plebani, Martina Zaninotto and Monica Maria Mion
Chapter 34 Translation of Protein Biomarkers for medical improvement (pages 633–651): Ian McCaffery, V. Dan Fitzpatrick, Shen Wu Wang, John M. Rossi, Haifeng Bao, Sid V. Suggs, John Ferbas and Scott D. Patterson

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Gafken, P. R. and Lampe, P. D. (2005) Evaluation of matrix-assisted laser desorption/ionization-time of flight mass spectrometry proteomic profiling: identification of a2-HS glycoprotein B-chain as a biomarker of diet. Proteomics, 5, 2238–2246. , Mohring, T. and Schulz-Knapp, P. (2005) Peptidomic analysis of human blood specimens: comparison between plasma specimens and serum by differential peptide display. Proteomics, 5, 3414–3422. Hseih, S. , Chen, R. , Pan, Y. H. and Lee, H. L. (2006) Systematical evaluation of the effects of sample procedures on low-molecular-weight serum/plasma proteome profiling.

Kristoffersen, D. , Lund, K. , Nossen, J. O. and Stenstrom, J. (1998) Reference range of some enzymes and proteins in untimed overnight urine and their stability after freezing. Clinica Chimica Acta, 272, 225–230. Schultz, C. , Dalton, R. , Neil, H. A. W. and Dunger, D. B. (2000) Freezing method affects the concentration and variability of urine proteins and the interpretation of data on microalbuminuria. Diabetic Medicine, 17, 7–14. Townsend, J. , Sadler, W. A. and Shanks, G. M. (1987) The effect of storage pH on the precipitation of proteins in deep frozen urine specimens.

7) [40]. Numerous subcellular fractionation kits are commercially available, and all are quite similar in their approach. A series of buffers used in conjunction with several centrifugation steps at different speeds results in a number of fractions each containing a different subset of the proteome under investigation. It is important to note that the total fractionation of any proteome is impossible as contamination Fig. 7 Serum depletion using the Agilent Multiple Affinity Removal System (MARS), a polyclonal antibody-based depletion system that removes the six most highly abundant proteins, circled in red (a).

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