14 results match your criteria Current Proteomics[Journal]

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Proteomic Changes Between Allotriploids and Diploids Revealed Using an iTRAQ-based Quantitative Approach.

Curr Proteomics 2017 Sep;14(3):166-174

National Engineering Laboratory for Tree Breeding, Key Laboratory of Genetics and Breeding in Forest Trees and Ornamental Plants, Ministry of Education, College of Biological Sciences and Technology, Beijing Forestry University, No. 35, Qinghua East Road, Beijing100083, China.

Background: Polyploid breeding is a powerful approach for Populus genetic improve-ment because polyploid trees have valuable characteristics, including better timber quality and a higher degree of stress resistance compared with their full-sib diploids. However, the genetic mech-anism underlying this phenomenon remains unknown.

Objective: To better understand the proteomic changes between Populus allotriploids and diploids, we examined the proteomic profiles of allotriploid and diploid Populus by iTRAQ labeling coupled with two-dimensional liquid chromatography and MALDI-TOF/TOF mass spectrometry (MS). Read More

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http://dx.doi.org/10.2174/1570164614666170310142405DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5676023PMC
September 2017
13 Reads

Identification of Osteoporosis-Associated Protein Biomarkers from Ovariectomized Rat Urine.

Curr Proteomics 2017 Jun;14(2):130-137

Carolina Healthcare, Charlotte, NC, USA.

Objective: Osteoporotic fracture is one of the most common health risks and aggravates the quality of life among postmenopausal women worldwide. In this study, osteoporosis-associated protein biomarkers were identified from urine of osteoporotic female Sprague-Dawley rats developed by ovariectomy.

Method: Four months after the operation, the bone mineral density of the femur of ovariectomized rats was significantly lowered in comparison with that of the sham operated rats. Read More

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http://dx.doi.org/10.2174/1570164614666161228124801DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5427775PMC
June 2017
18 Reads

B-factor Analysis and Conformational Rearrangement of Aldose Reductase.

Curr Proteomics 2014 ;11(3):151-160

UCLA-DOE, 611 Charles E. Young Drive East, 220 Boyer Hall, Los Angeles, CA 90095, USA.

The NADPH-dependent reduction of glucose reaction that is catalyzed by Aldose Reductase (AR) follows a sequential ordered kinetic mechanism in which the co-factor NADPH binds to the enzyme prior to the aldehyde substrate. The kinetic/structural experiments have found a conformational change involving a hinge-like movement of a surface loop (residues 213-224) which is anticipated to take place upon the binding of the diphosphate moiety of NADPH. The reorientation of this loop, expected to permit the release of NADP, represents the rate-limiting step of the catalytic mechanism. Read More

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http://dx.doi.org/10.2174/157016461103140922163444DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4212266PMC
January 2014
12 Reads
2 Citations
0.440 Impact Factor

Anti-cancer Therapies in High Grade Gliomas.

Curr Proteomics 2013 Sep;10(3):246-260

Victor Babes National Institute of Pathology, Department of Biochemistry-Proteomics, no 99-101 Splaiul Inde-pendentei, 050096 sect 5 Bucharest, Romania;

High grade gliomas represent one of the most aggressive and treatment-resistant types of human cancer, with only 1-2 years median survival rate for patients with grade IV glioma. The treatment of glioblastoma is a considerable therapeutic challenge; combination therapy targeting multiple pathways is becoming a fast growing area of research. This review offers an up-to-date perspective of the literature about current molecular therapy targets in high grade glioma, that include angiogenic signals, tyrosine kinase receptors, nodal signaling proteins and cancer stem cells related approaches. Read More

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http://dx.doi.org/10.2174/1570164611310030007DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3821381PMC
September 2013
14 Reads

Immunomics in Skin Cancer - Improvement in Diagnosis, Prognosis and Therapy Monitoring.

Curr Proteomics 2013 Sep;10(3):202-217

Bruker Daltonics, Billerica, MA, USA;

This review will focus on the elements of the skin's immune system, immune cells and/or non-immune cells that support immune mechanisms, molecules with immune origin and/or immune functions that are involved in skin carcinogenesis. All these immune elements are compulsory in the development of skin tumors and/or sustainability of the neoplastic process. In this light, recent data gathered in this review will acknowledge all immune elements that contribute to skin tumorigenesis; moreover, they can serve as immune biomarkers. Read More

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http://www.eurekaselect.com/openurl/content.php?genre=articl
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http://dx.doi.org/10.2174/1570164611310030003DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3821382PMC
September 2013
9 Reads

Structural Characterization of Carbohydrates by Fourier Transform Tandem Mass Spectrometry.

Curr Proteomics 2011 Dec;8(4):297-308

Department of Chemistry, University of Michigan, Ann Arbor, Michigan, USA.

Fourier transform tandem mass spectrometry (MS/MS) provides high mass accuracy, high sensitivity, and analytical versatility and has therefore emerged as an indispensable tool for structural elucidation of biomolecules. Glycosylation is one of the most common posttranslational modifications, occurring in ~50% of proteins. However, due to the structural diversity of carbohydrates, arising from non-template driven biosynthesis, achievement of detailed structural insight is highly challenging. Read More

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http://www.eurekaselect.com/openurl/content.php?genre=articl
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http://dx.doi.org/10.2174/157016411798220826DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3289259PMC
December 2011
6 Reads

Abundance- and Activity-Based Proteomics in Platelet Biology.

Curr Proteomics 2011 Oct;8(3):216-228

Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599.

Human platelets are thought to express approximately 2000-3000 proteins, but post-translational modifications, alternatively spliced variants and a rich diversity of vertebrate domain architectures likely make this a conservative estimate. Even though rapidly advancing proteomic techniques have facilitated the identification of roughly one third of the platelet proteome, a combination of abundance-based and activity-based proteomics methodologies is needed for elucidation of platelet functional characteristics including the definition of a "core proteome" and recognition of diverse enzyme activity profiles associated with various physiological states. In this review, we describe the latest mass spectrometry-based techniques capable of providing some of these physiological details required for more comprehensive evaluation of the human platelet repertoire. Read More

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http://www.eurekaselect.com/openurl/content.php?genre=articl
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http://dx.doi.org/10.2174/157016411797247512DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3270490PMC
October 2011
9 Reads

Novel Sample Preparation for Mass Spectral Analysis of Complex Biological Samples.

Curr Proteomics 2010 Jul;7(2):90-101

Department of Molecular Genetics and Microbiology, Duke University Medical Center, Durham, NC 27707.

The ability to combine a selective capture strategy with on chip MALDI-TOF analysis allows for rapid, sensitive analysis of a variety of different analytes. In this overview a series of applications of capture enhanced laser desorption ionization time of flight (CELDI-TOF) mass spectrometry are described. The key feature of the assay is an off-chip capture step that utilizes high affinity bacterial binding proteins to capture a selected ligand. Read More

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3128501PMC
July 2010
11 Reads

Bioinformatics Tools for Mass Spectrometry-Based High-Throughput Quantitative Proteomics Platforms.

Curr Proteomics 2011 Jul;8(2):125-137

Department of Biochemistry and Molecular Biology, The University of Texas Medical Branch, 301 University Blvd., Galveston, TX, 77555.

Determining global proteome changes is important for advancing a systems biology view of cellular processes and for discovering biomarkers. Liquid chromatography, coupled to mass spectrometry, has been widely used as a proteomics technique for discovering differentially expressed proteins in biological samples. However, although a large number of high-throughput studies have identified differentially regulated proteins, only a small fraction of these results have been reproduced and independently verified. Read More

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3448448PMC
July 2011
12 Reads

Analysis of Glycosaminoglycans Using Mass Spectrometry.

Curr Proteomics 2011;8(4):325-336

Center for Biomedical Mass Spectrometry, Dept. of Biochemistry, Boston University School of Medicine.

The glycosaminoglycans (GAGs) are linear polysaccharides expressed on animal cell surfaces and in extracellular matrices. Their biosynthesis is under complex control and confers a domain structure that is essential to their ability to bind to protein partners. Key to understanding the functions of GAGs are methods to determine accurately and rapidly patterns of sulfation, acetylation and uronic acid epimerization that correlate with protein binding or other biological activities. Read More

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http://www.eurekaselect.com/openurl/content.php?genre=articl
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http://dx.doi.org/10.2174/157016411798220871DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4334465PMC
January 2011
12 Reads

Dissecting virus-plant interactions through proteomics approaches.

Authors:
Kai Xu Peter D Nagy

Curr Proteomics 2010 Dec;7(4):316-327

Department of Plant Pathology, University of Kentucky, Lexington, KY.

Plant viruses exploit cellular factors, including host proteins, membranes and metabolites, for their replication in infected cells and to establish systemic infections. Besides traditional genetic, molecular, cellular and biochemical methods studying plant-virus interactions, both global and specialized proteomics methods are emerging as useful approaches for the identification of all the host proteins that play roles in virus infections. The various proteomics approaches include measuring differential protein expression in virus infected versus noninfected cells, analysis of viral and host protein components in the viral replicase or other virus-induced complexes, as well as proteome-wide screens to identify host protein - viral protein interactions using protein arrays or yeast two-hybrid assays. Read More

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http://www.eurekaselect.com/openurl/content.php?genre=articl
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http://dx.doi.org/10.2174/157016410793611792DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3769790PMC
December 2010
6 Reads

DIFFERENTIAL SERUM LEVEL OF SPECIFIC HAPTOGLOBIN ISOFORMS IN SMALL CELL LUNG CANCER.

Curr Proteomics 2010 Apr;7(1):49-65

Department of Medicine, Section of Molecular Medicine, Boston University School of Medicine, 88 East Newton Street, Boston, MA 02118.

Lung cancer is the leading cause of cancer death for both men and women in the United States, and similar trends are seen world wide. The lack of early diagnosis is one of the primary reasons for the high mortality rate. A number of biomarkers have been evaluated in lung cancer patients, however, their specificity and early stage diagnostic values are limited. Read More

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2880513PMC
April 2010
13 Reads

Proteomics on Fixed Tissue Specimens - A Review.

Curr Proteomics 2009 Apr;6(1):63-69

Departments of Gastroenterology and Surgery, University of Washington, Seattle, Washington 98195.

The vast majority of clinical tissue samples are formalin-fixed and paraffin-preserved. This type of preservation has been considered an obstacle to protein extraction from these tissues. However, these are the very tissue samples that have associated patient histories, diagnoses and outcomes - ideal samples in the quest to translate bench research into clinical applications. Read More

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http://dx.doi.org/10.2174/157016409787847420DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2760948PMC
April 2009
12 Reads

Insight into the Protein Components of the Box H/ACA RNP.

Curr Proteomics 2008 Jul;5(2):129-137

Department of Biochemistry and Biophysics, University of Rochester Medical Center, Rochester, New York 14642.

Among eukaryotic organisms a vast majority of Box H/ACA ribonucleoproteins (RNPs) are responsible for the post-transcriptional introduction of pseudouridine (Psi) into ribosomal RNAs (rRNA) and spliceosomal small nuclear RNAs (snRNA), thus influencing protein translation and pre-mRNA splicing, respectively. Additionally, a few distinct Box H/ACA RNPs are involved in the processing of rRNA, and the stabilization of vertebrate telomerase RNA. Thus, whether directly or indirectly, Box H/ACA RNPs impact major steps of gene expression, as well as play a role in maintaining genome integrity. Read More

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http://dx.doi.org/10.2174/157016408784911936DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2760984PMC
July 2008
5 Reads
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