02352nas a2200205   4500008004100000022001400041245015300055210006900208260008800277300001000365490000700375520148400382100002301866700002501889700002201914700002201936700003301958700002501991856013002016       2013                        eng d  a1536-231000aProteomic profiling and interactome analysis of ER-positive/HER2/neu negative invasive ductal carcinoma of the breast: towards proteomics biomarkers0 aProteomic profiling and interactome analysis of ERpositiveHER2ne  a140 HUGUENOT STREET, 3RD FL, NEW ROCHELLE, NY 10801 USAbMARY ANN LIEBERT, INCcJAN  a27-400 v173 a<p>Breast cancer, especially ER positive/HER2/neu negative IDC, is the predominant subtype of invasive ductal carcinoma. Although proteomic approaches have been used towards biomarker discovery in clinical breast cancer, ER positive/HER2/neu negative IDC is the least studied subtype. To discover biomarkers, as well as to understand the molecular events associated with disease progression of estrogen receptor positive/HER2/neu negative subtype of invasive ductal carcinoma, differential protein expression profiling was performed by using LC-MSE (MS at elevated energy). A total of 118 proteins were identified, of which 26 were differentially expressed. These identified proteins were functionally classified and their interactions and coexpression were analyzed by using bioinformatic tools PANTHER (Protein Analysis THrough Evolutionary Relationships) and STRING (Search Tool for the Retrieval of Interacting Genes). These proteins were found to be upregulated and were involved in cytoskeletal organization, calcium binding, and stress response. Interactions of annexin A5, actin, S100 A10, glyceraldehyde 3 phosphate dehydrogenase, superoxide dismutase 1, apolipoprotein, fibrinogen, and heat shock proteins were prominent. Differential expression of these proteins was validated by two-dimensional gel electrophoresis and Western blot analysis. The cluster of these proteins may serve as a signature profile for estrogen receptor positive/ HER2/neu negative subtype.</p>1 aKorwar, Arvind, M.1 aBhonsle, Hemangi, S.1 aGhole, Vikram, S.1 aGawai, Kachru, R.1 aKoppikar, Chaitanyananda, B.1 aKulkarni, Mahesh, J.  uhttps://library.ncl.res.in/content/proteomic-profiling-and-interactome-analysis-er-positiveher2neu-negative-invasive-ductal-001879nas a2200253   4500008004100000022001400041245011900055210006900174260006300243300001200306490000600318520096300324653001401287653001001301653001501311100002501326700002301351700002401374700002101398700002201419700002701441700002501468856013201493       2013                        eng d  a1791-299700aProteomic study reveals downregulation of apolipoprotein A1 in plasma of poorly controlled diabetes: a pilot study0 aProteomic study reveals downregulation of apolipoprotein A1 in p  aPOB 18179, ATHENS, 116 10, GREECEbSPANDIDOS PUBL LTDcFEB  a495-4980 v73 a<p>Proteomic approaches aid in gaining a better understanding of the pathophysiology of diabetic complications. In view of this, differential protein expression in diabetic plasma samples was studied by a combination of proteomic and western blot analyses. Diabetic plasma samples were categorized based on glycated haemoglobin levels as controlled diabetes (CD; 7-8%), poorly controlled diabetes (PCD; &gt;8%) and non-diabetic control (ND;&lt;6.4%). Two-dimensional electrophoresis and liquid chromatography-mass spectrometry revealed differential expression of proteins including upregulation of fibrinogen and haptoglobin and downregulation of vitamin D binding protein, alpha-1-antitrypsin, transthyretin and apolipoprotein A1 (Apo A1) in diabetic compared with non-diabetic plasma samples. Amongst these proteins, Apo A1 downregulation was prominent in PCD. Downregulation of Apo A1 may serve as an early predictive marker of diabetic complications.</p>10abiomarker10aHbA1c10aproteomics1 aBhonsle, Hemangi, S.1 aKorwar, Arvind, M.1 aChougale, Ashok, D.1 aKote, Sachin, S.1 aDhande, Nitin, L.1 aShelgikar, Kishore, M.1 aKulkarni, Mahesh, J.  uhttps://library.ncl.res.in/content/proteomic-study-reveals-downregulation-apolipoprotein-a1-plasma-poorly-controlled-diabetes-002477nas a2200325   4500008004100000022001400041245009500055210006900150260005700219300001400276490000700290520142400297653001201721653002001733653001501753653001101768653002001779100002001799700002001819700001701839700002501856700002101881700002001902700002201922700001901944700002501963700002101988700002202009856012002031       2014                        eng d  a0175-759800aProteomics of arsenic stress in the gram-positive organism Exiguobacterium sp PS NCIM 54630 aProteomics of arsenic stress in the grampositive organism Exiguo  a233 SPRING ST, NEW YORK, NY 10013 USAbSPRINGERcAUG  a6761-67730 v983 a<p>The general responses of microorganisms to environmental onslaughts are modulated by altering the gene expression pattern to reduce damage in the cell and produce compensating stress responses. The present study attempts to unravel the response of the Gram-positive Exiguobacterium sp. PS NCIM 5463 in the presence of [As(III)] and arsenate [As(V)] using comparative proteomics via two-dimension gel electrophoresis (2-DE) coupled with identification of proteins using matrix-assisted laser desorption/ionisation (MALDI-TOF/MALDI-TOF/TOF). Out of 926 Coomassie-stained proteins, 45 were differentially expressed (p &lt; 0.05). Considering the resolution and abundance level, 24 spots (peptides) were subjected to MALDI analysis, identified and categorised into several functional categories, viz., nitrogen metabolism, energy and stress regulators, carbohydrate metabolism, protein synthesis components and others. A functional role of each protein is discussed in Exiguobacterium sp. PS 5463 under arsenic stress and validated at their transcript level using a quantitative real-time polymerase chain reaction. Unlike previous reports that unravel the responses toward arsenic stress in Gram-negative organisms, the present study identified new proteins under arsenic stress in a Gram-positive organism, Exiguobacterium sp. PS NCIM 5463, which could elucidate the physiology of organisms under arsenic stress.</p>
10aArsenic10aExiguobacterium10aproteomics10aStress10aTranscriptomics1 aSacheti, Poonam1 aPatil, Rajendra1 aDube, Ankita1 aBhonsle, Hemangi, S.1 aThombre, Dipalee1 aMarathe, Sayali1 aVidhate, Ravindra1 aWagh, Priyanka1 aKulkarni, Mahesh, J.1 aRapole, Srikanth1 aGade, Wasudeo, N.  uhttps://library.ncl.res.in/content/proteomics-arsenic-stress-gram-positive-organism-exiguobacterium-sp-ps-ncim-5463