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Journal articles on the topic 'Proteins Analysis'

To see the other types of publications on this topic, follow the link: Proteins Analysis.

Author: Grafiati

Published: 4 June 2021

Last updated: 31 July 2024

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1

Meraj, Syeda Shaizadi, and Tanusree Chaudhuri. "Structurally Significant Analysis of Tuberculosis Proteins." International Journal of Scientific Research 3, no. 6 (June 1, 2012): 39–41. http://dx.doi.org/10.15373/22778179/june2014/16.

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2

Scopes, R. K., and John A. Smith. "Analysis of Proteins." Current Protocols in Molecular Biology 76, no. 1 (October 2006): 10.0.1–10.0.22. http://dx.doi.org/10.1002/0471142727.mb1000s76.

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3

Gupal, Anatoliy M., Ivan I. Andreychuk, Alexandra A. Vagis, and Ludmila A. Zakrevskaya. "Statistical Analysis of Proteins." Journal of Automation and Information Sciences 36, no. 12 (2004): 25–29. http://dx.doi.org/10.1615/jautomatinfscien.v36.i12.20.

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4

Trimpin, Sarah, and Bill Brizzard. "Analysis of insoluble proteins." BioTechniques 46, no. 5 (April 2009): 321–26. http://dx.doi.org/10.2144/000113135.

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5

Trimpin, Sarah, and Bill Brizzard. "Analysis of insoluble proteins." BioTechniques 46, no. 6 (May 2009): 409–19. http://dx.doi.org/10.2144/000113168.

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6

MADDY, A. H. "Analysis of Membrane Proteins." Biochemical Society Transactions 15, no. 3 (June 1, 1987): 571. http://dx.doi.org/10.1042/bst0150571.

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7

Chatterjee, Devjani, and Jacob V. Maizel. "Sequence analysis of proteins." Gene Analysis Techniques 4, no. 2 (March 1987): 27–40. http://dx.doi.org/10.1016/0735-0651(87)90015-x.

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8

Kelly, Robert H. "Electrophoretic analysis of proteins." Clinical Immunology Newsletter 13, no. 8 (August 1993): 93. http://dx.doi.org/10.1016/0197-1859(93)90015-c.

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9

Tanaka, I. "Structure analysis of ribosomal proteins." Seibutsu Butsuri 40, supplement (2000): S104. http://dx.doi.org/10.2142/biophys.40.s104_3.

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10

Swanson, Jessica MJ. "Multiscale kinetic analysis of proteins." Current Opinion in Structural Biology 72 (February 2022): 169–75. http://dx.doi.org/10.1016/j.sbi.2021.11.005.

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11

Kielkopf, Clara L., William Bauer, and Ina L. Urbatsch. "Analysis of Proteins by Immunoblotting." Cold Spring Harbor Protocols 2021, no. 12 (December 2021): pdb.prot102251. http://dx.doi.org/10.1101/pdb.prot102251.

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In immunoblotting (western blotting), proteins are first separated by SDS-PAGE and then transferred electrophoretically from the gel onto a support membrane that binds proteins tightly. After the unreacted binding sites of the membrane are blocked to suppress nonspecific adsorption of antibodies, the immobilized proteins are reacted with a specific polyclonal or monoclonal antibody. Antigen–antibody complexes are visualized using chromogenic, fluorescent, or chemiluminescent reactions. Immunoblotting protocols are reagent specific and, owing to the wide assortment of equipment, reagents, and antibodies available, highly diverse. Presented here is an example of a workable protocol for developing a blot using horseradish peroxidase (HRP)–conjugated secondary antibody and enhanced chemiluminescence (ECL). ECL is based on the emission of light during the HRP-catalyzed oxidation of luminal or other substrates. Emitted light is captured on film or by a CCD camera, for qualitative or semiquantitative analysis. Because ECL is so sensitive, it has become a popular detection method. This protocol can be modified for different membranes, antibodies, and detection systems. Optimal dilutions of the primary and secondary antibodies need to be determined empirically, but recommendations provided by the manufacturer are usually a good starting point.

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12

Priego-Capote, Feliciano, María Ramírez-Boo, Francesco Finamore, Florent Gluck, and Jean-Charles Sanchez. "Quantitative Analysis of Glycated Proteins." Journal of Proteome Research 13, no. 2 (January 13, 2014): 336–47. http://dx.doi.org/10.1021/pr4000398.

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13

Yan, JOHNSON F. "Sequence Analysis by Numbers: Proteins." Polymer-Plastics Technology and Engineering 35, no. 5 (September 1996): 697–726. http://dx.doi.org/10.1080/03602559608004056.

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14

Rossignol, Michel. "Proteomic analysis of phosphorylated proteins." Current Opinion in Plant Biology 9, no. 5 (October 2006): 538–43. http://dx.doi.org/10.1016/j.pbi.2006.07.004.

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15

Frickey, Tancred, and Andrei N. Lupas. "Phylogenetic analysis of AAA proteins." Journal of Structural Biology 146, no. 1-2 (April 2004): 2–10. http://dx.doi.org/10.1016/j.jsb.2003.11.020.

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16

Skjaerven, Lars, Siv M. Hollup, and Nathalie Reuter. "Normal mode analysis for proteins." Journal of Molecular Structure: THEOCHEM 898, no. 1-3 (March 2009): 42–48. http://dx.doi.org/10.1016/j.theochem.2008.09.024.

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17

Wilson, Richard, Daniele Belluoccio, and John F. Bateman. "Proteomic analysis of cartilage proteins." Methods 45, no. 1 (May 2008): 22–31. http://dx.doi.org/10.1016/j.ymeth.2008.01.008.

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18

Compton, Bruce Jon, and Lotte Kreilgaard. "Chromatographic analysis of therapeutic proteins." Analytical Chemistry 66, no. 23 (December 1994): 1175A—1180A. http://dx.doi.org/10.1021/ac00095a001.

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19

Jones, Andrew J. S. "Analysis of polypeptides and proteins." Advanced Drug Delivery Reviews 10, no. 1 (January 1993): 29–90. http://dx.doi.org/10.1016/0169-409x(93)90004-n.

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20

Loo, Tip W., and David M. Clarke. "Mutational analysis of ABC proteins." Archives of Biochemistry and Biophysics 476, no. 1 (August 2008): 51–64. http://dx.doi.org/10.1016/j.abb.2008.02.025.

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21

RYAN, NORMA M., PATRICK G. McCAULEY, and KAY OHLENDIECK. "Analysis of microsomal membrane proteins." Biochemical Society Transactions 18, no. 2 (April 1, 1990): 146–48. http://dx.doi.org/10.1042/bst0180146.

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22

Sweeney, H. L., and E. L. F. Holzbaur. "Mutational Analysis of Motor Proteins." Annual Review of Physiology 58, no. 1 (October 1996): 751–92. http://dx.doi.org/10.1146/annurev.ph.58.030196.003535.

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23

Mozdzanowski, Jacek, and David W. Speicher. "Microsequence analysis of electroblotted proteins." Analytical Biochemistry 207, no. 1 (November 1992): 11–18. http://dx.doi.org/10.1016/0003-2697(92)90492-p.

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24

Reim, David F., and David W. Speicher. "Microsequence analysis of electroblotted proteins." Analytical Biochemistry 207, no. 1 (November 1992): 19–23. http://dx.doi.org/10.1016/0003-2697(92)90493-q.

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25

Fenselau, Catherine, Martha M. Vestling, and Robert J. Cotter. "Mass spectrometric analysis of proteins." Current Opinion in Biotechnology 4, no. 1 (February 1993): 14–19. http://dx.doi.org/10.1016/0958-1669(93)90026-s.

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26

Szeberényi, József. "Analysis of mutant Ras proteins." Biochemistry and Molecular Biology Education 35, no. 6 (2007): 452–53. http://dx.doi.org/10.1002/bmb.20143.

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27

Islam, Suhail A., Jingchu Luo, and Michael J. E. Sternberg. "Identification and analysis of domains in proteins." "Protein Engineering, Design and Selection" 8, no. 6 (1995): 513–26. http://dx.doi.org/10.1093/protein/8.6.513.

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28

Vodička, Jan, Jiří Dostál, Dušan Holub, Radovan Pilka, Petr Džubák, Marián Hajdúch, and Tomáš Oždian. "Tissue expression analysis of cervical mucus proteome." Česká gynekologie 88, no. 1 (February 23, 2023): 4–12. http://dx.doi.org/10.48095/cccg20234.

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Cervical mucus is a viscous fluid functioning as a cervix plug. Products of the endometrial and cervical glands can be detected in the cervical mucus. Cervical mucus is further enriched with transudate originating from the fallopian tubes and proteins originating from the ovaries, peritoneum and distant tissues. With increasing levels of ovarian estrogens, the properties of cervical mucus for possible collection and processing change appropriately. For these reasons, we chose a group of 10 patients treated in the center of assisted reproduction by controlled ovarian stimulation for in vitro fertilization. This study focuses on the proteomic characterization of cervical mucus and localizes the possible sources of the identified proteins. The most abundant proteins were extracellular proteins, mainly mucins; however, most of the identified proteins, present usually in lower quantities, were of intracellular origin. The tissue analysis revealed that proteins from female reproductive organs are also expressed in other tissues in addition to female reproductive organs, but also proteins specific to the testis, liver, placenta, retina, and cerebellum. This study confirms the suitability and high potential of cervical mucus as a source of proteomic bio markers not only for the diagnosis of the female reproductive tract. Key words: cervical mucus – proteomics – tissue expression

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29

Basuri, Tarashankar, and Swatika S. Varli. "Tandam mass spectrometry instrumentation and application in pharmaceutical analysis." IP International Journal of Comprehensive and Advanced Pharmacology 9, no. 2 (June 15, 2024): 98–108. http://dx.doi.org/10.18231/j.ijcaap.2024.015.

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Proteins and peptides can be analyzed using mass spectrometry (MS) using a range of techniques, including matrix-aided laser desorption ionization-mass spectrometry (MALDI-MS) and electrospray ionization-mass spectrometry (ESI-MS). These techniques make it possible to determine a protein's mass as an intact molecule or to identify a protein using peptide-mass fingerprinting that is produced during enzymatic digestion. The amino acid sequence of proteins (top-down and middle-down proteomics) and peptides (bottom-up proteomics) can be ascertained by fragmenting the proteins and peptides using tandem mass spectrometry (MS/MS). Furthermore, post-translational modifications (PTMs) of proteins and peptides can be identified using tandem mass spectrometry. In this article, we go over the use of MS/MS in biomedical research and provide concrete examples of how to identify proteins, peptides, and their PTMs as useful biomarkers for diagnosis and treatment. In numerous applications, tandem mass spectrometry (MS/MS) has shown to be a practical and efficient analytical method for the direct detection of target compounds in food samples. It combines the power of MS/MS as an identification and confirmation approach with the separation capabilities of chromatography when used with chromatographic techniques.

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30

Moutaoufik, Mohamed Taha, and Robert M. Tanguay. "Analysis of insect nuclear small heat shock proteins and interacting proteins." Cell Stress and Chaperones 26, no. 1 (September 4, 2020): 265–74. http://dx.doi.org/10.1007/s12192-020-01156-3.

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31

Van Arnam, John S., Jonathan L. McMurry, May Kihara, and Robert M. Macnab. "Analysis of an Engineered Salmonella Flagellar Fusion Protein, FliR-FlhB." Journal of Bacteriology 186, no. 8 (April 15, 2004): 2495–98. http://dx.doi.org/10.1128/jb.186.8.2495-2498.2004.

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ABSTRACT Salmonella FliR and FlhB are membrane proteins necessary for flagellar export. In Clostridium a fliR-flhB fusion gene exists. We constructed a similar Salmonella fusion gene which is able to complement fliR, flhB, and fliR flhB null strains. Western blotting revealed that the FliR-FlhB fusion protein retains the FlhB protein's cleavage properties. We conclude that the FliR and FlhB proteins are physically associated in the wild-type Salmonella basal body, probably in a 1:1 ratio.

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32

Yamaguchi, Tetsuro, Kentaro Yamakawa, Takao Furuki, and Rie Hatanaka. "1P079 Analysis on the interaction between G3LEA proteins and other proteins by quartz crystal microbalance(01D. Protein : Function,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))." Seibutsu Butsuri 54, supplement1-2 (2014): S154. http://dx.doi.org/10.2142/biophys.54.s154_1.

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33

Nojima, Daisuke, Tomomi Nonoyama, Tomoko Yoshino, and Tsuyoshi Tanaka. "Lipid droplet-associated proteins in diverse microalgae revealed by proteomic analysis." Perspectives in Phycology 4, no. 1 (May 1, 2017): 25–32. http://dx.doi.org/10.1127/pip/2017/0069.

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34

Cai, Xianmei, and Chhabil Dass. "Conformational Analysis of Proteins and Peptides." Current Organic Chemistry 7, no. 18 (December 1, 2003): 1841–54. http://dx.doi.org/10.2174/1385272033486161.

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35

Rudakov, O. B., and L. V. Rudakova. "Amino acid analysis of milk proteins." Milk branch magazine, no. 12 (November 28, 2019): 32–35. http://dx.doi.org/10.33465/2222-5455-2019-12-32-35.

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36

Cho, Seonghyeon, Van-An Duong, Jeong-Hun Mok, Minjoong Joo, Jong-Moon Park, and Hookeun Lee. "Enrichment and analysis of glycated proteins." Reviews in Analytical Chemistry 41, no. 1 (January 1, 2022): 83–97. http://dx.doi.org/10.1515/revac-2022-0036.

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Abstract Glycation is a spontaneous post-translational modification of lysine, arginine, and the N-terminus of proteins. Protein glycation is closely related to the pathogenesis of human diseases, including diabetes, Alzheimer’s disease, renal disease, and cancer. The levels of advanced glycation end products (AGEs) are positively correlated with the progression of many diseases. However, it remains challenging to analyze glycation-related products, such as reactive carbonyl species, Schiff bases, Amadori compounds, and AGEs, because of their high heterogeneity. Many analysis methods, such as fluorescence detection, immunoassays, and liquid chromatography-tandem mass spectrometry, have attempted to correlate glycation products with diseases. Some enrichment methods have been used to increase the probability of detection of glycated proteins due to their low abundance in blood plasma. This review summarizes the enrichment and analysis methods that are currently used to identify glycation as a disease biomarker in exploratory studies.

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37

Murata, K. "Electron structural analysis of membrane proteins." Seibutsu Butsuri 41, supplement (2001): S18. http://dx.doi.org/10.2142/biophys.41.s18_2.

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38

Sonoyama, M. "Genome-wide analysis of membrane proteins." Seibutsu Butsuri 41, supplement (2001): S9. http://dx.doi.org/10.2142/biophys.41.s9_1.

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39

MIO, Kazuhiro, Toshihiko OGURA, Yuusuke MARUYAMA, and Chikara SATO. "Single Particle Analysis of Membrane Proteins." Seibutsu Butsuri 49, no. 3 (2009): 143–46. http://dx.doi.org/10.2142/biophys.49.143.

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40

Yamane, Ken, Atsushi Minamoto, Hidetoshi Yamashita, Hiroshi Takamura, Yuka Miyamoto-Myoken, Katsutoshi Yoshizato, Takuji Nabetani, Akira Tsugita, and Hiromu K. Mishima. "Proteome Analysis of Human Vitreous Proteins." Molecular & Cellular Proteomics 2, no. 11 (September 15, 2003): 1177–87. http://dx.doi.org/10.1074/mcp.m300038-mcp200.

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41

Pham, Trong Khoa, Pawel Sierocinski, John van der Oost, and Phillip C. Wright. "Quantitative Proteomic Analysis ofSulfolobus solfataricusMembrane Proteins." Journal of Proteome Research 9, no. 2 (February 5, 2010): 1165–72. http://dx.doi.org/10.1021/pr9007688.

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42

Bürger, Marco, Nils Schrader, Patricia Stege, and Ingrid R. Vetter. "Structural analysis of nuclear pore proteins." Acta Crystallographica Section A Foundations of Crystallography 66, a1 (August 29, 2010): s140. http://dx.doi.org/10.1107/s0108767310096893.

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43

Nandakumar, M. P., Agnes Cheung, and Mark R. Marten. "Proteomic Analysis of Extracellular Proteins fromEscherichiacoliW3110." Journal of Proteome Research 5, no. 5 (May 2006): 1155–61. http://dx.doi.org/10.1021/pr050401j.

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44

Wei, Candong, Jian Yang, Junping Zhu, Xiaobing Zhang, Wenchuan Leng, Jing Wang, Ying Xue, et al. "Comprehensive Proteomic Analysis ofShigellaflexneri2a Membrane Proteins." Journal of Proteome Research 5, no. 8 (August 2006): 1860–65. http://dx.doi.org/10.1021/pr0601741.

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45

Ma, Yuanhui, Daniel B. McClatchy, Salim Barkallah, William W. Wood, and John R. Yates. "Quantitative analysis of newly synthesized proteins." Nature Protocols 13, no. 8 (July 23, 2018): 1744–62. http://dx.doi.org/10.1038/s41596-018-0012-y.

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46

Collins, Mark O., Lu Yu, Marcelo P. Coba, Holger Husi, Iain Campuzano, Walter P. Blackstock, Jyoti S. Choudhary, and Seth G. N. Grant. "Proteomic Analysis ofin VivoPhosphorylated Synaptic Proteins." Journal of Biological Chemistry 280, no. 7 (November 30, 2004): 5972–82. http://dx.doi.org/10.1074/jbc.m411220200.

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47

BAGGERMAN, G., F. LIU, G. WETS, and L. SCHOOFS. "Bioinformatic Analysis of Peptide Precursor Proteins." Annals of the New York Academy of Sciences 1040, no. 1 (April 2005): 59–65. http://dx.doi.org/10.1196/annals.1327.006.

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48

YAMAMOTO, Shota, and Shin MORISHITA. "Natural vibration analysis of transmembrane proteins." Proceedings of the Bioengineering Conference Annual Meeting of BED/JSME 2018.30 (2018): 2B10. http://dx.doi.org/10.1299/jsmebio.2018.30.2b10.

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49

Lea, S., and D. Stuart. "Analysis of antigenic surfaces of proteins." FASEB Journal 9, no. 1 (January 1995): 87–93. http://dx.doi.org/10.1096/fasebj.9.1.7821764.

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50

Dowal, Louisa, Wei Yang, Michael R. Freeman, Hanno Steen, and Robert Flaumenhaft. "Proteomic analysis of palmitoylated platelet proteins." Blood 118, no. 13 (September 29, 2011): e62-e73. http://dx.doi.org/10.1182/blood-2011-05-353078.

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Abstract Protein palmitoylation is a dynamic process that regulates membrane targeting of proteins and protein-protein interactions. We have previously demonstrated a critical role for protein palmitoylation in platelet activation and have identified palmitoylation machinery in platelets. Using a novel proteomic approach, Palmitoyl Protein Identification and Site Characterization, we have begun to characterize the human platelet palmitoylome. Palmitoylated proteins were enriched from membranes isolated from resting platelets using acyl-biotinyl exchange chemistry, followed by identification using liquid chromatography-tandem mass spectrometry. This global analysis identified > 1300 proteins, of which 215 met criteria for significance and represent the platelet palmitoylome. This collection includes 51 known palmitoylated proteins, 61 putative palmitoylated proteins identified in other palmitoylation-specific proteomic studies, and 103 new putative palmitoylated proteins. Of these candidates, we chose to validate the palmitoylation of triggering receptors expressed on myeloid cell (TREM)–like transcript-1 (TLT-1) as its expression is restricted to platelets and megakaryocytes. We determined that TLT-1 is a palmitoylated protein using metabolic labeling with [3H]palmitate and identified the site of TLT-1 palmitoylation as cysteine 196. The discovery of new platelet palmitoyl protein candidates will provide a resource for subsequent investigations to validate the palmitoylation of these proteins and to determine the role palmitoylation plays in their function.

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