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Journal articles on the topic 'Human Biochemistry'

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1

Bakhshilloyevna, Sultonova Dildor. "Biochemistry and molecular genetics of human glycogenoses." American Journal of Applied Sciences 7, no. 7 (2025): 78–82. https://doi.org/10.37547/tajas/volume07issue07-08.

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Most of the glycogen metabolism disorders that affect skeletal muscle involve enzymes of glycogenolysis (myophosphorylase ( PYGM ), glycogen debranching enzyme ( AGL ), phosphorylase b -kinase ( PHKB )) and glycolysis (phosphofructokinase ( PFK ), phosphoglyceromutase ( PGAM 2), aldolase A ( ALDOA ), β -enolase ( ENO 3)); however, 3 of them involve glycogen synthesis (glycogenin-1 ( GYG 1), glycogen synthase ( GSE ), and debranching enzyme ( GBE 1)). Many present with exercise-induced cramps and rhabdomyolysis with more intense exercise (ie, PYGM , PFK , PGAM 2), while others present with musc
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2

Hajjawi, Omar S. "Human Brain Biochemistry." American Journal of BioScience 2, no. 4 (2014): 122. http://dx.doi.org/10.11648/j.ajbio.20140204.13.

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3

Wiederschain, Gherman. "Human biochemistry and disease." Biochemistry (Moscow) 73, no. 11 (2008): 1269–70. http://dx.doi.org/10.1134/s000629790811014x.

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4

Zempleni, Janos, and DonaldM Mock. "Biotin biochemistry and human requirements." Journal of Nutritional Biochemistry 10, no. 3 (1999): 128–38. http://dx.doi.org/10.1016/s0955-2863(98)00095-3.

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5

Kokubu, T., and Y. Takada. "Biochemistry of Human Converting Enzyme." Clinical and Experimental Hypertension. Part A: Theory and Practice 9, no. 2-3 (1987): 217–28. http://dx.doi.org/10.3109/10641968709164181.

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6

Murty, B. Ramachandra. "The biochemistry of human senescence." Resonance 11, no. 2 (2006): 17–26. http://dx.doi.org/10.1007/bf02837272.

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7

Kumar Trivedi, Mahendra, Alice Branton, Dahryn Trivedi, Gopal Nayak, Sambhu Charan Mondal, and Snehasis Jana. "Effect of the Consciousness Energy Healing Treatment on DMEM for the Proliferation and Differentiation of Human Bone Osteosarcoma Cells to Improve Bone Health." Trends Journal of Sciences Research 3, no. 3 (2018): 124–32. http://dx.doi.org/10.31586/biochemistry.0303.04.

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8

Trivedi, Mahendra Kumar, Alice Branton, Dahryn Trivedi, Gopal Nayak, Sambhu Charan Mondal, and Snehasis Jana. "Effect of the Consciousness Energy Healing Treatment on DMEM for the Proliferation and Differentiation of Human Bone Osteosarcoma Cells to Improve Bone Health." Trends Journal of Sciences Research 3, no. 3 (2018): 124–32. https://doi.org/10.31586/Biochemistry.0303.04.

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The bone health is an important part of healthy-life and longevity in current situation due to huge toxins and contaminants in the environment and food chain. Considering the importance of bone health in the modern era, the present study was undertaken to investigate the effect of the Consciousness Energy Healing (The Trivedi Effect®) Treatment on Dulbecco's Modified Eagle Medium (DMEM) in which the human bone osteosarcoma cells - MG-63 (ATCC® CRL-1427™) was grown for the assessment of bone cell proliferation and differentiation in vitro. The study parameters were assessed us
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9

Zakowski, Jack J., and David E. Bruns. "Biochemistry of Human Alpha Amylase Isoenzymes." CRC Critical Reviews in Clinical Laboratory Sciences 21, no. 4 (1985): 283–322. http://dx.doi.org/10.3109/10408368509165786.

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10

Silva, André M. N., Tânia Moniz, Baltazar de Castro, and Maria Rangel. "Human transferrin: An inorganic biochemistry perspective." Coordination Chemistry Reviews 449 (December 2021): 214186. http://dx.doi.org/10.1016/j.ccr.2021.214186.

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11

Auchus, Richard J., and William E. Rainey. "Adrenarche - physiology, biochemistry and human disease." Clinical Endocrinology 60, no. 3 (2004): 288–96. http://dx.doi.org/10.1046/j.1365-2265.2003.01858.x.

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12

Milne, Ginger L., Huiyong Yin, and Jason D. Morrow. "Human Biochemistry of the Isoprostane Pathway." Journal of Biological Chemistry 283, no. 23 (2008): 15533–37. http://dx.doi.org/10.1074/jbc.r700047200.

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13

Ewald, D. Rose, and Susan C. J. Sumner. "Blood type biochemistry and human disease." Wiley Interdisciplinary Reviews: Systems Biology and Medicine 8, no. 6 (2016): 517–35. http://dx.doi.org/10.1002/wsbm.1355.

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14

Samland, Anne K., and Georg A. Sprenger. "Transaldolase: From biochemistry to human disease." International Journal of Biochemistry & Cell Biology 41, no. 7 (2009): 1482–94. http://dx.doi.org/10.1016/j.biocel.2009.02.001.

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15

Liu, Brian C. S., and Micheal J. Droller. "Biochemistry of Human Bladder Tumor Invasion." Scandinavian Journal of Urology and Nephrology 25, sup138 (1991): 145–51. http://dx.doi.org/10.1080/21681805.1991.12068882.

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16

Omer Abdalla, Kamal. "Biochemistry, Medicinal Properties & Toxicity of Acacia Nilotica Fruits." Biomedical Research and Clinical Reviews 3, no. 2 (2021): 01–06. http://dx.doi.org/10.31579/2692-9406/040.

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Acacia nilotica tree is native to Africa, the Middle East and the Indian subcontinent. Due to its wide medicinal properties & uses this plant attracted the attention of many scientists. Its fruits are rich in more than 16 classes of different bioactive molecules & elements very beneficial for human health. These molecules & elements include tannins, saponins, phytosterols, cyclitols, alkaloids, anticoagulant agents, regulatory molecules, amines, mucilage, fibers, gums, proteins, various classes of amino acids, carbohydrates, terpenses, crude fats, oils, fatty acids & minerals.
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17

Hunter, Tony. "My biochemical journey from a Cambridge undergraduate to the discovery of phosphotyrosine." Biochemist 43, no. 6 (2021): 74–77. http://dx.doi.org/10.1042/bio_2021_197.

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The most notable moment in my career as a biochemist was the discovery of phosphotyrosine, a somewhat serendipitous finding that turned out to have some very important consequences, notably, in human cancer. My career as a biochemist which has spanned nearly 60 years, began when I was 16. At the time, I was in the sixth form at Felsted School, a boarding school in Essex England, and my biology master, David Sturdy, elected to teach me some extracurricular biochemistry, giving me one-on-one tutorials on glycolysis and the TCA cycle. These early biochemistry lessons turned out to be invaluable b
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18

Miros, Francois, Ran Liu, and Hongying Shen. "Systems biochemistry to “deorphanize” human mitochondrial proteome." Molecular Cell 82, no. 15 (2022): 2735–37. http://dx.doi.org/10.1016/j.molcel.2022.07.005.

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19

Schallreuter, Karin U., Mohamed M. A. E. L. Salem, Sybille Hasse, and Hartmut Rokos. "The redox - biochemistry of human hair pigmentation." Pigment Cell & Melanoma Research 24, no. 1 (2010): 51–62. http://dx.doi.org/10.1111/j.1755-148x.2010.00794.x.

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20

Harzer, G., M. Haug, and J. G. Bindels. "Biochemistry of human milk in early lactation." Zeitschrift für Ernährungswissenschaft 25, no. 2 (1986): 77–90. http://dx.doi.org/10.1007/bf02020737.

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21

Notarangelo, Luigi D., Min-Sung Kim, Jolan E. Walter, and Yu Nee Lee. "Human RAG mutations: biochemistry and clinical implications." Nature Reviews Immunology 16, no. 4 (2016): 234–46. http://dx.doi.org/10.1038/nri.2016.28.

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22

Di Nardo, Giovanna, and Gianfranco Gilardi. "Human aromatase: Perspectives in biochemistry and biotechnology." Biotechnology and Applied Biochemistry 60, no. 1 (2013): 92–101. http://dx.doi.org/10.1002/bab.1088.

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23

Agapiou, A., K. Mikedi, S. Karma, et al. "Physiology and biochemistry of human subjects during entrapment." Journal of Breath Research 7, no. 1 (2013): 016004. http://dx.doi.org/10.1088/1752-7155/7/1/016004.

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24

UEDA, Kazumitsu. "Biochemistry of Human P-Glycoproteins, the Multidrug Transporter." Journal of the agricultural chemical society of Japan 66, no. 11 (1992): 1617–24. http://dx.doi.org/10.1271/nogeikagaku1924.66.1617.

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25

Laker, M. F. "The Human Tissue Act: implications for clinical biochemistry." Annals of Clinical Biochemistry 43, no. 6 (2006): 427–30. http://dx.doi.org/10.1258/000456306778904704.

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26

Searle, Andrew. "Biochemistry in human nutrition and dietetics degree courses." Biochemical Society Transactions 30, no. 1 (2002): A23. http://dx.doi.org/10.1042/bst030a023a.

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27

Lönnerdal, B. "Biochemistry and physiological function of human milk proteins." American Journal of Clinical Nutrition 42, no. 6 (1985): 1299–317. http://dx.doi.org/10.1093/ajcn/42.6.1299.

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28

Mussap, Michele, and Mario Plebani. "Biochemistry and Clinical Role of Human Cystatin C." Critical Reviews in Clinical Laboratory Sciences 41, no. 5-6 (2004): 467–550. http://dx.doi.org/10.1080/10408360490504934.

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29

Handelman, Garry J. "The evolving role of carotenoids in human biochemistry." Nutrition 17, no. 10 (2001): 818–22. http://dx.doi.org/10.1016/s0899-9007(01)00640-2.

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30

Saffran, Murray. "Tetrahydrobiopterin: Basic biochemistry and role in human disease." Biochemical Education 26, no. 2 (1998): 189–90. http://dx.doi.org/10.1016/s0307-4412(98)00066-1.

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31

Morin, G. B. "The implications of telomerase biochemistry for human disease." European Journal of Cancer 33, no. 5 (1997): 750–60. http://dx.doi.org/10.1016/s0959-8049(97)00061-0.

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32

Vella, F. "The Biochemistry of Human Nutrition: A Desk Reference." Biochemical Education 15, no. 3 (1987): 160. http://dx.doi.org/10.1016/0307-4412(87)90063-x.

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33

Kaplan, L., J. J. Lopez Costa, S. E. Carbone, et al. "Neurotransmitters in human term placenta: biochemistry and immunochemistry." Placenta 10, no. 5 (1989): 502–3. http://dx.doi.org/10.1016/0143-4004(89)90150-1.

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34

Phelps, M., and J. Mazziotta. "Positron emission tomography: human brain function and biochemistry." Science 228, no. 4701 (1985): 799–809. http://dx.doi.org/10.1126/science.2860723.

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35

Roman, Marco, Petru Jitaru, and Carlo Barbante. "Selenium biochemistry and its role for human health." Metallomics 6, no. 1 (2014): 25–54. http://dx.doi.org/10.1039/c3mt00185g.

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36

Freeze, Hudson H. "Understanding Human Glycosylation Disorders: Biochemistry Leads the Charge." Journal of Biological Chemistry 288, no. 10 (2013): 6936–45. http://dx.doi.org/10.1074/jbc.r112.429274.

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37

Opresko, Patricia L., Wen-Hsing Cheng, and Vilhelm A. Bohr. "Junction of RecQ Helicase Biochemistry and Human Disease." Journal of Biological Chemistry 279, no. 18 (2004): 18099–102. http://dx.doi.org/10.1074/jbc.r300034200.

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38

Rubio Calvo, Amalia. "Diseño de un Ciclo de Mejora en la docencia no presencial de la asignatura Bioquímica Humana del Grado en Bioquímica." JORNADAS DE FORMACIÓN E INNOVACIÓN DOCENTE DEL PROFESORADO, no. 3 (2020): 3442–60. http://dx.doi.org/10.12795/9788447231003.156.

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39

Innis, Sheila M. "Omega-3 Fatty Acid Biochemistry: Perspectives from Human Nutrition." Military Medicine 179, no. 11S (2014): 82–87. http://dx.doi.org/10.7205/milmed-d-14-00147.

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40

Tobin, Desmond J. "Biochemistry of human skin—our brain on the outside." Chem. Soc. Rev. 35, no. 1 (2006): 52–67. http://dx.doi.org/10.1039/b505793k.

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41

Karg, E., G. Odh, E. Rosengren, A. Wittbjer, and H. Rorsman. "Melanin-related biochemistry of IGR 1 human melanoma cells." Melanoma Research 1, no. 1 (1991): 5–14. http://dx.doi.org/10.1097/00008390-199104000-00002.

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42

Valentine, J. S. "BIOCHEMISTRY: Enhanced: Delivering Copper Inside Yeast and Human Cells." Science 278, no. 5339 (1997): 817–18. http://dx.doi.org/10.1126/science.278.5339.817.

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43

Colman, Robert W., Marc Schapira, Ariane de Agostini, and Jurg A. Schifferli. "Biochemistry and Pathophysiology of Human Cl Inhibitor: Current Issues." Complement 2, no. 2-3 (1985): 111–26. http://dx.doi.org/10.1159/000467851.

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44

Goldstein, Joyce A., and Sonia M. F. de Morais. "Biochemistry and molecular biology of the human CYP2C subfamily." Pharmacogenetics 4, no. 6 (1994): 285–300. http://dx.doi.org/10.1097/00008571-199412000-00001.

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45

Streu, Craig N., David Thomas Moore, Paul C. Billings, et al. "Assessing the Biochemistry of Kindlin-3 In Human Platelets." Blood 116, no. 21 (2010): 2011. http://dx.doi.org/10.1182/blood.v116.21.2011.2011.

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Abstract Abstract 2011 Although both talin and kindlin-3 binding to the β3 cytoplasmic domain are required for agonist-induced αIIbβ3 activation in platelets, the biochemical basis for this dual requirement is not clear. Recent NMR and hydrogen-deuterium exchange studies of disulfide-stabilized complexes containing the full cytoplasmic domains of αIIb and β3 dispersed in detergent micelles or lipid bilayers revealed that the β3 cytoplasmic domain consists of three helices: a stable proximal helix contiguous with the transmembrane domain and two distal dynamic amphiphilic helices whose fluctuat
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46

DiMauro, Salvatore, Seiichi Tsujino, Sara Shanske, and Lewis P. Rowland. "Biochemistry and molecular genetics of human glycogenoses: An overview." Muscle & Nerve 18, S14 (1995): S10—S17. http://dx.doi.org/10.1002/mus.880181405.

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47

Arner, Peter. "Human fat cell lipolysis: Biochemistry, regulation and clinical role." Best Practice & Research Clinical Endocrinology & Metabolism 19, no. 4 (2005): 471–82. http://dx.doi.org/10.1016/j.beem.2005.07.004.

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48

Goetze, Jens P., Emil D. Bartels, Theodor W. Shalmi, Lilian Andraud-Dang, and Jens F. Rehfeld. "Biochemistry of the Endocrine Heart." Biology 11, no. 7 (2022): 971. http://dx.doi.org/10.3390/biology11070971.

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Production and release of natriuretic peptides and other vasoactive peptides are tightly regulated in mammalian physiology and involved in cardiovascular homeostasis. As endocrine cells, the cardiac myocytes seem to possess almost all known chemical necessities for translation, post-translational modifications, and complex peptide proteolysis. In several ways, intracellular granules in the cells contain not only peptides destined for secretion but also important granin molecules involved in maintaining a regulated secretory pathway. In this review, we will highlight the biochemical phenotype o
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49

Kräutler, B. "Vitamin B12: chemistry and biochemistry." Biochemical Society Transactions 33, no. 4 (2005): 806–10. http://dx.doi.org/10.1042/bst0330806.

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Vitamin B12, the ‘antipernicious anaemia factor’, is required for human and animal metabolism. It was discovered in the late 1940s and its unique corrin ligand was revealed approx. 10 years later by X-ray crystallography. The B12-coenzymes are cofactors in various important enzymatic reactions and are particularly relevant in the metabolism of anaerobic microorganisms. Microorganisms are the only natural sources of the B12-derivatives, whereas most spheres of life (except for the higher plants) depend on these cobalt corrinoids.
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50

Gautschi, Markus, Andreas Natsch, and Fridtjof Schröder. "Biochemistry of Human Axilla Malodor and Chemistry of Deodorant Ingredients." CHIMIA International Journal for Chemistry 61, no. 1 (2007): 27–32. http://dx.doi.org/10.2533/chimia.2007.27.

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