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Książki na temat „Inhibitor”

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Autor: Grafiati

Data publikacji: 4 czerwca 2021

Data aktualizacji: 29 lipca 2024

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1

Li, Rongshi, i Jeffrey A. Stafford, red. Kinase Inhibitor Drugs. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2009. http://dx.doi.org/10.1002/9780470524961.

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2

A, Stafford Jeffrey, red. Kinase inhibitor drugs. Hoboken, N.J: J. Wiley, 2009.

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3

Chang, Henry E. HIV protease inhibitor report. Wyd. 2. Brooklyn, NY (72 Orange St., #3C, Brooklyn 11201): National AIDS Treatment Advocacy Project, 1996.

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4

Bashein, Abdulla Masood. Vitreous-derived inhibitor of angiogenesis. Manchester: University of Manchester, 1995.

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5

C, Shirley Anne, red. Trends in serotonin uptake inhibitor research. Hauppauge, NY: Nova Science Pub., 2004.

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6

Krämer, Oliver H., red. HDAC/HAT Function Assessment and Inhibitor Development. New York, NY: Springer US, 2023. http://dx.doi.org/10.1007/978-1-0716-2788-4.

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7

Krämer, Oliver H., red. HDAC/HAT Function Assessment and Inhibitor Development. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-6527-4.

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8

Lendeckel, Uwe, i Nigel M. Hooper, red. Viral Proteases and Antiviral Protease Inhibitor Therapy. Dordrecht: Springer Netherlands, 2009. http://dx.doi.org/10.1007/978-90-481-2348-3.

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9

Miskei, Gyorgy Zsolt. Studies on lung lavage alphai proteinase inhibitor. Birmingham: University of Birmingham, 1998.

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10

H, Kennedy Sidney, red. Clinical advances in monoamine oxidase inhibitor therapies. Washington, DC: American Psychiatric Press, 1994.

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11

Iqbal, Choudhary Muhammad, red. Biological inhibitors. Amsterdam: Harwood Academic Publishers, 1996.

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12

Helmsen, Sabine. Protein-Ligand-, Protein-Inhibitor- und Protein-Protein-Wechselwirkungen. Wiesbaden: Springer Fachmedien Wiesbaden, 2020. http://dx.doi.org/10.1007/978-3-658-30151-4.

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13

Mullen, Elizabeth Anne. An inhibitor of angiogenesis isolated from bovine cornea. [s.l: s.n.], 1992.

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14

Seeney, A. A study of molybdate as a corrosion inhibitor. Birmingham: University of Birmingham, 1986.

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15

König, Birgit. Biologisch aktive Polypeptide in Meeresschwämmen: Ein Kallikrein-Inhibitor. [s.l.]: [s.n.], 1995.

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16

Bond, Charles S. Trypanothione reductase: structure, specificity and approaches to inhibitor identification. Manchester: University of Manchester, 1995.

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17

C, Moellering Robert, red. Therapeutic implications of treatment with beta-lactamase inhibitor combinations. Montreal: PharmaLibri Publishers, 1994.

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18

Chen, Ginny. Analysis of Saccharomyces cerevisiae cyclin dependent kinase inhibitor Far1. Ottawa: National Library of Canada, 2003.

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19

Estrada, Sergio. Cystatin A, a mammalian cysteine proteinase inhibitor: Mechanism of inhibition of target proteinases by recombinant cystatin A variants. Uppsala: Sveriges Lantbruksuniversitet, 1998.

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20

Mendonça Teixeira, Alexandre, Lara de Oliveira Arinelli, José Luiz de Medeiros i Ofélia de Queiroz Fernandes Araújo. Monoethylene Glycol as Hydrate Inhibitor in Offshore Natural Gas Processing. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-66074-5.

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21

Storm, Detlef. Untersuchung von "clearance"-Mechanismen für C1-Inhibitor-C1-Esterase-Komplexe. [s.l.]: [s.n.], 1997.

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22

Kjaeldgaard, Marianne. Studies on tissue plasminogen activator and its inhibitor in human saliva. Stockholm: Kongl. Carolinska Medico Chirurgiska Institutet, 1991.

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23

Kjaeldgaard, Marianne. Studies on tissue plasminogen activator and its inhibitor in human saliva. [S.l: s.n.], 1991.

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24

Reynolds, Alastair. Inhibitor Phase. Orbit, 2021.

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25

Reynolds, Alastair. Inhibitor Phase. Orbit, 2021.

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26

Reynolds, Alastair. Inhibitor Phase. Hachette Book Group and Blackstone Publishing, 2021.

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27

Reynolds, Alastair. Inhibitor Phase. Orion Publishing Group, Limited, 2021.

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28

Inhibitor Phase. London, UK: Orion Publishing Group, Limited, 2022.

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29

Inhibitor Phase. Orbit, 2021.

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30

Purich, Daniel L. The Inhibitor Index. CRC Press, 2017. http://dx.doi.org/10.1201/9781315184289.

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31

Li, Rongshi, i Jeffrey A. Stafford. Kinase Inhibitor Drugs. Wiley & Sons, Incorporated, John, 2011.

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32

Li, Rongshi, i Jeffrey A. Stafford. Kinase Inhibitor Drugs. Wiley & Sons, Incorporated, John, 2011.

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33

Li, Rongshi, i Jeffrey A. Stafford. Kinase Inhibitor Drugs. Wiley & Sons, Incorporated, John, 2009.

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34

Kinase Inhibitor Drugs. Wiley & Sons, Incorporated, John, 2009.

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35

Fleischmann, Roy. Signalling pathway inhibitors. Oxford University Press, 2013. http://dx.doi.org/10.1093/med/9780199642489.003.0081.

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Oral, small-molecule signalling pathway inhibitors, including ones that inhibit the JAK and SyK pathways, are currently in development for the treatment of rheumatoid arthritis (RA). Tofacitinib is an orally administered small-molecule inhibitor that targets the intracellular Janus kinase 3 and 1 (JAK1/3) molecules to a greater extent than JAK2 while baricitinib (formerly INCB028050) predominantly inhibits JAK1/2. Many of the proinflammatory cytokines implicated in the pathogenesis of RA utilize cell signalling that involves the JAK-STAT pathways and therefore inhibition of JAK-STAT signalling, by targeting multiple RA-associated cytokine pathways, has the potential to simultaneously reduce inflammation, cellular activation, and proliferation of key immune cells. Fostamatinib disodium is an orally available inhibitor of spleen tyrosine kinase (SyK), which is a cytoplasmic tyrosine kinase that is an important mediator of immunoreceptor signalling in mast cells, macrophages, neutrophils, and B cells. Interruption of SyK signalling may interrupt production of tumour necrosis factor (TNF) and metalloproteinase and therefore affect RA disease activity. Tofacitinib has been investigated in multiple phase 2 and phase 3 trials which have investigated its efficacy (clinical, functional, and radiographic) and safety in patients who have failed disease-modifying anti-inflammatory drugs (DMARDs) as monotherapy or in combination with DMARDs, compared to an inhibitor of tumour necrosis factor alpha (TNFα‎) and in patients who have failed TNFα‎ inhibitors. The efficacy of fostamatinib and baricitinib has been investigated in phase 2 trials; both are in large phase 3 clinical programmes. Each of these medications has demonstrated efficacy; their safety profile has been shown to be different from each other and from currently approved biological agents. This chapter discusses what is currently known and understood about their efficacy and safety.

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36

COX-2 Inhibitor Research. Nova Science Publishers, 2006.

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37

Howardell, Maynard J. Cox-2 Inhibitor Research. Nova Science Publishers, Incorporated, 2006.

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38

Enzyme Inhibitor from Marine Organisms. MDPI, 2020. http://dx.doi.org/10.3390/books978-3-03943-784-9.

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39

Duffy, J. A. The Inhibitor: The Stansfield House. iUniverse Publishing, 2011.

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40

Musumeci, Francesca, red. Kinase Inhibitor for Cancer Therapy. MDPI, 2024. http://dx.doi.org/10.3390/books978-3-7258-1289-9.

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41

Enzyme Inhibitor from Marine Organisms. Mdpi AG, 2020.

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42

Lawrence, Daniel A. Plasminogen activator inhibitor type 1. Unit for Applied Celland Molecualr Biology, UMEA University, 1989.

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43

Trends in Serotonin Uptake Inhibitor Research. Nova Biomedical Books, 2006.

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44

Problems With Protease Inhibitor Development Plans. Diane Pub Co, 1995.

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45

Thuveson, Maria. Intracellular Processing of Pre-A-Inhibitor. Uppsala Universitet, 1999.

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46

Colo.) Corrosion 9 (1996 Denver. Reviews on Corrosion Inhibitor Science & Technology. N A C E International, 1996.

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47

Raman. Reviews on Corrosion Inhibitor Science & Technology. Natl Assn of Corrosion, 1996.

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48

Howardell, Maynard J. Trends in Cox-2 Inhibitor Research. Nova Science Publishers, 2006.

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49

Reynolds, Alastair. Inhibitor Phase: A Revelation Space Novel. Orion Publishing Group, Limited, 2021.

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50

Kramer, Carolyn, i Emily Blumberg. Immunosuppressants and Antiretroviral Therapy in HIV-Positive Transplant Patients. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780190493097.003.0028.

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Protease inhibitors (PIs), especially ritonavir, are inhibitors of CYP3A4 and P-gp1 and can significantly increase levels of calcineurin inhibitors and mammalian target of rapamycin (mTOR) inhibitors. Cobicistat is an inhibitor of CYP3A4, and its effect on levels of calcineurin inhibitors and mTOR inhibitors is likely to be similar to that of ritonavir. Efavirenz may result in lower concentrations of calcineurin inhibitors and mTOR inhibitors. Dose reduction and careful attention to monitoring drug levels are critical to avoid toxicity and maintain therapeutic immunosuppressive concentrations when PIs or cobicistat are coadministered with calcineurin inhibitors or mTOR inhibitors. Although there is no formalized recommendation for the ideal antiretroviral therapy regimen in HIV-positive transplant recipients, a regimen consisting of two nucleoside reverse transcriptase and an integrase inhibitor minimizes the risk of drug–drug interactions and simplifies dosing of immunosuppressive agents while maintaining a high barrier to resistance.

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