• Refine Query
  • Source
  • Publication year
  • to
  • Language
  • 99
  • 41
  • 19
  • 15
  • 8
  • 6
  • 5
  • 3
  • 3
  • 2
  • 2
  • 1
  • 1
  • 1
  • 1
  • Tagged with
  • 246
  • 246
  • 46
  • 41
  • 37
  • 37
  • 32
  • 31
  • 27
  • 27
  • 27
  • 25
  • 25
  • 23
  • 21
  • About
  • The Global ETD Search service is a free service for researchers to find electronic theses and dissertations. This service is provided by the Networked Digital Library of Theses and Dissertations.
    Our metadata is collected from universities around the world. If you manage a university/consortium/country archive and want to be added, details can be found on the NDLTD website.
1

Expression and function of multidrug resistance-associated proteins (MRP) in human intestine

Prime-Chapman, Hannah Margaret January 2002 (has links)
No description available.
2

The GDNF family of neurotrophic factors : effects on adult sensory neurons

Boucher, Timothy John January 2001 (has links)
No description available.
3

Analysis of the role of RXR in monocyte-macrophage differentiation and function using U937 monoblastoid cells

Stonehouse, Timothy James January 1999 (has links)
No description available.
4

Expression of antisense RNA to investigate the interaction between unique and shared receptor subunits in the granulocyte-macrophage colony-stimulating factor (GM-CSF) receptor

Edwards, Jane Ann January 1999 (has links)
No description available.
5

Conditional regulation of Hoxa2 gene expression in CG4 cells

Wang, Juan (Monica) 02 August 2007
Oligodendrocytes (OLs) are the glial cells responsible for the synthesis and maintenance of myelin in the central nervous system. Recently, Hoxa2 was found by our laboratory to be expressed by OLs and down-regulated at the terminal differentiation stage during oligodendrogenesis in mice (Nicolay et al., 2004b). To further investigate the role of Hoxa2 in oligodendroglial development, a tetracycline regulated controllable expression system was utilized to establish two stable cell lines where the expression level of Hoxa2 gene could be up-regulated (CG4-SHoxa2 [sense Hoxa2]) or down-regulated (CG4-ASHoxa2 [Antisense Hoxa2]) in CG4 glial cells. Morphologically, no obvious differences were observed between CG4-SHoxa2 and CG4 wild-type cells, whereas CG4-ASHoxa2 cells exhibited much shorter processes compared with those of CG4 wild-type cells. Data from BrdU uptake assays indicated that an up-regulation of Hoxa2 gene promoted the proliferation of CG4-SHoxa2 cells. PDGF&alphaR (Platelet-derived growth factor [PDGF] receptor alpha), a receptor for the mitogen PDGF that enhances the survival and proliferation of OLs, was assessed at the mRNA level in both CG4 and CG4-SHoxa2 cells, but no significant differences were observed between Hoxa2 up-regulated cells and wild-type CG4 cells with respect to the mRNA level of PDGF&alphaR. In addition, specific investigations of the differentiation of CG4-SHoxa2 cells were carried out by characterizing the composition of stage specific oligodendroglial subpopulations in culture. Our immunocytochemical study did not indicate the differentiation course of the genetically engineered cells was significantly altered compared to CG4 wild-type cells, although results from semi-quantitative RT-PCR of oligodendrocyte-specific ceramide galactosyltransferase (CGT) and myelin basic protein (MBP) indicate that the differentiation of CG4-SHoxa2 cells was delayed when Hoxa2 gene was up-regulated.
6

Conditional regulation of Hoxa2 gene expression in CG4 cells

Wang, Juan (Monica) 02 August 2007 (has links)
Oligodendrocytes (OLs) are the glial cells responsible for the synthesis and maintenance of myelin in the central nervous system. Recently, Hoxa2 was found by our laboratory to be expressed by OLs and down-regulated at the terminal differentiation stage during oligodendrogenesis in mice (Nicolay et al., 2004b). To further investigate the role of Hoxa2 in oligodendroglial development, a tetracycline regulated controllable expression system was utilized to establish two stable cell lines where the expression level of Hoxa2 gene could be up-regulated (CG4-SHoxa2 [sense Hoxa2]) or down-regulated (CG4-ASHoxa2 [Antisense Hoxa2]) in CG4 glial cells. Morphologically, no obvious differences were observed between CG4-SHoxa2 and CG4 wild-type cells, whereas CG4-ASHoxa2 cells exhibited much shorter processes compared with those of CG4 wild-type cells. Data from BrdU uptake assays indicated that an up-regulation of Hoxa2 gene promoted the proliferation of CG4-SHoxa2 cells. PDGF&alphaR (Platelet-derived growth factor [PDGF] receptor alpha), a receptor for the mitogen PDGF that enhances the survival and proliferation of OLs, was assessed at the mRNA level in both CG4 and CG4-SHoxa2 cells, but no significant differences were observed between Hoxa2 up-regulated cells and wild-type CG4 cells with respect to the mRNA level of PDGF&alphaR. In addition, specific investigations of the differentiation of CG4-SHoxa2 cells were carried out by characterizing the composition of stage specific oligodendroglial subpopulations in culture. Our immunocytochemical study did not indicate the differentiation course of the genetically engineered cells was significantly altered compared to CG4 wild-type cells, although results from semi-quantitative RT-PCR of oligodendrocyte-specific ceramide galactosyltransferase (CGT) and myelin basic protein (MBP) indicate that the differentiation of CG4-SHoxa2 cells was delayed when Hoxa2 gene was up-regulated.
7

Plaque formation by dengue viruses under gum tragacanth overlayer and determination of virus growth curves in extracellular fluids of various cell lines /

Danee Laosunthorn. January 1976 (has links) (PDF)
Thesis (M.Sc. in Microbiology) -- Mahidol University, 1976.
8

Proteomic studies on anti-proliferating activities of adenosine and cordycepin in human cancer cell lines.

January 2004 (has links)
Tam Wai-Kwan Karen. / Thesis (M.Phil.)--Chinese University of Hong Kong, 2004. / Includes bibliographical references (leaves 109-128). / Abstracts in English and Chinese. / Thesis committee --- p.i / Statement --- p.ii / Abstract --- p.iii / Acknowledgements --- p.vi / Abbreviations --- p.vii / Table of Contents --- p.ix / List of Tables --- p.xii / List of Figures --- p.xiv / Chapter 1. --- Introduction --- p.1 / Chapter 2. --- Literature Review --- p.2 / Chapter 2.1 --- Introduction of Cordyceps --- p.2 / Chapter 2.2 --- Pharmacological functions of Cordyceps --- p.3 / Chapter 2.2.1 --- Functions in respiratory system --- p.3 / Chapter 2.2.2 --- Functions in renal system --- p.7 / Chapter 2.2.3 --- Functions in hepatic system --- p.8 / Chapter 2.2.4 --- Functions in cardiovascular system --- p.9 / Chapter 2.2.5 --- Functions in endocrine and steroid system --- p.10 / Chapter 2.2.6 --- Functions in the immune system --- p.11 / Chapter 2.2.7 --- Functions in nervous system --- p.15 / Chapter 2.2.8 --- Controls in glucose metabolism --- p.15 / Chapter 2.2.9 --- Anti-oxidation activity --- p.16 / Chapter 2.2.10 --- Anti-tumor activity --- p.18 / Chapter 2.3 --- Active ingredients of Cordyceps and their related biological activities --- p.20 / Chapter 2.3.1 --- Polysaccharides --- p.20 / Chapter 2.3.2 --- Nucleosides --- p.21 / Chapter 2.3.2.1 --- Adenosine --- p.21 / Chapter 2.3.2.2 --- Cordycepin --- p.24 / Chapter 2.4 --- Proteomic tools in studies of the change in protein expression --- p.25 / Chapter 2.4.1 --- Two-dimensional electrophoresis --- p.27 / Chapter 2.4.2 --- Mass Spectrometry --- p.28 / Chapter 3. --- Methods and Materials --- p.30 / Chapter 3.1 --- Cell lines and culture conditions --- p.30 / Chapter 3.2 --- Trypan blue exclusion method --- p.30 / Chapter 3.3 --- Cell counting --- p.31 / Chapter 3.4 --- Anti-proliferation assay --- p.31 / Chapter 3.5 --- Anti-proliferation assay of normal cell line --- p.32 / Chapter 3.6 --- Determination of ic50 --- p.33 / Chapter 3.7 --- Sample preparation for proteins studies --- p.33 / Chapter 3.8 --- Protein quantitation --- p.34 / Chapter 3.9 --- Gel electrophoresis --- p.36 / Chapter 3.10 --- Image analysis --- p.37 / Chapter 3.11 --- In-gel digestion and MALDI-ToF MS --- p.37 / Chapter 3.12 --- Statistical Analysis --- p.39 / Chapter 3.13 --- Chemicals --- p.39 / Chapter 4. --- Results --- p.41 / Chapter 4.1 --- MTT assay --- p.41 / Chapter 4.1.1 --- The anti-proliferating activity of adenosine against cancer cell lines (HepG2 and SV7tert) and normal cell line (Hs68) --- p.41 / Chapter 4.1.2 --- The anti-proliferating activity of cordycepin against cancer cell lines (HepG2 and SV7tert) and normal cell line (Hs68) --- p.42 / Chapter 4.1.3 --- The anti-proliferation effects of adenosine and cordycepin --- p.42 / Chapter 4.2 --- Changes in protein expression --- p.50 / Chapter 4.2.1 --- "Corresponding drug treatment of cell lines (HepG2, SV7tert and Hs68)" --- p.50 / Chapter 4.2.2 --- "Comparison of protein profiles from cells (HepG2, SV7tert or Hs68) under the normal and drug treated (with either adenosine or cordycepin) conditions" --- p.51 / Chapter 4.2.2.1 --- HepG2 study --- p.51 / Chapter 4.2.2.2 --- SV7tert study --- p.52 / Chapter 4.2.2.3 --- Hs68 study --- p.52 / Chapter 4.2.3 --- Protein identification --- p.53 / Chapter 4.2.3.1 --- HepG2 cell line --- p.53 / Chapter 4.2.3.2 --- HepG2-changes in protein expressions after adenosine treatment --- p.54 / Chapter 4.2.3.3 --- HepG2-changes in protein expressions after cordycepin treatment --- p.54 / Chapter 4.2.3.4 --- SV7tert cell line --- p.54 / Chapter 4.2.3.5 --- SV7tert-changes in protein expressions after cordycepin treatment --- p.55 / Chapter 4.2.3.6 --- Hs68 cell line --- p.55 / Chapter 4.2.3.7 --- Hs68-changes in protein expressions after cordycepin treatment --- p.56 / Chapter 5. --- Discussion --- p.89 / Chapter 5.1 --- anti-proliferation assays --- p.89 / Chapter 5.2 --- changes in protein expression: --- p.90 / Chapter 5.2.1 --- Protein alterations in HepG2 --- p.91 / Chapter 5.2.1.1 --- Changes in protein expression (membrane protein and transport: Trimethyllysine hydroxylase) --- p.91 / Chapter 5.2.1.2 --- Changes in protein expression (protein synthesis and folding: carboxypeptidase E) --- p.92 / Chapter 5.2.1.3 --- Changes in protein expression (membrane proteins and transport: calumenin and electron transfer flavoproteins) --- p.93 / Chapter 5.2.2 --- Protein alterations in SV7tert --- p.94 / Chapter 5.2.2.1 --- Changes in protein expression (protein synthesis and folding: BiP(GRP78)) --- p.94 / Chapter 5.2.2.2 --- Changes in protein expression (cell defense and tolerance: Hsp60 (chaperonin); TANK binding kinase-1) --- p.96 / Chapter 5.2.2.3 --- Changes in protein expression (metabolism: prolyl 4-hydroxylase; aldolase A; glyceraldehyde-3-phosphate dehydrogenase) --- p.97 / Chapter 5.2.2.4 --- Changes in protein expression (cell growth and division: βII tubulin; HnRNP Al) --- p.100 / Chapter 5.2.3 --- Protein alterations in Hs68 --- p.101 / Chapter 5.2.3.1 --- Changes in protein expression (metabolism: triosephosphate isomerse 1) --- p.101 / Chapter 6. --- Discussion --- p.103 / Chapter 6.1 --- The antiproliferating activities of adenosine and cordycepin --- p.103 / Chapter 6.2 --- "Effects of adenosine and cordycepin on the changes in protein expressions in HepG2, SV7tert and Hs68" --- p.104 / Chapter 6.3 --- Problems and improvements in two-dimensional gel electrophoresis --- p.105 / Chapter 7. --- Conclusion and future prospectives --- p.107 / References --- p.109
9

Intrathecal GDNF Gene Delivery Enhances Recovery from Neuropathic Pain in Rats

Wu, Ping-Ching 14 July 2003 (has links)
Neuronal cell death may be responsible for the pathogenesis of neuropathic pain. Glial cell line-derived neurotrophic factor (GDNF) protects sensory neurons after injury and offers a promising alternative for the management of intractable pain. However, continuous administration of trophic factors into the central nervous system is costly and difficult to maintain. Therefore, we evaluated the potential of intrathecal GDNF gene delivery for the treatment of neuropathic pain. Recombinant adenovirus encoding GDNF (Ad-GDNF) was characterized and shown to enhance viability of neuronal cultures. After intrathecal injection of Ad-GDNF, an elevated GDNF level was observed in spinal cord for four weeks. In rats with sciatic nerve axotomy,intrathecal injection of Ad-GDNF significantly ameliorated the duration of neuropathic pain. However, animals treated with Ad-GDNF developed hyperalgesia in the early stage of treatment. Immunofluorescence analysis indicated that intrathecal GDNF gene delivery prominently attenuated the neuronal loss due to nerve injury. Unexpectedly, varying degrees of hair loss was found in some rats receiving Ad-GDNF. Histological analysis revealed that hair loss resulted from severe degeneration of hair follicles in skin from Ad-GDNF-treated animals. In summary, the present study demonstrate the feasibility and limitations of GDNF gene delivery for the management of neuropathic pain.
10

An investigation into the biology of seminoma

Eastwood, Deborah Jane January 1999 (has links)
No description available.

Page generated in 0.0949 seconds