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You searched for subject:(tau Proteins metabolism). Showing records 1 – 4 of 4 total matches.

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1. Matthews, Tori A. Pathological modifications of tau induce toxicity and facilitate cell death.

Degree: PhD, 2009, University of Alabama – Birmingham

lzheimer’s disease (AD) is a progressive neurodegenerative disorder characterized by two major pathophysiological hallmarks, beta-amyloid (A[Beta]) plaques and tau tangles. In AD and other tau(more)

Subjects/Keywords: Caspases  – metabolism<; br>; Cell Death  – physiology<; br>; Microtubules  – metabolism<; br>; tau Proteins  – physiology

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Matthews, T. A. (2009). Pathological modifications of tau induce toxicity and facilitate cell death. (Doctoral Dissertation). University of Alabama – Birmingham. Retrieved from http://contentdm.mhsl.uab.edu/u?/etd,607

Chicago Manual of Style (16th Edition):

Matthews, Tori A. “Pathological modifications of tau induce toxicity and facilitate cell death.” 2009. Doctoral Dissertation, University of Alabama – Birmingham. Accessed November 20, 2019. http://contentdm.mhsl.uab.edu/u?/etd,607.

MLA Handbook (7th Edition):

Matthews, Tori A. “Pathological modifications of tau induce toxicity and facilitate cell death.” 2009. Web. 20 Nov 2019.

Vancouver:

Matthews TA. Pathological modifications of tau induce toxicity and facilitate cell death. [Internet] [Doctoral dissertation]. University of Alabama – Birmingham; 2009. [cited 2019 Nov 20]. Available from: http://contentdm.mhsl.uab.edu/u?/etd,607.

Council of Science Editors:

Matthews TA. Pathological modifications of tau induce toxicity and facilitate cell death. [Doctoral Dissertation]. University of Alabama – Birmingham; 2009. Available from: http://contentdm.mhsl.uab.edu/u?/etd,607

2. Ding, Huiping. Regulation of tau functions by posttranslational modifications of tau and histone deacetylase 6.

Degree: PhD, 2008, University of Alabama – Birmingham

Alzheimer’s disease (AD), the most common neurodegenerative disease, is pathologically characterized by senile plaques composed of amyloid [beta] peptide and neurofibrillary tangles composed of hyperphosphorylated… (more)

Subjects/Keywords: Alzheimer Disease  – metabolism<; br>; Brain  – metabolism<; br>; Caspases  – metabolism<; br>; Histone Deacetylases  – metabolism<; br>; Microtubules  – metabolism<; br>; Neurons  – metabolism<; br>; tau Proteins  – metabolism

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Ding, H. (2008). Regulation of tau functions by posttranslational modifications of tau and histone deacetylase 6. (Doctoral Dissertation). University of Alabama – Birmingham. Retrieved from http://contentdm.mhsl.uab.edu/u?/etd,439

Chicago Manual of Style (16th Edition):

Ding, Huiping. “Regulation of tau functions by posttranslational modifications of tau and histone deacetylase 6.” 2008. Doctoral Dissertation, University of Alabama – Birmingham. Accessed November 20, 2019. http://contentdm.mhsl.uab.edu/u?/etd,439.

MLA Handbook (7th Edition):

Ding, Huiping. “Regulation of tau functions by posttranslational modifications of tau and histone deacetylase 6.” 2008. Web. 20 Nov 2019.

Vancouver:

Ding H. Regulation of tau functions by posttranslational modifications of tau and histone deacetylase 6. [Internet] [Doctoral dissertation]. University of Alabama – Birmingham; 2008. [cited 2019 Nov 20]. Available from: http://contentdm.mhsl.uab.edu/u?/etd,439.

Council of Science Editors:

Ding H. Regulation of tau functions by posttranslational modifications of tau and histone deacetylase 6. [Doctoral Dissertation]. University of Alabama – Birmingham; 2008. Available from: http://contentdm.mhsl.uab.edu/u?/etd,439

3. Dolan, Philip J. The role of post-translational modifications and valosin-containing protein in the turnover and stability of the microtubule-associated protein tau.

Degree: PhD, 2010, University of Alabama – Birmingham

Alzheimer Disease (AD) is pathologically characterized by the appearance of senile plaques composed of β-amyloid (Aβ) and neurofibrillary tangles composed of the microtubule-associated protein tau.… (more)

Subjects/Keywords: Alzheimer Disease  – enzymology<; br>; Autophagy<; br>; Caspases  – metabolism<; br>; Protein Kinases  – metabolism<; br>; Signal Transduction<; br>; tau Proteins  – physiology

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Dolan, P. J. (2010). The role of post-translational modifications and valosin-containing protein in the turnover and stability of the microtubule-associated protein tau. (Doctoral Dissertation). University of Alabama – Birmingham. Retrieved from http://contentdm.mhsl.uab.edu/u?/etd,1090

Chicago Manual of Style (16th Edition):

Dolan, Philip J. “The role of post-translational modifications and valosin-containing protein in the turnover and stability of the microtubule-associated protein tau.” 2010. Doctoral Dissertation, University of Alabama – Birmingham. Accessed November 20, 2019. http://contentdm.mhsl.uab.edu/u?/etd,1090.

MLA Handbook (7th Edition):

Dolan, Philip J. “The role of post-translational modifications and valosin-containing protein in the turnover and stability of the microtubule-associated protein tau.” 2010. Web. 20 Nov 2019.

Vancouver:

Dolan PJ. The role of post-translational modifications and valosin-containing protein in the turnover and stability of the microtubule-associated protein tau. [Internet] [Doctoral dissertation]. University of Alabama – Birmingham; 2010. [cited 2019 Nov 20]. Available from: http://contentdm.mhsl.uab.edu/u?/etd,1090.

Council of Science Editors:

Dolan PJ. The role of post-translational modifications and valosin-containing protein in the turnover and stability of the microtubule-associated protein tau. [Doctoral Dissertation]. University of Alabama – Birmingham; 2010. Available from: http://contentdm.mhsl.uab.edu/u?/etd,1090

4. Li, Zhiyong. Evaluation Of Tau As A Target For Alzheimer Disease And Other Conditions With Epileptiform Activity.

Degree: 2014, University of Alabama – Birmingham

Alzheimer disease (AD) is a devastating neurological condition that slowly destroys memory and thinking skills of the affected patients. No disease-modifying medications are available. While… (more)

Subjects/Keywords: Aged<; br>; Alzheimer Disease – therapy<; br>; Cognition Disorders<; br>; Epilepsy – therapy<; br>; Seizures<; br>; tau Proteins – metabolism

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Li, Z. (2014). Evaluation Of Tau As A Target For Alzheimer Disease And Other Conditions With Epileptiform Activity. (Thesis). University of Alabama – Birmingham. Retrieved from http://contentdm.mhsl.uab.edu/u?/etd,1800

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Li, Zhiyong. “Evaluation Of Tau As A Target For Alzheimer Disease And Other Conditions With Epileptiform Activity.” 2014. Thesis, University of Alabama – Birmingham. Accessed November 20, 2019. http://contentdm.mhsl.uab.edu/u?/etd,1800.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Li, Zhiyong. “Evaluation Of Tau As A Target For Alzheimer Disease And Other Conditions With Epileptiform Activity.” 2014. Web. 20 Nov 2019.

Vancouver:

Li Z. Evaluation Of Tau As A Target For Alzheimer Disease And Other Conditions With Epileptiform Activity. [Internet] [Thesis]. University of Alabama – Birmingham; 2014. [cited 2019 Nov 20]. Available from: http://contentdm.mhsl.uab.edu/u?/etd,1800.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Li Z. Evaluation Of Tau As A Target For Alzheimer Disease And Other Conditions With Epileptiform Activity. [Thesis]. University of Alabama – Birmingham; 2014. Available from: http://contentdm.mhsl.uab.edu/u?/etd,1800

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

.