Michael Landon - Concepedia

Author

Michael Landon

Also Known As

M J Landon, M Landon, M. J. LANDON, M. J. Landon, M. LANDON, M. Landon, M.J Landon, M.J. LANDON, M.J. Landon, MICHAEL LANDON

160

Publications

7.7K

Citations

H-Index

152

Concepts

All Affiliations

Queen's Medical Centre University of Nottingham Princess Mary Maternity Hospital University of California, Los Angeles Eötvös Loránd University

About

Michael Landon is an author at Queen's Medical Centre specializing in medicine, natural sciences, and biochemistry.

Top Concepts

#	Concept	H-Index	Publications	Citations
1	Medicine	31	47	2.9K
2	Natural Sciences	18	19	1.6K
3	Public Health	9	9	237
4	Social Sciences	4	4	188
5	Health Sciences	1	1	53

Michael Landon

Publications

6.5K

Citations

H-Index

Page 1

	Year	Citations
Beta amyloid protein deposition in the brain after severe head injury: implications for the pathogenesis of Alzheimer's disease. G.W. Roberts, Stephen M. Gentleman, Aoibhinn Lynch, Journal of Neurology Neurosurgery & Psychiatry	1994	565
Ubiquitin is a common factor in intermediate filament inclusion bodies of diverse type in man, including those of Parkinson's disease, Pick's disease, and Alzheimer's disease, as well as Rosenthal fibres in cerebellar astrocytomas, cytoplasmic bodies in muscle, and mallory bodies in alcoholic liver disease James Lowe, Andrew D. Blanchard, Ken Morrell, The Journal of Pathology	1988	542
Ubiquitin carboxyl‐terminal hydrolase (PGP 9.5) is selectively present in ubiquitinated inclusion bodies characteristic of human neurodegenerative diseases James Lowe, Helen McDermott, Michael Landon, The Journal of Pathology	1990	354
Inhibition of the ubiquitin-proteasome system in Alzheimer's disease Y. Amy Lam, Cecile M. Pickart, Andrew Alban, Proceedings of the National Academy of Sciences ProteasomeMolecular BiologyNeurochemical BiomarkersUbiquitin-proteasome SystemAlzheimer's Disease	2000	327
[15] Cleavage at aspartylprolyl bonds Michael Landon Methods in enzymology on CD-ROM/Methods in enzymology Aspartylprolyl BondsBiochemistrySupramolecular Chemistry	1977	319
Anomalous cleavage of aspartyl-proline peptide bonds during amino acid sequence determinations Dennis Piszkiewicz, Michael Landon, Emil L. Smith Biochemical and Biophysical Research Communications Protein ChemistryBiochemistryProtein FoldingNatural SciencesPeptide Library	1970	291
A filamentous inclusion body within anterior horn neurones in motor neurone disease defined by immunocytochemical localisation of ubiquitin James Lowe, Graham Lennox, D. Jefferson, Neuroscience Letters Motor Neurone DiseaseFilamentous Inclusion BodyAmyotrophic Lateral SclerosisAnterior Horn NeuronesNeuroanatomy	1988	226
αB crystallin expression in nonlenticular tissues and selective presence in ubiquitinated inclusion bodies in human disease James Lowe, Helen McDermott, Ian Pike, The Journal of Pathology	1992	211
Anti-ubiquitin immunocytochemistry is more sensitive than conventional techniques in the detection of diffuse Lewy body disease. Graham Lennox, James Lowe, Ken Morrell, Journal of Neurology Neurosurgery & Psychiatry ImmunologyDisease DetectionCortical Lewy BodiesNeurobiology Of DiseaseSerologic Testing	1989	194
Neurofibrillary tangles of Alzheimer's disease brains contain 14-3-3 proteins Robert Layfield, Jill Fergusson, Alistair Aitken, Neuroscience Letters Alzheimer's Disease14-3-3 ProteinsNeurochemical BiomarkersProtein MisfoldingNeurology	1996	191

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