J. Michael Lord mainly focuses on Ricin, Biochemistry, Endoplasmic reticulum, Cytosol and Cell biology. His work deals with themes such as Molecular biology and Ribosome, Ribosome-inactivating protein, which intersect with Ricin. His Ricinus, Abrin and Molecular mass study, which is part of a larger body of work in Biochemistry, is frequently linked to Vacuole, bridging the gap between disciplines.
The various areas that J. Michael Lord examines in his Endoplasmic reticulum study include Endocytic cycle, Endocytosis and Lectin. His research integrates issues of Toxin and Protein degradation in his study of Cytosol. Cell biology and Secretory protein are frequently intertwined in his study.
Biochemistry, Ricin, Endoplasmic reticulum, Cell biology and Molecular biology are his primary areas of study. Biochemistry is closely attributed to Ribosome in his work. His Ricin research incorporates elements of Lectin, Ribosome-inactivating protein, Endocytosis and Ricinus.
His Endoplasmic reticulum research incorporates themes from Protein degradation and Cytosol. In his study, Shiga toxin is strongly linked to Cholera toxin, which falls under the umbrella field of Cell biology. His research in Molecular biology tackles topics such as Cytotoxicity which are related to areas like Cytotoxic T cell.
His main research concerns Ricin, Endoplasmic reticulum, Biochemistry, Cell biology and Golgi apparatus. J. Michael Lord combines subjects such as Transport protein and Ricinus with his study of Ricin. His Endoplasmic reticulum study incorporates themes from Endocytosis and Cytosol.
His Biochemistry research is multidisciplinary, incorporating elements of Ribosome and Ribosome-inactivating protein. His studies deal with areas such as Receptor, Shiga toxin and Cholera toxin as well as Cell biology. His Golgi apparatus course of study focuses on Vesicular transport protein and ADP ribosylation factor, Guanine nucleotide exchange factor, GTPase, Golgi disassembly and Diphtheria toxin.
His primary areas of investigation include Endoplasmic reticulum, Ricin, Cell biology, Endocytosis and Biochemistry. His work carried out in the field of Endoplasmic reticulum brings together such families of science as Cholera toxin, Chaperone, Endosome and Cytosol. His Endosome study combines topics in areas such as Pseudomonas exotoxin, KDEL and Internalization.
Much of his study explores Ricin relationship to Transport protein. His is doing research in Circular dichroism and Endosperm, both of which are found in Biochemistry. His Golgi apparatus research incorporates elements of Protein degradation, Glycosylation, ERAD pathway, Endoplasmic-reticulum-associated protein degradation and Glycoprotein.
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Nucleotide sequence of cloned cDNA coding for preproricin.
F. Ian Lamb;Lynne M. Roberts;J. Michael Lord.
FEBS Journal (1985)
Toxin Entry: Retrograde Transport through the Secretory Pathway
J. Michael Lord;Lynne M. Roberts.
Journal of Cell Biology (1998)
The low lysine content of ricin A chain reduces the risk of proteolytic degradation after translocation from the endoplasmic reticulum to the cytosol.
Emma D. Deeks;Jonathan P. Cook;Philip J. Day;Daniel C. Smith.
Biochemistry (2002)
Ricin A chain utilises the endoplasmic reticulum‐associated protein degradation pathway to enter the cytosol of yeast
Jeremy C. Simpson;Lynne M. Roberts;Karin Römisch;John Davey.
FEBS Letters (1999)
How Ricin and Shiga Toxin Reach the Cytosol of Target Cells: Retrotranslocation from the Endoplasmic Reticulum
Robert A. Spooner;J. Michael Lord.
Current Topics in Microbiology and Immunology (2011)
Single-chain ribosome inactivating proteins from plants depurinate Escherichia coli 23S ribosomal RNA.
Martin R. Hartley;Giuseppe Legname;Rupert Osborn;Zhaochun Chen.
FEBS Letters (1991)
Correlation between the activities of five ribosome‐inactivating proteins in depurination of tobacco ribosomes and inhibition of tobacco mosaic virus infection
Sally Taylor;Andrea Massiah;George Lomonossoff;Lynne M. Roberts.
Plant Journal (1994)
Protein disulphide-isomerase reduces ricin to its A and B chains in the endoplasmic reticulum.
Robert A. Spooner;Peter Duncan Watson;Catherine J. Marsden;Daniel C. Smith.
Biochemical Journal (2004)
Toxin entry: how reversible is the secretory pathway?
Hugh R.B. Pelham;Lynne M. Roberts;J.Michael Lord.
Trends in Cell Biology (1992)
The internal propeptide of the ricin precursor carries a sequence-specific determinant for vacuolar sorting
Lorenzo Frigerio;Nicholas A. Jolliffe;Alessandra Di Cola;Doramys Hernández Felipe.
Plant Physiology (2001)
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