J. Michael Lord

What is he best known for?

The fields of study he is best known for:

• Enzyme
• DNA
• Biochemistry

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.

His most cited work include:

• Nucleotide sequence of cloned cDNA coding for preproricin. (269 citations)
• Toxin Entry: Retrograde Transport through the Secretory Pathway (171 citations)
• Ricin A chain utilises the endoplasmic reticulum‐associated protein degradation pathway to enter the cytosol of yeast (133 citations)

What are the main themes of his work throughout his whole career to date?

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.

He most often published in these fields:

• Biochemistry (67.57%)
• Ricin (63.96%)
• Endoplasmic reticulum (43.24%)

What were the highlights of his more recent work (between 2005-2015)?

• Ricin (63.96%)
• Endoplasmic reticulum (43.24%)
• Biochemistry (67.57%)

In recent papers he was focusing on the following fields of study:

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.

Between 2005 and 2015, his most popular works were:

• How Ricin and Shiga Toxin Reach the Cytosol of Target Cells: Retrotranslocation from the Endoplasmic Reticulum (118 citations)
• Syntaxin 16 and syntaxin 5 are required for efficient retrograde transport of several exogenous and endogenous cargo proteins. (95 citations)
• Internalized Pseudomonas exotoxin A can exploit multiple pathways to reach the endoplasmic reticulum. (67 citations)

In his most recent research, the most cited papers focused on:

• Enzyme
• DNA
• Amino acid

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.