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- Publications
- Influence
The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane.
- A. Chishti, A. Kim, +21 authors K. B. Hoover
- Chemistry, Medicine
- Trends in biochemical sciences
- 1 August 1998
The migration of lymphocytes through the endothelium of venules in lymph nodes: an electron microscope study
- V. Marchesi, J. Gowans
- Biology, Medicine
- Proceedings of the Royal Society of London…
- 14 January 1964
The post-capillary venules in the lymph nodes of rats have been examined with the electron microscope. The walls of these vessels normally contain many small lymphocytes, some of which are… Expand
Identification of the functional site of erythrocyte protein 4.1 involved in spectrin-actin associations.
- I. Correas, T. Leto, D. Speicher, V. Marchesi
- Biology, Medicine
- The Journal of biological chemistry
- 5 March 1986
Peptides produced by mild chymotryptic digestion of human erythrocyte protein 4.1 mimic the ability of intact 4.1 to promote the binding of spectrin to F-actin. This complex-promoting activity was… Expand
A Nonerythroid Isoform of Protein 4.1R Interacts with the Nuclear Mitotic Apparatus (NuMA) Protein
- S. Mattagajasingh, Shu-Ching Huang, J. S. Hartenstein, M. Snyder, V. Marchesi, E. Benz
- Biology, Medicine
- The Journal of cell biology
- 5 April 1999
Red blood cell protein 4.1 (4.1R) is an 80- kD erythrocyte phosphoprotein that stabilizes the spectrin/actin cytoskeleton. In nonerythroid cells, multiple 4.1R isoforms arise from a single gene by… Expand
Interactions between protein 4.1 and band 3. An alternative binding site for an element of the membrane skeleton.
- G. Pasternack, R. A. Anderson, T. Leto, V. Marchesi
- Biology, Medicine
- The Journal of biological chemistry
- 25 March 1985
Protein 4.1 from human erythrocytes formed a complex with band 3 in inside-out erythrocyte membrane vesicles and with soluble peptides derived from the cytoplasmic domain of band 3. Protein 4.1… Expand
Regulation of the association of membrane skeletal protein 4.1 with glycophorin by a polyphosphoinositide
- R. Anderson, V. Marchesi
- Biology, Medicine
- Nature
- 21 November 1985
Many of the physical properties of the erythrocyte membrane appear to depend on the membrane skeleton, which is attached to the membrane through associations with transmembrane proteins1–5. A… Expand
Stabilizing infrastructure of cell membranes.
- V. Marchesi
- Biology, Medicine
- Annual review of cell biology
- 1985
A mutant deubiquitinating enzyme (Ubp-M) associates with mitotic chromosomes and blocks cell division.
- S. Cai, R. Babbitt, V. Marchesi
- Biology, Medicine
- Proceedings of the National Academy of Sciences…
- 16 March 1999
A new ubiquitin-processing protease (Ubp-M) has been identified in mammalian cells that is phosphorylated at the onset of mitosis and dephosphorylated during the metaphase/anaphase transition. The… Expand
Erythrocyte spectrin is comprised of many homologous triple helical segments
- D. Speicher, V. Marchesi
- Biology, Medicine
- Nature
- 13 September 1984
Spectrin is an αβ heterodimeric protein (molecular weight (Mr) = 460,000) which is a major component of the erythrocyte membrane skeleton1–8. The membrane skeleton also includes actin (band 5) and is… Expand
Human erythrocyte membrane glycoprotein: a re-evaluation of the molecular weight as determined by SDS polyacrylamide gel electrophoresis.
- J. Segrest, R. Jackson, E. Andrews, V. Marchesi
- Chemistry, Medicine
- Biochemical and biophysical research…
- 16 July 1971
Abstract Molecular weights for the human erythrocyte membrane glycoprotein and other glycoproteins calculated relative to protein standards on SDS acrylamide gel electrophoresis depend upon the… Expand