• Publications
  • Influence
The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane.
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The migration of lymphocytes through the endothelium of venules in lymph nodes: an electron microscope study
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 areExpand
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Identification of the functional site of erythrocyte protein 4.1 involved in spectrin-actin associations.
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 wasExpand
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A Nonerythroid Isoform of Protein 4.1R Interacts with the Nuclear Mitotic Apparatus (NuMA) Protein
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 byExpand
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Interactions between protein 4.1 and band 3. An alternative binding site for an element of the membrane skeleton.
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 4.1Expand
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Regulation of the association of membrane skeletal protein 4.1 with glycophorin by a polyphosphoinositide
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. AExpand
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Stabilizing infrastructure of cell membranes.
  • V. Marchesi
  • Biology, Medicine
  • Annual review of cell biology
  • 1985
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A mutant deubiquitinating enzyme (Ubp-M) associates with mitotic chromosomes and blocks cell division.
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. TheExpand
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Erythrocyte spectrin is comprised of many homologous triple helical segments
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 isExpand
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Human erythrocyte membrane glycoprotein: a re-evaluation of the molecular weight as determined by SDS polyacrylamide gel electrophoresis.
Abstract Molecular weights for the human erythrocyte membrane glycoprotein and other glycoproteins calculated relative to protein standards on SDS acrylamide gel electrophoresis depend upon theExpand
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