Research Topics
| JOEL CHASISSummaryAffiliation: Lawrence Berkeley National Laboratory Country: USA Publications
Research Grants
| Collaborators
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Detail Information
Publications
Erythroblastic islands: specialized microenvironmental niches for erythropoiesisJoel Anne Chasis
Life Sciences Division, University of California, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA
Curr Opin Hematol 13:137-41. 2006..This review focuses on current understanding of molecular mechanisms operating within erythroblastic islands including cell-cell adhesion, regulatory feedback, and central macrophage function...
Erythroblastic islands: niches for erythropoiesisJoel Anne Chasis
Life Sciences Division, University of California, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA
Blood 112:470-8. 2008..Coupling of historical, current, and future insights will be essential to understand the tightly regulated production of red cells both in steady state and stress erythropoiesis...- Novel secreted isoform of adhesion molecule ICAM-4: potential regulator of membrane-associated ICAM-4 interactionsGloria Lee
Life Sciences Division, University of California, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA
Blood 101:1790-7. 2003..We postulate that secretion of this newly described isoform, ICAM-4S, may modulate binding of membrane-associated ICAM-4 and could thus play a critical regulatory role in erythroblast molecular attachments... - Two distinct domains of protein 4.1 critical for assembly of functional nuclei in vitroSharon Wald Krauss
Department of Subcellular Structure, Life Sciences Division, University of California, Lawrence Berkeley National Laboratory, 94720, USA
J Biol Chem 277:44339-46. 2002..1R. Our data establish that protein 4.1 is essential for nuclear assembly and identify two distinct 4.1 domains, initially characterized in cytoskeletal interactions, that have crucial and versatile functions in nuclear assembly... - Two protein 4.1 domains essential for mitotic spindle and aster microtubule dynamics and organization in vitroSharon Wald Krauss
Lawrence Berkeley National Laboratory, Life Sciences Division, University of California, Berkeley 94720, USA
J Biol Chem 279:27591-8. 2004..These investigations underscore an important functional context for protein 4.1 in microtubule morphogenesis and highlight a previously unappreciated role for 4.1 in cell division... - Nuclear substructure reorganization during late-stage erythropoiesis is selective and does not involve caspase cleavage of major nuclear substructural proteinsSharon Wald Krauss
Life Sciences Division, University of California Lawrence Berkeley National Laboratory, Bldg 74, 1 Cyclotron Rd, Berkeley, CA 94720, USA
Blood 106:2200-5. 2005..These findings imply that nuclear condensation and extrusion during terminal erythroid differentiation involve novel mechanisms that do not entail major activation of apoptotic machinery... - Targeted gene deletion demonstrates that the cell adhesion molecule ICAM-4 is critical for erythroblastic island formationGloria Lee
Life Sciences Division, University of California, Lawrence Berkeley National Laboratory, Bldg 74, 1 Cyclotron Road, Berkeley, CA 94720, USA
Blood 108:2064-71. 2006.... - Peptides based on alphaV-binding domains of erythrocyte ICAM-4 inhibit sickle red cell-endothelial interactions and vaso-occlusion in the microcirculationDhananjay K Kaul
Dept of Medicine, Albert Einstein College of Medicine, Bronx, NY 10461, USA
Am J Physiol Cell Physiol 291:C922-30. 2006..Thus peptides or small molecule mimetics of ICAM-4 may have therapeutic potential... - Protein 4.1R-dependent multiprotein complex: new insights into the structural organization of the red blood cell membraneMarcela Salomao
Red Cell Physiology Laboratory and Membrane Biochemistry Laboratory, New York Blood Center, New York, NY 10065, USA
Proc Natl Acad Sci U S A 105:8026-31. 2008.... - The Laminin 511/521-binding site on the Lutheran blood group glycoprotein is located at the flexible junction of Ig domains 2 and 3Tosti J Mankelow
Bristol Institute for Transfusion Sciences, National Blood Service, Southmead Road, Bristol, United Kingdom
Blood 110:3398-406. 2007..These studies imply that structural flexibility of Lutheran may be essential for its interaction with Laminin and present a novel opportunity for the development of therapeutics for sickle cell disease...
Research Grants
- NOVEL FUNCTIONS OF RED CELL PROTEINS LU AND LWJoel A Chasis; Fiscal Year: 2010..They are also relevant to diseases associated with bone marrow fibrosis and abnormal red blood cell production. ..
- NOVEL FUNCTIONS OF RED CELL PROTEINS LU AND LWJOEL CHASIS; Fiscal Year: 2009..They are also relevant to diseases associated with bone marrow fibrosis and abnormal red blood cell production. ..
- NOVEL FUNCTIONS OF RED CELL PROTEINS LU AND LWJOEL CHASIS; Fiscal Year: 2007..Successful accomplishment of these aims will further our goals of developing a mechanistic understanding of normal erythropoiesis and the pathophysiology of sickle cell disease which could lead to novel therapeutic modalities . ..
- NOVEL FUNCTIONS OF RED CELL PROTEINS LU AND LWJOEL CHASIS; Fiscal Year: 2003....
- GORDON CONFERENCE ON THE RED CELLJOEL CHASIS; Fiscal Year: 2003..approaches/interests combined with the richness of discussions of previous Red Cell Gordon Conferences has led to numerous productive collaborations and fostered new developments in these important areas of basic and clinical research ..