Search Results - "Fessler, L.I"

Drosophila UDP-glucose:glycoprotein glucosyltransferase: sequence and characterization of an enzyme that distinguishes between denatured and native proteins by Parker, C.G, Fessler, L.I, Nelson, R.E, Fessler, J.H

“…A Drosophila UDP glucose:glycoprotein glucosyl-transferase was isolated, cloned and characterized. Its 1548 amino acid sequence begins with a signal peptide,…”
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Laminin A chain: expression during Drosophila development and genomic sequence by Kusche-Gullberg, M, Garrison, K, MacKrell, A.J, Fessler, L.I, Fessler, J.H

“…A Drosophila laminin A chain gene was characterized as a 14 kb genomic nucleotide sequence which encodes an open reading frame of 3712 amino acids in 15 exons…”
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Peroxidasin: a novel enzyme-matrix protein of Drosophila development by Nelson, R.E, Fessler, L.I, Takagi, Y, Blumberg, B, Keene, D.R, Olson, P.F, Parker, C.G, Fessler, J.H

“…Peroxidasin is a novel protein combining peroxidase and extracellular matrix motifs. Hemocytes differentiate early from head mesoderm, make peroxidasin and…”
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Peroxidasin forms sulfilimine chemical bonds using hypohalous acids in tissue genesis by Bhave, Gautam, Cummings, Christopher F, Vanacore, Roberto M, Kumagai-Cresse, Chino, Ero-Tolliver, Isi A, Rafi, Mohamed, Kang, Jeong-Suk, Pedchenko, Vadim, Fessler, Liselotte I, Fessler, John H, Hudson, Billy G

“…Peroxidasin uses hypohalous acid oxidants to catalyze the formation of sulfilimine bonds in basement membranes. Collagen IV comprises the predominant protein…”
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Drosophila extracellular matrix by Fessler, L I, Nelson, R E, Fessler, J H

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Embryonic origin of hemocytes and their relationship to cell death in Drosophila by TEPASS, U, FESSLER, L. I, AZIZ, A, HARTENSTEIN, V

“…We have studied the embryonic development of Drosophila hemocytes and their conversion into macrophages. Hemocytes derive exclusively from the mesoderm of the…”
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Programmed cell death during Drosophila embryogenesis by ABRAMS, J. M, WHITE, K, FESSLER, L. I, STELLER, H

“…The deliberate and orderly removal of cells by programmed cell death is a common phenomenon during the development of metazoan animals. We have examined the…”
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Assembly and processing of procollagen type III in chick embryo blood vessels by Fessler, L I, Timpl, R, Fessler, J H

“…The processing of [3H]proline-labeled procollagen III in excised chick embryo blood vessels was found to differ significantly from that of procollagen I in the…”
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Separate amino and carboxyl procollagen peptidases in chick embryo tendon by Leung, M K, Fessler, L I, Greenberg, D B, Fessler, J H

“…Procollagen synthesized by freshly excised chick enbryo leg tendons is efficiently processed by proteolytic removal of first the amino propeptides and then the…”
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Characterization of type III procollagen from chick embryo blood vessels by Fessler, L I, Fessler, J H

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Papilin in development; a pericellular protein with a homology to the ADAMTS metalloproteinases by Kramerova, I A, Kawaguchi, N, Fessler, L I, Nelson, R E, Chen, Y, Kramerov, A A, Kusche-Gullberg, M, Kramer, J M, Ackley, B D, Sieron, A L, Prockop, D J, Fessler, J H

“…Papilin is an extracellular matrix glycoprotein that we have found to be involved in, (1) thin matrix layers during gastrulation, (2) matrix associated with…”
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Tiggrin, a novel Drosophila extracellular matrix protein that functions as a ligand for Drosophila alpha PS2 beta PS integrins by FOGERTY, F. J, FESSLER, L. I, BUNCH, T. A, YARON, Y, PARKER, C. G, NELSON, R. E, BROWER, D. L, GULLBERG, D, FESSLER, J. H

“…Genetic and other studies of Drosophila integrins have implicated these extracellular matrix receptors in various morphogenetic events, but identification of…”
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The PS2 integrin ligand tiggrin is required for proper muscle function in Drosophila by Bunch, T A, Graner, M W, Fessler, L I, Fessler, J H, Schneider, K D, Kerschen, A, Choy, L P, Burgess, B W, Brower, D L

“…Tiggrin is a novel extracellular matrix ligand for the Drosophila PS2 integrins. We have used flanking P elements to generate a precise deletion of tiggrin…”
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DFak56 is a novel Drosophila melanogaster focal adhesion kinase by Palmer, R.H, Fessler, L.I, Edeen, P.T, Madigan, S.J, McKeown, M, Hunter, T

“…The mammalian focal adhesion kinase (FAK) family of nonreceptor protein-tyrosine kinases have been implicated in controlling a multitude of cellular responses…”
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Drosophila PS1 integrin is a laminin receptor and differs in ligand specificity from PS2 by Gotwals, P.J. (Massachusetts Institute of Technology, Cambridge, MA.), Fessler, L.I, Wehrli, M, Hynes, R.O

“…We have expressed Drosophila position-specific (PS) integrins on the surfaces of Schneider S2 cells and tested for adhesion and spreading on various matrix…”
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DFak56 is a novel Drosophila melanogaster focal adhesion kinase by Palmer, R.H, Fessler, L.I, Edeen, P.T, Madigan, S.J, McKeown, M, Hunter, T

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Glutactin, a novel Drosophila basement membrane‐related glycoprotein with sequence similarity to serine esterases by Olson, P.F., Fessler, L.I., Nelson, R.E., Sterne, R.E., Campbell, A.G., Fessler, J.H.

“…Glutactin, a new acidic sulfated glycoprotein, was isolated from Drosophila Kc cell culture media. Immunofluorescence microscopy located it to embryonic…”
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Site-specific cleavage of basement membrane collagen IV during Drosophila metamorphosis by FESSLER, L. I, CONDIC, M. L, NELSON, R. E, FESSLER, J. H, FRISTROM, J. W

“…Breakdown of basement membranes is an important step in the controlled rearrangement of cells during metamorphosis, cell migration, and metastatic spread of…”
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Drosophila basement membrane procollagen IV. I. Protein characterization and distribution by Lunstrum, G P, Bächinger, H P, Fessler, L I, Duncan, K G, Nelson, R E, Fessler, J H

“…A collagen was isolated from Drosophila E85, Schneider line 2L and Kc cell cultures. The purified protein was characterized and antibodies were raised against…”
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Papilin: a Drosophila proteoglycan-like sulfated glycoprotein from basement membranes by Campbell, A G, Fessler, L I, Salo, T, Fessler, J H

“…A sulfated glycoprotein was isolated from the culture media of Drosophila Kc cells and named papilin. Affinity purified antibodies against this protein…”
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