Výsledky vyhledávání - "Bruce Linders"

A Self-inactivating γ-Retroviral Vector Reduces Manifestations of Mucopolysaccharidosis I in Mice

Autor: Kevin K. Ohlemiller, Attila Kovacs, Li He, Douglas M. Tollefsen, Jason A. Metcalf, Axel Schambach, Xiucui Ma, Susan Wu, Bruce Linders, Katherine P. Ponder, Mark Bigg

Publikováno v: Molecular Therapy. 18(2):334-342

Mucopolysaccharidosis I (MPS I) is a lysosomal storage disease due to deficiency in alpha-L-iduronidase (IDUA) that results in accumulation of glycosaminoglycans (GAGs) throughout the body, causing numerous clinical defects. Intravenous administratio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35ac421f9ac25c539b04f9ac7d30f166

Zobrazit plný text záznamu

Effect of Lung Surfactant Collectins on Bronchoalveolar Macrophage Interaction withBlastomyces dermatitidis: Inhibition of Tumor Necrosis Factor Alpha Production by Surfactant Protein D

Autor: Bruce Linders, Elmer Brummer, Erika C. Crouch, Madhavi Lekkala, Michael J. Linke, Ann Marie LeVine, David A. Stevens

Publikováno v: Infection and Immunity. 74:4549-4556

Alveolar surfactant modulates the antimicrobial function of bronchoalveolar macrophages (BAM). Little is known about the effect of surfactant-associated proteins in bronchoalveolar lavage fluid (BALF) on the interaction of BAM andBlastomyces dermatit

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df779a652aba5bf5fa9f8220525edd1a
https://doi.org/10.1128/iai.00243-06

Zobrazit plný text záznamu

Upregulation of elastase activity in aorta in mucopolysaccharidosis I and VII dogs may be due to increased cytokine expression

Autor: Meg M. Sleeper, Michael P. Whyte, Katherine P. Ponder, Susan Wu, Patricia O'Donnell, Bruce Linders, Mark E. Haskins, Paul W. Bigg, Jason A. Metcalf

Publikováno v: Molecular genetics and metabolism. 99(4)

Mucopolysaccharidosis I (MPS I) and MPS VII are due to loss-of-function mutations within the genes that encode the lysosomal enzymes alpha-l-iduronidase and beta-glucuronidase, respectively, and result in accumulation of glycosaminoglycans and multis

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cbf59246bcecaa9dd770dd4594a3a7f1
https://pubmed.ncbi.nlm.nih.gov/20044292

Zobrazit plný text záznamu

Multimerization of surfactant protein D, but not its collagen domain, is required for antiviral and opsonic activities related to influenza virus

Autor: John E. Heuser, Bruce Linders, Tesfaldet Tecle, Erika C. Crouch, Paul S. Kingma, Mitchell R. White, Kevan L. Hartshorn, Nilgun Kacak

Publikováno v: Journal of immunology (Baltimore, Md. : 1950). 181(11)

Surfactant protein D (SP-D) plays important roles in the initial innate defense against influenza A virus (IAV). The collagen domain of SP-D is probably critical for its homeostatic functions in vivo and has been implicated in the modulation of macro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::02c6093f02fd8e23470c33efba1efcc3
https://pubmed.ncbi.nlm.nih.gov/19017984

Zobrazit plný text záznamu

Species Differences in the Carbohydrate Binding Preferences of Surfactant Protein D

Autor: Uffe Holmskov, Barbara McDonald, James F. Head, Kelly D. Smith, Erika C. Crouch, David Briner, Bruce Linders, Kevan L. Hartshorn, Joseph J. McDonald

Publikováno v: Crouch, E C, Smith, K, McDonald, B, Briner, D, Linders, B, McDonald, J, Holmskov, U, Head, J & Hartshorn, K 2006, ' Species Differences in the Carbohydrate Binding Preferences of Surfactant Protein D ', American Journal of Respiratory Cell and Molecular Biology, vol. 35, pp. 84-94 .

Udgivelsesdato: 2006 Interactions of surfactant protein D (SP-D) with micro-organisms and organic antigens involve binding to the trimeric neck plus carbohydrate recognition domain (neck+CRD). In these studies, we compared the ligand binding of homol

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c2f9c1fc00fa2d12c1458c1081fa16a
https://portal.findresearcher.sdu.dk/da/publications/1e58f6b0-d7b9-11db-ae98-000ea68e967b

Zobrazit plný text záznamu

Role of the alpha1 and alpha2 integrin cytoplasmic domains in cell morphology, motility and responsiveness to stimulation by the protein kinase C pathway

Autor: Samuel A. Santoro, Mary M. Zutter, Quiwei Gai, Zhengzhi Li, Haochuan Wang, Xun Yang, Bruce Linders

Publikováno v: Cell adhesion and communication. 7(4)

The alpha1beta1 and alpha2beta1 integrins, extracellular matrix receptors for collagens and/or laminins, have similarities in structure and ligand binding. Recent studies suggest that the two receptors mediate distinct post-ligand binding events and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d04d76b3d89c81c86c218722838d18a7
https://pubmed.ncbi.nlm.nih.gov/10714390

Zobrazit plný text záznamu

Small-Angle X-Ray Scattering Studies of ADAMTS13 Demonstrate a Conformational Response to Substrate Binding in Solution

Autor: Joshua Muia, Joseph D. Batchelor, Bruce Linders, Jian Zhu, Niraj H. Tolia, J. Evan Sadler

Publikováno v: Blood. 118:1191-1191

Abstract 1191 The metalloprotease ADAMTS13 inhibits the growth of platelet thrombi by cleaving the Tyr1605-Met1606 peptide bond in the A2 domain of von Willerbrand factor (VWF). Previous studies have shown that when subjected to tensile stress in sol

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d60e4c9bb1081ba1e95853c52afed2e3
https://doi.org/10.1182/blood.v118.21.1191.1191

Zobrazit plný text záznamu

Immunogenicity of MHC class I alloantigens expressed on parenchymal cells in the human kidney

Autor: T. Mohanakumar, Gregg A. Hadley, Bruce Linders

Publikováno v: Transplantation. 54(3)

The goal of the present study was to examine the capacity of human kidney cell lines (KCL) to elicit T cell responses to MHC class I alloantigens. KCL exhibited the phenotypic characteristics of tubular epithelial cells and were devoid of detectable

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::26f2f918198e7442703c936551aa4360
https://pubmed.ncbi.nlm.nih.gov/1412735

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání