Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Michael W. Schelle"'
Autor:
Kimberly M Sogi, Zev J Gartner, Mark A Breidenbach, Mason J Appel, Michael W Schelle, Carolyn R Bertozzi
Publikováno v:
PLoS ONE, Vol 8, Iss 6, p e65080 (2013)
The genome of Mycobacterium tuberculosis (Mtb) encodes nine putative sulfatases, none of which have a known function or substrate. Here, we characterize Mtb's single putative type II sulfatase, Rv3406, as a non-heme iron (II) and α-ketoglutarate-dep
Externí odkaz:
https://doaj.org/article/b9b0a37a4d504cb69bdfc8b21cf1c5b6
Autor:
Benjamin C. Kline, Michael W. Schelle, Gregory T. Crimmins, Anat A. Herskovits, Peggy P. Ni, Nicole Meyer-Morse, Daniel A. Portnoy, Anthony T. Iavarone
Publikováno v:
Infection and Immunity. 77:3014-3022
Infection with wild-type Listeria monocytogenes activates a host cytosolic surveillance response characterized by the expression of beta interferon (IFN-β). We performed a genetic screen to identify L. monocytogenes transposon insertion mutants that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4662c02fb190d4ae7e6a75f51e8d2458
https://doi.org/10.1128/iai.01511-08
https://doi.org/10.1128/iai.01511-08
Publikováno v:
ChemBioChem. 7:1516-1524
Pathogenic bacteria have developed numerous mechanisms to survive inside a hostile host environment. The human pathogen Mycobacterium tuberculosis (M. tb) is thought to control the human immune response with diverse biomolecules, including a variety
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2bc18f3c8fe94235d0c81021e06d8646
https://doi.org/10.1002/cbic.200600224
https://doi.org/10.1002/cbic.200600224
Autor:
Carolyn R. Bertozzi, Sarah C. Hubbard, David J. Vocadlo, James M. Berger, Michael W. Schelle, Joseph D. Mougous, Dong H. Lee
Publikováno v:
Molecular Cell. 21:109-122
Summary Sulfate assimilation is a critical component of both primary and secondary metabolism. An essential step in this pathway is the activation of sulfate through adenylation by the enzyme ATP sulfurylase (ATPS), forming adenosine 5′-phosphosulf
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3e1ae85ac5a26bea0542d441141689e
https://doi.org/10.1016/j.molcel.2005.10.034
https://doi.org/10.1016/j.molcel.2005.10.034
Sulfated metabolites are abundant in higher eukaryotes, where they play roles in cell-to-cell communication. This chapter highlights recent advances in the understanding of sulfolipid-1 (SL-1) biosynthesis and discusses the potential biological signi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::98d20955857655cca05da72532d9b3f3
https://doi.org/10.1128/9781555815783.ch18
https://doi.org/10.1128/9781555815783.ch18
Autor:
Zev J. Gartner, Carolyn R. Bertozzi, Mark A. Breidenbach, Mason J. Appel, Kimberly M. Sogi, Michael W. Schelle
Publikováno v:
PLoS ONE, Vol 8, Iss 6, p e65080 (2013)
PLoS ONE
PLoS ONE
The genome of Mycobacterium tuberculosis (Mtb) encodes nine putative sulfatases, none of which have a known function or substrate. Here, we characterize Mtb's single putative type II sulfatase, Rv3406, as a non-heme iron (II) and α-ketoglutarate-dep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9bf42769230dce3a8d2636083ce5eac3
http://europepmc.org/articles/PMC3675115?pdf=render
http://europepmc.org/articles/PMC3675115?pdf=render
Autor:
Cynthia M. Holsclaw, Carolyn R. Bertozzi, Julie A. Leary, Michael W. Schelle, Jeffery S. Cox, Clifton D. Leigh, Sarah A. Gilmore, Madhulika Jain
Publikováno v:
ACS chemical biology, vol 7, iss 5
ACS Chemical Biology
ACS Chemical Biology
Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis, is a highly evolved human pathogen characterized by its formidable cell wall. Many unique lipids and glycolipids from the Mtb cell wall are thought to be virulence factors that me
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d695a2fb57e4580b50e2cc0901cf4ce
https://escholarship.org/uc/item/6tv006cx
https://escholarship.org/uc/item/6tv006cx
Autor:
Julie A. Leary, Cynthia M. Holsclaw, Sarah A. Gilmore, Zsofia Botyanszki, Jessica C. Seeliger, Michael W. Schelle, Benjamin F. Cravatt, Michael Niederweis, Carolyn R. Bertozzi, Sarah E. Tully
Publikováno v:
The Journal of Biological Chemistry
Background: Sulfolipid-1 (SL-1) is a Mycobacterium tuberculosis outer membrane lipid whose biosynthesis is not fully understood. Results: Chp1 catalyzes two acyl transfer reactions to form SL-1. Sap modulates SL-1 levels and transmembrane transport.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c48b63111db37096347e817071c9c5b
https://pubmed.ncbi.nlm.nih.gov/22194604
https://pubmed.ncbi.nlm.nih.gov/22194604
Autor:
Cynthia M. Holsclaw, Carolyn R. Bertozzi, Michael W. Schelle, Stavroula K. Hatzios, Robert C. Fahey, Gerald L. Newton, Kimberly M. Sogi
Publikováno v:
Bioorganicmedicinal chemistry letters. 21(17)
CysQ is a 3'-phosphoadenosine-5'-phosphatase that dephosphorylates intermediates from the sulfate assimilation pathway of Mycobacterium tuberculosis (Mtb). Here, we demonstrate that cysQ disruption attenuates Mtb growth in vitro and decreases the bio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b08d5800d2a86885dce2e4bcdbed77e0
https://pubmed.ncbi.nlm.nih.gov/21795043
https://pubmed.ncbi.nlm.nih.gov/21795043
Autor:
Michael W. Schelle, Brian L. Carlson, Christopher R. Behrens, Fiona L. Lin, Cynthia M. Holsclaw, Carolyn R. Bertozzi, Julie A. Leary, Pawan Kumar, Zsofia Botyanszki, Stavroula K. Hatzios
Publikováno v:
The Journal of Biological Chemistry
Mycobacterium tuberculosis possesses an unusual cell wall that is replete with virulence-enhancing lipids. One cell wall molecule unique to pathogenic M. tuberculosis is polyacyltrehalose (PAT), a pentaacylated, trehalose-based glycolipid. Little is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46f6667f10fa9f0bb4391baf2d73e223
https://pubmed.ncbi.nlm.nih.gov/19276083
https://pubmed.ncbi.nlm.nih.gov/19276083