Zobrazeno 1 - 10 of 91 pro vyhledávání: '"Joann Sanders"'
2
Catheter-Associated Urinary Tract Infection Reduction in a Pediatric Safety Engagement Network
Autor: Charles B. Foster, Joann Sanders, Patricia Sisson, Rachel E. Wenthe, Laurie Mustin, Kathy Ackerman, Vera Hupertz
Publikováno v: Pediatrics. 146
BACKGROUND: Catheter-associated urinary tract infections (CAUTIs) are a leading cause of health care–associated infection. Catheter insertion bundles (IBs) and maintenance bundles (MBs) have been developed to prevent CAUTIs but have not been extens
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee792c1be3ee66b52bffa17bcc314dfb
https://doi.org/10.1542/peds.2019-2057
Zobrazit plný text záznamu
3
Catheter-Associated Urinary Tract Infection Reduction in the Solutions for Patient Safety Pediatric Safety Engagement Network
Autor: Sisson Patricia, Vera Hupertz, Charles B. Foster, Joann Sanders, Laurie Mustin, Kathy Ackerman, Rachel E. Wenthe
Publikováno v: Infection Control & Hospital Epidemiology. 41:s152-s153
Background: Catheter-associated urinary tract infections (CAUTIs) are a leading cause of healthcare-associated infection. Catheter insertion and maintenance bundles have been developed to prevent CAUTIs, but they have not been extensively validated f
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b921861e5b4fcb85b43f6657551fa7b0
https://doi.org/10.1017/ice.2020.672
Zobrazit plný text záznamu
5
N-Isotope effects on the Raman spectra of Fe2S2 ferredoxin and Rieske ferredoxin: evidence for structural rigidity of metal sites
Autor: Frederik A.J. Rotsaert, Joann Sanders-Loehr, Jeremie D. Pikus, John L. Markley, Brian G. Fox
Publikováno v: JBIC Journal of Biological Inorganic Chemistry. 8:318-326
The diiron ferredoxins have a common diamond-core structure with two bridging sulfides, but differ in the nature of their terminal ligands: either four cysteine thiolates in the Fe(2)S(2) ferredoxins or two cysteine thiolates and two histidine imidaz
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12f8fa5fbc53031d0f8bdeeca3f28bce
https://doi.org/10.1007/s00775-002-0417-4
Zobrazit plný text záznamu
6
A New Type 2 Copper Cysteinate Azurin
Autor: Irene M. C. van Amsterdam, Gerard W. Canters, Frederik A.J. Rotsaert, Marcellus Ubbink, Marieke van den Bosch, Joann Sanders-Loehr
Publikováno v: Journal of Biological Chemistry. 277:44121-44130
The double mutant H117G/N42C azurin exhibits tetragonal type 2 copper site characteristics with Cys42 as one of the copper ligands as concluded from spectroscopic evidence (UV-visible, EPR, and resonance Raman). Analysis of the kinetics of copper upt
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::356bd997ef3dcf968198446981e949da
https://doi.org/10.1074/jbc.m202977200
Zobrazit plný text záznamu
7
The Catalytic Center in Nitrous Oxide Reductase, CuZ, Is a Copper−Sulfide Cluster
Autor: Ben C. Berks, Tim Rasmussen, Joann Sanders-Loehr, Walter G. Zumft, Andrew J. Thomson, David M. Dooley
Publikováno v: Biochemistry. 39:12753-12756
The crystal structure of nitrous oxide reductase, the enzyme catalyzing the final step of bacterial denitrification in which nitrous oxide is reduced to dinitrogen, exhibits a novel catalytic site, called Cu(Z). This comprises a cluster of four coppe
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2894adb6833dd1c455e15b0a3b9e2a0d
https://doi.org/10.1021/bi001811i
Zobrazit plný text záznamu
8
Resonance Raman Studies of the Stoichiometric Catalytic Turnover of a Substrate−Stearoyl-Acyl Carrier Protein Δ9 Desaturase Complex
Autor: Thomas M. Loehr, Jingyuan Ai, Joann Sanders-Loehr, Karen S. Lyle, Brian G. Fox, Pierre Möenne-Loccoz
Publikováno v: Biochemistry. 39:10507-10513
Resonance Raman spectroscopy has been used to study the effects of substrate binding (stearoyl-acyl carrier protein, 18:0-ACP) on the diferric centers of Ricinus communis 18:0-ACP Delta(9) desaturase. These studies show that complex formation produce
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0aac4388dede6ea0892d959915e41720
https://doi.org/10.1021/bi000965v
Zobrazit plný text záznamu
9
The O2 Binding Pocket of Myohemerythrin: Role of a Conserved Leucine
Autor: Jingyuan Ai, Shi Jin, Donald M. Kurtz, Joann Sanders-Loehr, Junjie Xiong, Robert S. Phillips
Publikováno v: Biochemistry. 39:8526-8536
A conserved O(2) binding pocket residue in Phascolopsis gouldii myohemerythrin (myoHr), namely, L104, was mutated to several other residues, and the effects on O(2) association and dissociation rates, O(2) affinity, and autoxidation were examined. Th
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::069d6d8c7865d437be00793a5d13a294
https://doi.org/10.1021/bi9929397
Zobrazit plný text záznamu
10
A Hemerythrin-like Domain in a Bacterial Chemotaxis Protein
Autor: Joann Sanders-Loehr, Junjie Xiong, Jingyuan Ai, Donald M. Kurtz
Publikováno v: Biochemistry. 39:5117-5125
Hemerythrin (Hr) is an O(2)-carrying protein found in some marine invertebrates. A conserved sequence motif in all Hrs provides five histidine and two carboxylate ligands to an oxo-/hydroxo-bridged diiron active site, as well as a hydrophobic O(2) bi
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f95c12de79a6b72db52ef419023199e
https://doi.org/10.1021/bi992796o
Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání

Omezení vyhledávání
Plný text Recenzováno Digitální knihovna AV ČR
Zdroje