Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Matthew R. Naticchia"'
Autor:
Kamil Godula, Abhishek Singharoy, Pascal Gagneux, Matthew R. Naticchia, Meghan O. Altman, Taryn M. Lucas, Emi Sanchez, Chitrak Gupta
Publikováno v:
Chem, vol 7, iss 12
Chem
Chem
Influenza A viruses (IAVs) exploit host glycans in airway epithelial mucosa to gain entry and initiate infection. Rapid detection of changes in IAV specificity towards host glycan classes can provide early indication of virus transmissibility and inf
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c9ae726a5513d8aeba4ebf8196b9c3f0
https://doi.org/10.1016/j.chempr.2021.09.015
https://doi.org/10.1016/j.chempr.2021.09.015
Cell surface engineering with synthetic glycomimetic co-receptors for FGF2 was used to establish gradients of stem cells with enhanced FGF2 affinity in embryoid bodies (EBs). Gradient shape was controlled by pre-assembly of glycomimetics into nanosca
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::03785ceab5b38f4ab195a423fd327428
https://doi.org/10.26434/chemrxiv.12755849.v1
https://doi.org/10.26434/chemrxiv.12755849.v1
Autor:
Logan K. Laubach, Mia L. Huang, Kamil Godula, Ember M. Tota, Matthew R. Naticchia, Taryn M. Lucas
Publikováno v:
ACS Chemical Biology. 13:2880-2887
Cell surface glycans, such as heparan sulfate (HS), are increasingly identified as co-regulators of growth factor signaling in early embryonic development; therefore, chemical tailoring of HS activity within the cellular glycocalyx of stem cells offe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd71b7f7b2e72659d82ca4b467bb6442
https://doi.org/10.1021/acschembio.8b00436
https://doi.org/10.1021/acschembio.8b00436
Autor:
Kristin M Allan, Wesley J. Murphy, Jennifer E. Hurtig, Juliet Chepngeno, Jonathan K. Allotey, Herbert Sizek, Kevin A. Morano, Matthew Loberg, Jennifer M. Pilat, Afton H. Widdershins, Susmit Tripathi, Matthew R. Naticchia, Min Goo Kang, Joseph B. David, James West
Publikováno v:
Free Radical Biology and Medicine. 101:356-366
A broad range of redox-regulated proteins undergo reversible disulfide bond formation on oxidation-prone cysteine residues. Heightened reactivity of the thiol groups in these cysteines also increases susceptibility to modification by organic electrop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::876be6dcd3e2b39af0663dc324a035c7
https://doi.org/10.1016/j.freeradbiomed.2016.10.506
https://doi.org/10.1016/j.freeradbiomed.2016.10.506
Autor:
Haley A. Brown, James West, Andrew M. Lamade, Rachelle P. Herrin, Samantha L. Justice, Francisco J. Garcia, Kevin A. Morano, Matthew R. Naticchia
Thioredoxin protects cells against oxidative damage by reducing disulfide bonds in improperly oxidized proteins. Previously, we found that the baker's yeast cytosolic thioredoxin Trx2 undergoes cross-linking to form several protein-protein complexes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::60c80f4d5b5cbddd224a7de70c110fa7
https://europepmc.org/articles/PMC3637938/
https://europepmc.org/articles/PMC3637938/