Výsledky vyhledávání - "Anna Wilkins Maniccia"

Rational design of a conformation-switchable Ca2+- and Tb3+-binding protein without the use of multiple coupled metal-binding sites

Autor: Harianto Tjong, Jenny J. Yang, Wei Yang, Anna Wilkins Maniccia, Doyle J. Barrow, Shunyi Li, Huan-Xiang Zhou

Publikováno v: FEBS Journal. 275:5048-5061

Ca2+, as a messenger of signal transduction, regulates numerous target molecules via Ca2+-induced conformational changes. Investigation into the determinants for Ca2+-induced conformational change is often impeded by cooperativity between multiple me

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::cc90bb337543f98f42c9db8c22be6e8d
https://doi.org/10.1111/j.1742-4658.2008.06638.x

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Rational design of a novel calcium-binding site adjacent to the ligand-binding site on CD2 increases its CD48 affinity

Autor: P. Anton van der Merwe, Wei Yang, Jenny J. Yang, Anna Wilkins Maniccia, Lisa M. Jones, Alice Harrison

Publikováno v: Protein Science. 17:439-449

Electrostatic interactions are important for molecular recognition processes including Ca2+-binding and cell adhesion. To understand these processes, we have successfully introduced a novel Ca2+-binding site into the non-Ca2+-dependent cell adhesion

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3cce0dac33f0de61cb3043f55c4377c
https://doi.org/10.1110/ps.073328208

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Inverse tuning of metal binding affinity and protein stability by altering charged coordination residues in designed calcium binding proteins

Autor: Huan-Xiang Zhou, Julian A. Johnson, Shunyi Li, Jenny J. Yang, Harianto Tjong, Anna Wilkins Maniccia, Lev A Shaket, Wei Yang

Publikováno v: PMC Biophysics

Ca(2+ )binding proteins are essential for regulating the role of Ca(2+ )in cell signaling and maintaining Ca(2+ )homeostasis. Negatively charged residues such as Asp and Glu are often found in Ca(2+ )binding proteins and are known to influence Ca(2+

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ef4fc0bd29249b0a8b21534d279b0c2
https://pubmed.ncbi.nlm.nih.gov/20025729

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Using protein design to dissect the effect of charged residues on metal binding and protein stability

Autor: Shunyi Li, Julian A. Johnson, Anna Wilkins Maniccia, Jenny J. Yang, Wei Yang

Publikováno v: Biochemistry. 45(18)

Ca2+ controls biological processes by interacting with proteins with different affinities, which are largely influenced by the electrostatic interaction from the local negatively charged ligand residues in the coordination sphere. We have developed a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ed6dff4c48433fd1c3253861ddadf45
https://pubmed.ncbi.nlm.nih.gov/16669627

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