Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Ambalika S. Khadria"'
Autor:
Ambalika S. Khadria, Ranga Rajan
Publikováno v:
The FASEB Journal. 36
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3b78e55e8fb0016475bc9692d5589ac0
https://doi.org/10.1096/fasebj.2022.36.s1.r2856
https://doi.org/10.1096/fasebj.2022.36.s1.r2856
Autor:
Alessandro Senes, Janice L. Robertson, Rahul Chadda, John A. Crooks, Loren M. LaPointe, Deena Al Mahbuba, Ambalika S. Khadria, Samson G.F. Condon, Aaron A. Hoskins, Gladys Diaz-Vazquez, Douglas B. Weibel, Samuel J. Craven, Qiang Cui, Claire R. Armstrong, Nambirajan Rangarajan
Publikováno v:
Journal of Biological Chemistry. 293:1623-1641
In Escherichia coli, FtsLB plays a central role in the initiation of cell division, possibly transducing a signal that will eventually lead to the activation of peptidoglycan remodeling at the forming septum. The molecular mechanisms by which FtsLB o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee1764c3c03e81dcac0e47fad7a61ab0
https://doi.org/10.1074/jbc.ra117.000426
https://doi.org/10.1074/jbc.ra117.000426
Autor:
Ambalika S. Khadria, Alessandro Senes
Publikováno v:
Biopolymers. 104:247-264
Forster resonance energy transfer (FRET) has been widely used as a spectroscopic tool in vitro to study the interactions between transmembrane (TM) helices in detergent and lipid environments. This technique has been instrumental to many studies that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::42db4d498a12994ce15f2f1780d9c960
https://doi.org/10.1002/bip.22667
https://doi.org/10.1002/bip.22667
Autor:
Alessandro Senes, Benjamin K. Mueller, Jonathan A. Stefely, Chin Huat Tan, Ambalika S. Khadria, David J. Pagliarini
Publikováno v:
Journal of the American Chemical Society
Interactions between α-helices within the hydrophobic environment of lipid bilayers are integral to the folding and function of transmembrane proteins; however, the major forces that mediate these interactions remain debated, and our ability to pred
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f569c2a840a15711322455d2fef07d0
https://doi.org/10.1021/ja505017f
https://doi.org/10.1021/ja505017f
Autor:
Claire R. Armstrong, Rahul Chadda, Alessandro Senes, Janice L. Robertson, Aaron A. Hoskins, Ambalika S. Khadria
Publikováno v:
Biophysical Journal. 112:501a
The divisome is a multi-protein complex required for bacterial cell division. The divisome has been extensively characterized genetically, but its structural organization and the oligomeric state of its components remain mostly unknown. An essential
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d37e9aed23e36dfe0cce3d23d0164fc9
https://doi.org/10.1016/j.bpj.2016.11.2713
https://doi.org/10.1016/j.bpj.2016.11.2713
Autor:
Alessandro Senes, Ambalika S. Khadria
Publikováno v:
Biophysical Journal. 106(2)
FtsB and FtsL are two essential integral membrane proteins of the bacterial division complex or "divisome", both characterized by a single transmembrane helix and a juxta-membrane coiled coil domain. The two domains are important for the association
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df1452a2e4b5aa4ec271a4ab7936dd9a
Autor:
Alessandro Senes, Ambalika S. Khadria
FtsB and FtsL are two essential integral membrane proteins of the bacterial division complex or "divisome", both characterized by a single transmembrane helix and a juxtamembrane coiled coil domain. The two domains are important for the association o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1dbb6d84c513fd4a10eb528d78a13790
https://europepmc.org/articles/PMC4133089/
https://europepmc.org/articles/PMC4133089/
Autor:
Ivan Rayment, Alessandro Senes, Ambalika S. Khadria, Loren M. LaPointe, Keenan C. Taylor, Sabareesh Subramaniam
Publikováno v:
Biochemistry. 52(15)
We report the first structural analysis of an integral membrane protein of the bacterial divisome. FtsB is a single-pass membrane protein with a periplasmic coiled coil. Its heterologous association with its partner FtsL represents an essential event
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a42c463d0895aa09a06a022058f73ac5
https://pubmed.ncbi.nlm.nih.gov/23520975
https://pubmed.ncbi.nlm.nih.gov/23520975
Autor:
Alessandro Senes, Ambalika S. Khadria
Publikováno v:
Membrane Proteins ISBN: 9781627035828
Present day understanding of the thermodynamic properties of integral membrane proteins (IMPs) lags behind that of water-soluble proteins due to difficulties in mimicking the physiological environment of the IMPs in order to obtain a reversible folde
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b916d48ff270c0469a9548abdc3b1fc6
https://doi.org/10.1007/978-1-62703-583-5_2
https://doi.org/10.1007/978-1-62703-583-5_2
Autor:
Alessandro Senes, Ambalika S. Khadria
Publikováno v:
Biophysical Journal. 108:39a
FtsB and FtsL are two essential integral membrane proteins of the bacterial division complex or ‘divisome’, both characterized by a single transmembrane helix and a juxta-membrane coiled coil domain. The two domains are important for the associat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6220c0ba9bb908c111bb959b079873ff
https://doi.org/10.1016/j.bpj.2014.11.242
https://doi.org/10.1016/j.bpj.2014.11.242