Publication date: 16 February 2016 Source:Biophysical Journal, Volume 110, Issue 3, Supplement 1
Author(s): Adina M. Kilpatrick, C. Andrew Fowler, Theodore Gurrola, Jerry E. Honts
[NMR paper] Structural insights into the calcium-mediated allosteric transition in the C-terminal domain of calmodulin from NMR measurements.
Structural insights into the calcium-mediated allosteric transition in the C-terminal domain of calmodulin from NMR measurements.
Related Articles Structural insights into the calcium-mediated allosteric transition in the C-terminal domain of calmodulin from NMR measurements.
Biochemistry. 2015 Nov 30;
Authors: Kukic P, Lundström P, Camilloni C, Evenäs J, Akke M, Vendruscolo M
Abstract
Calmodulin is a two-domain signalling protein that becomes activated upon binding cooperatively two pairs of calcium ions, leading to large-scale...
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Fluorescence Microscopy and Solution NMR Studies of Cytoskeletal Proteins from Tetrahymena
Fluorescence Microscopy and Solution NMR Studies of Cytoskeletal Proteins from Tetrahymena
Publication date: 27 January 2015
Source:Biophysical Journal, Volume 108, Issue 2, Supplement 1</br>
Author(s): Robert Sterner , Jerry Honts , Adina Kilpatrick</br>
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Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain
March 2012
Publication year: 2012
Source:Biochimie, Volume 94, Issue 3</br>
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The insulin-like growth factor binding proteins are a family of six proteins (IGFBP-1 to -6) that bind insulin-like growth factors-I and -II (IGF-I/II) with high affinity. In addition to regulating IGF actions, IGFBPs have IGF-independent functions. IGFBP-2, the largest member of this family, is over-expressed in many cancers and has been proposed as a possible target for the...
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Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Biochimie. 2011 Sep 22;
Authors: Galea CA, Mobli M, McNeil KA, Mulhern TD, Wallace JC, King GF, Forbes BE, Norton RS
Abstract
The insulin-like growth factor binding proteins are a family of six proteins (IGFBP-1 to 6) that bind insulin-like growth factors-I and -II (IGF-I/II) with high affinity. In addition...
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09-30-2011 06:00 AM
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Biochimie. 2011 Sep 22;
Authors: Galea CA, Mobli M, McNeil KA, Mulhern TD, Wallace JC, King GF, Forbes BE, Norton RS
Abstract
The insulin-like growth factor binding proteins are a family of six proteins (IGFBP-1 to 6) that bind insulin-like growth factors-I and -II (IGF-I/II) with high affinity. In...
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09-30-2011 05:59 AM
NMR, biophysical and biochemical studies reveal the minimal calmodulin-binding domain of the HIV-1 matrix protein.
NMR, biophysical and biochemical studies reveal the minimal calmodulin-binding domain of the HIV-1 matrix protein.
NMR, biophysical and biochemical studies reveal the minimal calmodulin-binding domain of the HIV-1 matrix protein.
J Biol Chem. 2011 Jul 28;
Authors: Samal AB, Ghanam RH, Fernandez TF, Monroe EB, Saad JS
Subcellular distribution of Calmodulin (CaM) in human immunodeficiency virus type-1 (HIV-1) infected cells is distinct from that observed in uninfected cells. CaM has been shown to interact and co-localize with the HIV-1 Gag protein...
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07-30-2011 11:23 AM
[NMR paper] NMR structural studies of domain 1 of receptor-associated protein.
NMR structural studies of domain 1 of receptor-associated protein.
Related Articles NMR structural studies of domain 1 of receptor-associated protein.
J Biomol NMR. 2004 Jul;29(3):271-9
Authors: Wu Y, Migliorini M, Walsh J, Yu P, Strickland DK, Wang YX
The 39 kDa receptor-associated protein (RAP) is an endoplasmic reticulum resident protein that binds tightly to the low-density lipoprotein receptor-related protein (LRP) as well as to other members of the low-density lipoprotein receptor superfamily. The association of RAP with LRP prevents...
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11-24-2010 09:51 PM
[NMR paper] Structural studies of the acidic transactivation domain of the Vmw65 protein of herpe
Structural studies of the acidic transactivation domain of the Vmw65 protein of herpes simplex virus using 1H NMR.
Related Articles Structural studies of the acidic transactivation domain of the Vmw65 protein of herpes simplex virus using 1H NMR.
Biochemistry. 1992 Apr 28;31(16):4150-6
Authors: O'Hare P, Williams G
We have overproduced and purified the carboxy-terminal transactivation domain of Vmw65 (VP16) of herpes simplex virus, and studied potential folding of the domain by 1H NMR. Two species of the acidic domain were obtained from the...
NMR Structural Studies of the C-Domain of Tcb2, A Calcium Binding Protein from Tetrahymena Thermophila
Linear Mode
