scholarly article | Q13442814 |
P50 | author | Jill Trewhella | Q18640471 |
Mitchell Guss | Q58307407 | ||
Cy M Jeffries | Q79137393 | ||
P2093 | author name string | Ann H Kwan | |
John Y H Chow | |||
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Calmodulin Wraps around Its Binding Domain in the Plasma Membrane Ca2+ Pump Anchored by a Novel 18-1 Motif | Q27658550 | ||
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Spinach calmodulin: isolation, characterization, and comparison with vertebrate calmodulins | Q71468433 | ||
Two nuclear localization signals in the HIV-1 matrix protein regulate nuclear import of the HIV-1 pre-integration complex | Q73910247 | ||
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Carp muscle calcium-binding protein. II. Structure determination and general description | Q28244663 | ||
A nuclear localization signal within HIV-1 matrix protein that governs infection of non-dividing cells | Q28249434 | ||
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Functional dynamics of the hydrophobic cleft in the N-domain of calmodulin | Q28363673 | ||
Crystal structures of apocalmodulin and an apocalmodulin/SK potassium channel gating domain complex | Q28569282 | ||
Association of integrase, matrix, and reverse transcriptase antigens of human immunodeficiency virus type 1 with viral nucleic acids following acute infection | Q28646834 | ||
Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set | Q29616463 | ||
Opposing mechanisms involving RNA and lipids regulate HIV-1 Gag membrane binding through the highly basic region of the matrix domain | Q33667586 | ||
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Calculation of standard atomic volumes for RNA and comparison with proteins: RNA is packed more tightly | Q34388031 | ||
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Human immunodeficiency virus type 1 Gag proteins are processed in two cellular compartments | Q34618267 | ||
Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly. | Q34984031 | ||
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Mutations in the N-terminal region of human immunodeficiency virus type 1 matrix protein block intracellular transport of the Gag precursor | Q36654136 | ||
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The N-terminal basic domain of the HIV-1 matrix protein does not contain a conventional nuclear localization sequence but is required for DNA binding and protein self-association. | Q40019816 | ||
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Solution X-ray scattering reveals a novel structure of calmodulin complexed with a binding domain peptide from the HIV-1 matrix protein p17. | Q46540414 | ||
Small-angle X-ray scattering reveals the N-terminal domain organization of cardiac myosin binding protein C. | Q46723642 | ||
Comparison of the crystal and solution structures of calmodulin and troponin C | Q48112277 | ||
Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible. | Q52443969 | ||
Structural similarity between the p17 matrix protein of HIV-1 and interferon-γ | Q57065085 | ||
Latent and active p53 are identical in conformation | Q58002479 | ||
P433 | issue | 4 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 702-714 | |
P577 | publication date | 2010-05-19 | |
P1433 | published in | Journal of Molecular Biology | Q925779 |
P1476 | title | Calmodulin disrupts the structure of the HIV-1 MA protein | |
P478 | volume | 400 |
Q60952323 | Bayesian inference of protein conformational ensembles from limited structural data |
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Q36150795 | Calmodulin binds a highly extended HIV-1 MA protein that refolds upon its release. |
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Q35312116 | NMR, biophysical, and biochemical studies reveal the minimal Calmodulin binding domain of the HIV-1 matrix protein |
Q37530471 | Post-translational intracellular trafficking determines the type of immune response elicited by DNA vaccines expressing Gag antigen of Human Immunodeficiency Virus Type 1 (HIV-1) |
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Q35761675 | Role of the HIV-1 Matrix Protein in Gag Intracellular Trafficking and Targeting to the Plasma Membrane for Virus Assembly |
Q27681606 | Solution Structure of Calmodulin Bound to the Binding Domain of the HIV-1 Matrix Protein |
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Q41767925 | The motif of human cardiac myosin-binding protein C is required for its Ca2+-dependent interaction with calmodulin |
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