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Molecular basis of filamin A-FilGAP interaction and its impairment in congenital disorders associated with filamin A mutations.

PloS one | 2009

Mutations in filamin A (FLNa), an essential cytoskeletal protein with multiple binding partners, cause developmental anomalies in humans.

Pubmed ID: 19293932 RIS Download

Research resources used in this publication

None found

Antibodies used in this publication

None found

Associated grants

  • Agency: NHLBI NIH HHS, United States
    Id: R01 HL019429
  • Agency: NHLBI NIH HHS, United States
    Id: R01 HL056252
  • Agency: NHLBI NIH HHS, United States
    Id: HL-56252
  • Agency: NHLBI NIH HHS, United States
    Id: HL-19429

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This is a list of tools and resources that we have found mentioned in this publication.


COILS: Prediction of Coiled Coil Regions in Proteins (tool)

RRID:SCR_008440

COILS is a program that compares a sequence to a database of known parallel two-stranded coiled-coils and derives a similarity score. By comparing this score to the distribution of scores in globular and coiled-coil proteins, the program then calculates the probability that the sequence will adopt a coiled-coil conformation.

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Sparky (tool)

RRID:SCR_014228

A graphical NMR assignment and integration program for proteins, nucleic acids, and other polymers. Sparky displays NMR spectra, the peaks of which users may pick, assign, and integrate using a graphical interface. Users can work with any number of 2, 3 or 4 dimensional spectra simultaneously. Spectra for input to Sparky can be produced with processing programs NMRPipe, Felix, VNMR, XWinNMR or UXNMR. Output consists of text peak lists showing assignments, chemical shifts, volumes, line widths, etc.

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CYANA (tool)

RRID:SCR_014229

Software for automated structure calculation of biological macromolecules on basis of conformational constraints from nuclear magnetic resonance. Program for automated NMR protein structure calculation. CYANA requires a sufficient list of assigned chemical shifts and lists of cross-peak positions and columns from 2D, 3D, or4D NOESY spectra in order to calculate the assignment of the NOESY cross-peaks and the 3D structure of the protein in solution.

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Assisted Model Building with Energy Refinement (AMBER) (tool)

RRID:SCR_014230

Software package of molecular simulation programs. It is distributed into AmberTools15 and Amber14. AmberTools15 is a software package which can carry out complete molecular dynamics simulations with either explicit water or generalized Born solvent models. It is distributed in source code format and must be compiled in order to be used. Amber14 builds on AmberTools15 by adding the pmemd program, which provides better performance on multiple CPUs and dramatic speed improvements on GPUs compared to sander (molecular dynamics). GPU info, manuals, and tutorials are available on the website.

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MODELLER (tool)

RRID:SCR_008395

Software tool as Program for Comparative Protein Structure Modelling by Satisfaction of Spatial Restraints. Used for homology or comparative modeling of protein three dimensional structures. User provides alignment of sequence to be modeled with known related structures and MODELLER automatically calculates model containing all non hydrogen atoms.

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