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https://www.ncbi.nlm.nih.gov/geo/

THIS RESOURCE IS NO LONGER IN SERVICE, documented on January 19, 2022.

Proper citation: NCBI Epigenomics (RRID:SCR_006151) Copy   

•   Source: SciCrunch Registry

http://commonfund.nih.gov/molecularlibraries/ipdc/index.aspx

A core synthesis facility dedicated to the preparation of imaging probes, initially for intramural NIH scientists, and later, for the extramural scientific community. The IPDC provides a mechanism for the production of sensitive probes for use by imaging scientists who cannot obtain such probes commercially. The probes to be made will encompass all major imaging modalities including radionuclide, magnetic resonance, and optical. Nearly all of these imaging probes are not commercially available, nor are they viable commercial products, and most are new compositions-of-matter (http://nihlibrary.ors.nih.gov/ipdcdb/IPDCDB_Search.asp). The IPDC was born from the realization that imaging technologies will be crucial in basic, translational, and clinical research in the 21st century, and that the synthetic chemistry required to reliably produce imaging probes lies at the heart of research within imaging technologies. To this end, the IPDC has recruited the equipment and expertise to concurrently synthesize multiple types of imaging probes for bioscientists with diverse research interests, encompassing all imaging modalities, including optical, radionuclide, ultrasound, and magnetic resonance. The IPDC embodies an exciting new approach to apply and combine chemistry and imaging sciences toward specific problems in biology and medical sciences, and will be a truly interdisciplinary effort aimed at maximizing returns from the revolutionary new discoveries being described in modern imaging. A significant part of the IPDC will also be directed, independently, to the discovery of new imaging approaches and compositions. The IPDC houses scientific staff, mostly chemists, who have interests and expertise in one or more aspects of molecular imaging. The IPDC is generating known and novel imaging probes for targeting receptors, cells, and tissues, and for preclinical in vivo evaluations by its intramural collaborators. Many such interesting agents have been described in the scientific literature, but are often not explored further due to lack of a reliable supply of reagent. One aspect of the IPDC''s mission is to rectify this situation. IPDC-supplied reagents will not be limited to one imaging modality, but will include the flexible application of diverse technologies. Also, the IPDC will seek to develop novel state-of-the-art imaging probes in collaboration with biological and biomedical intramural scientists who can provide or suggest suitable targeting agent/receptor pairs. The Imaging Probe Development Center (IPDC) was initiated in the incubator space of the Common Fund and has transitioned to the intramural program of the National Heart, Lung, and Blood Institute.

Proper citation: Imaging Probe Development Center (IPDC) (RRID:SCR_006744) Copy   

•   Source: SciCrunch Registry

http://www.bioinsilico.org/cgi-bin/CAPSDB/staticHTML/home

It is a structural classification of helix-cappings or caps compiled from protein structures. Caps extracted from protein structures have been structurally classified based on geometry and conformation and organized in a tree-like hierarchical classification where the different levels correspond to different properties of the caps. CASP-DB is fully browsable and searchable and is regularly updated. The regions of the polypeptide chain immediately preceding or following a helix are known as Nt- and Ct cappings, respectively. Cappings play a central role stabilizing helices due to lack of intrahelical hydrogen bonds in the first and last turn. Sequence patterns of amino acid type preferences have been derived for cappings but the structural motifs associated to them are still unclassified. CAPS-DB is a database of clusters of structural patterns of different capping types. The clustering algorithm is based in the geometry and the space conformation of these regions. CAPS-DB is a relational database that allows the user to search, browse, inspect and retrieve structural data associated to cappings. The contents of CAPS-DB might be of interest to a wide range of scientist covering different areas such as protein design and engineering, structural biology and bioinformatics. CapsDB v4.0 * PDB structures: 4591 * Number of clusters: 859 * Number of caps: 31452

Proper citation: CAPS Database (RRID:SCR_006862) Copy   

•   Source: SciCrunch Registry

http://scop.mrc-lmb.cam.ac.uk/scop/

The Structural Classification of Proteins (SCOP) database is a comprehensive ordering of all proteins of known structure, according to their evolutionary and structural relationships. Protein domains in SCOP are hierarchically classified into families, superfamilies, folds and classes. The continual accumulation of sequence and structural data allows more rigorous analysis and provides important information for understanding the protein world and its evolutionary repertoire. SCOP participates in a project that aims to rationalize and integrate the data on proteins held in several sequence and structure databases. As part of this project, starting with release 1.63, we have initiated a refinement of the SCOP classification, which introduces a number of changes mostly at the levels below superfamily. The pending SCOP reclassification will be carried out gradually through a number of future releases. In addition to the expanded set of static links to external resources, available at the level of domain entries, we have started modernization of the interface capabilities of SCOP allowing more dynamic links with other databases.

Proper citation: SCOP: Structural Classification of Proteins (RRID:SCR_007039) Copy   

•   Source: SciCrunch Registry

http://chemistry.st-andrews.ac.uk/staff/jbom/group/databases.html

It is a publicly available web-based database that aims to provide further understanding of protein-ligand interactions. It''s a resource containing biomolecular data, including binding energies, Tanimoto ligand similarity scores and protein sequence similarities of protein-ligand complexes. The PLD contains biomolecular data including calculated binding energies, Tanimoto ligand similarity scores and protein percentage sequence similarities. The database has potential for application as a tool in molecular design.

Proper citation: Protein Ligand Database (RRID:SCR_006980) Copy   

•   Source: SciCrunch Registry

http://www.physionet.org/physiobank/database/gaitndd/

Database of records from patients with Parkinson's disease (n = 15), Huntington's disease (n = 20), or amyotrophic lateral sclerosis (n = 13). Records from 16 healthy control subjects are also included here. The raw data were obtained using force-sensitive resistors, with the output roughly proportional to the force under the foot. Stride-to-stride measures of footfall contact times were derived from these signals.

Proper citation: Gait Dynamics in Neuro-Degenerative Disease Data Base (RRID:SCR_006979) Copy   

•   Source: SciCrunch Registry

http://ekhidna.biocenter.helsinki.fi/dali/start

Resource out of service. Documented on May, 5th, 2021.The Dali Database is based on all-against-all 3D structure comparison of protein structures in the Protein Data Bank (PDB). The structural neighborhoods and alignments are automatically maintained and regularly updated using the Dali search engine. The Dali Database contains structural alignments of PDB90 versus the full PDB using DaliLite. The data can be viewed interactively here, or downloaded in its entirety Users may search by PDB identifier or keyword.

Proper citation: Dali database (RRID:SCR_006974) Copy   

•   Source: SciCrunch Registry

http://zork.wustl.edu/nida/neurosnp.html

The goal of this project is to aid genetic association studies of addiction by creating a resource of biologically relevant genes, pathways and single nucleotide polymorphisms (SNPs). The primary users of the NeuroSNP resource are investigators conducting genome-wide association studies (GWASs) of addiction-related phenotypes. NeuroSNP will allow investigators to identify biologically relevant genes for addiction based on curated expert knowledge, and assess the coverage of these genes provided by commercial SNP microarrays. If investigators wish to ensure the coverage of certain addiction-related genes is optimal, NeuroSNP provides a mechanism for supplementation. While commercial SNP microarrays offer affordable and comprehensive coverage of the human genome, some diseases have biologically relevant genomic regions that may require additional coverage. Addiction, for example, is believed to be influenced by complex interactions involving several genes and pathways. NIDA has assembled a number of investigators specializing in fields such as genetics, pharmacogenetics, bioinformatics and neurobiology through a Request for Information. These investigators have pooled their expert knowledge to produce a database of addiction-related genes and SNPs. Commercial SNP microarrays, such as those offered by Affymetrix and Illumina, are then analyzed to determine how well certain addiction-related genes are covered. When the coverage is less than optimal, a SNP prioritization scheme is used to supplement the commercial array with the most biologically informative markers. For example, SNPs in coding regions, promoters, and evolutionary conserved regions are selected first.

Proper citation: NeuroSNP Project (RRID:SCR_007029) Copy   

•   Source: SciCrunch Registry

https://sites.google.com/site/bipolardatabase/

Database of 141 studies which have investigated brain structure (using MRI and CT scans) in patients with bipolar disorder compared to a control group. Ninety-eight studies and 47 brain structures are included in the meta-analysis. The database and meta-analysis are contained in an Excel spreadsheet file which may be freely downloaded from this website.

Proper citation: Bipolar Disorder Neuroimaging Database (RRID:SCR_007025) Copy   

•   Source: SciCrunch Registry

http://ipu.ac.in/

Proper citation: Guru Gobind Singh Indraprastha University; Delhi; India (RRID:SCR_011260) Copy   

•   Source: SciCrunch Registry

http://medicine.uab.edu/

Proper citation: University of Alabama at Birmingham School of Medicine; Alabama; USA (RRID:SCR_010293) Copy   

•   Source: SciCrunch Registry

http://www.irbbarcelona.org/index.php/en

Institute for biomedical research in Barcelona, Spain.

Proper citation: Institute for Research in Biomedicine; Barcelona; Spain (RRID:SCR_011301) Copy   

•   Source: SciCrunch Registry

http://www.jhsph.edu/

Proper citation: Johns Hopkins Bloomberg School of Public Health; Maryland; USA (RRID:SCR_010222) Copy   

•   Source: SciCrunch Registry

http://www.huji.ac.il/huji/eng/

Proper citation: Hebrew University of Jerusalem; Jerusalem; Israel (RRID:SCR_011278) Copy   

•   Source: SciCrunch Registry

http://www.uni-frankfurt.de/en?locale=en

Proper citation: Goethe University Frankfurt am Main; Hessen; Germany (RRID:SCR_011240) Copy   

•   Source: SciCrunch Registry

http://www.ewha.ac.kr/english/

Proper citation: Ewha Womans University; Seoul; South Korea (RRID:SCR_011220) Copy   

•   Source: SciCrunch Registry

http://www.ucm.es/centros/webs/en/

Proper citation: Complutense University of Madrid; Madrid; Spain (RRID:SCR_011166) Copy   

•   Source: SciCrunch Registry

http://www.etsu.edu/

Proper citation: East Tennessee State University; Tennessee; USA (RRID:SCR_011200) Copy   

•   Source: SciCrunch Registry

http://med.emory.edu/

Emory University School of Medicine is graduate medical school of Emory University and component of Emory’s Robert W. Woodruff Health Sciences Center.

Proper citation: Emory University School of Medicine; Atlanta; Georgia; USA (RRID:SCR_011206) Copy   

•   Source: SciCrunch Registry

http://www.elte.hu/en

Proper citation: Eotvos Lorand University; Budapest; Hungary (RRID:SCR_011208) Copy   

•   Source: SciCrunch Registry