LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 10 of total 33

Search options

  1. Article ; Online: Signal transduction: RABGEF1 fingers RAS for ubiquitination.

    Colicelli, John

    Current biology : CB

    2010  Volume 20, Issue 15, Page(s) R630–2

    Abstract: RAS proteins conduct signaling from surface receptors to cytoplasmic effectors, and RAS gain-of-function mutations are pervasive in cancer. A new mechanism for RAS signal attenuation with implications for receptor trafficking has been uncovered. ...

    Abstract RAS proteins conduct signaling from surface receptors to cytoplasmic effectors, and RAS gain-of-function mutations are pervasive in cancer. A new mechanism for RAS signal attenuation with implications for receptor trafficking has been uncovered.
    MeSH term(s) Animals ; Endosomes/metabolism ; Guanine Nucleotide Exchange Factors/genetics ; Guanine Nucleotide Exchange Factors/metabolism ; Humans ; Signal Transduction ; Ubiquitination ; ras Proteins/genetics ; ras Proteins/metabolism
    Chemical Substances Guanine Nucleotide Exchange Factors ; RABGEF1 protein, human ; ras Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2010-06-04
    Publishing country England
    Document type Comment ; Journal Article
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/j.cub.2010.06.019
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 3208: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  2. Article ; Online: ABL tyrosine kinases: evolution of function, regulation, and specificity.

    Colicelli, John

    Science signaling

    2010  Volume 3, Issue 139, Page(s) re6

    Abstract: ABL-family proteins comprise one of the best conserved branches of the tyrosine kinases. Each ABL protein contains an SH3-SH2-TK (Src homology 3-Src homology 2-tyrosine kinase) domain cassette, which confers autoregulated kinase activity and is common ... ...

    Abstract ABL-family proteins comprise one of the best conserved branches of the tyrosine kinases. Each ABL protein contains an SH3-SH2-TK (Src homology 3-Src homology 2-tyrosine kinase) domain cassette, which confers autoregulated kinase activity and is common among nonreceptor tyrosine kinases. This cassette is coupled to an actin-binding and -bundling domain, which makes ABL proteins capable of connecting phosphoregulation with actin-filament reorganization. Two vertebrate paralogs, ABL1 and ABL2, have evolved to perform specialized functions. ABL1 includes nuclear localization signals and a DNA binding domain through which it mediates DNA damage-repair functions, whereas ABL2 has additional binding capacity for actin and for microtubules to enhance its cytoskeletal remodeling functions. Several types of posttranslational modifications control ABL catalytic activity, subcellular localization, and stability, with consequences for both cytoplasmic and nuclear ABL functions. Binding partners provide additional regulation of ABL catalytic activity, substrate specificity, and downstream signaling. Information on ABL regulatory mechanisms is being mined to provide new therapeutic strategies against hematopoietic malignancies caused by BCR-ABL1 and related leukemogenic proteins.
    MeSH term(s) Actins/genetics ; Actins/metabolism ; Animals ; DNA Damage/physiology ; DNA Repair/physiology ; Evolution, Molecular ; Fusion Proteins, bcr-abl/genetics ; Fusion Proteins, bcr-abl/metabolism ; Hematologic Neoplasms/genetics ; Hematologic Neoplasms/metabolism ; Hematologic Neoplasms/therapy ; Humans ; Microtubules/genetics ; Microtubules/metabolism ; Nuclear Localization Signals/genetics ; Nuclear Localization Signals/metabolism ; Protein Binding/physiology ; Protein Processing, Post-Translational/physiology ; Protein Transport/physiology ; Proto-Oncogene Proteins c-abl/genetics ; Proto-Oncogene Proteins c-abl/metabolism ; src Homology Domains
    Chemical Substances Actins ; Nuclear Localization Signals ; Fusion Proteins, bcr-abl (EC 2.7.10.2) ; Proto-Oncogene Proteins c-abl (EC 2.7.10.2)
    Language English
    Publishing date 2010-09-14
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 2417226-1
    ISSN 1937-9145 ; 1945-0877
    ISSN (online) 1937-9145
    ISSN 1945-0877
    DOI 10.1126/scisignal.3139re6
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  3. Article ; Online: Human RAS superfamily proteins and related GTPases.

    Colicelli, John

    Science's STKE : signal transduction knowledge environment

    2004  Volume 2004, Issue 250, Page(s) RE13

    Abstract: The tumor oncoproteins HRAS, KRAS, and NRAS are the founding members of a larger family of at least 35 related human proteins. Using a somewhat broader definition of sequence similarity reveals a more extended superfamily of more than 170 RAS-related ... ...

    Abstract The tumor oncoproteins HRAS, KRAS, and NRAS are the founding members of a larger family of at least 35 related human proteins. Using a somewhat broader definition of sequence similarity reveals a more extended superfamily of more than 170 RAS-related proteins. The RAS superfamily of GTP (guanosine triphosphate) hydrolysis-coupled signal transduction relay proteins can be subclassified into RAS, RHO, RAB, and ARF families, as well as the closely related Galpha family. The members of each family can, in turn, be arranged into evolutionarily conserved branches. These groupings reflect structural, biochemical, and functional conservation. Recent findings have provided insights into the signaling characteristics of representative members of most RAS superfamily branches. The analysis presented here may serve as a guide for predicting the function of numerous uncharacterized superfamily members. Also described are guanosine triphosphatases (GTPases) distinct from members of the RAS superfamily. These related proteins employ GTP binding and GTPase domains in diverse structural contexts, expanding the scope of their function in humans.
    MeSH term(s) Amino Acid Sequence/genetics ; Animals ; GTP Phosphohydrolases/genetics ; Humans ; Molecular Sequence Data ; Proto-Oncogene Proteins p21(ras)/genetics ; Sequence Alignment
    Chemical Substances GTP Phosphohydrolases (EC 3.6.1.-) ; HRAS protein, human (EC 3.6.5.2) ; Proto-Oncogene Proteins p21(ras) (EC 3.6.5.2)
    Language English
    Publishing date 2004-09-07
    Publishing country United States
    Document type Journal Article ; Review
    ISSN 1525-8882
    ISSN (online) 1525-8882
    DOI 10.1126/stke.2502004re13
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  4. Article: RIN1 regulates cell migration through RAB5 GTPases and ABL tyrosine kinases.

    Balaji, Kavitha / Colicelli, John

    Communicative & integrative biology

    2013  Volume 6, Issue 5, Page(s) e25421

    Abstract: Stimulation of a receptor tyrosine kinase (RTK), such as EGFR, leads to RAS activation followed by RIN1 activation. RIN1, in turn, activates RAB5 family GTPases, as well as ABL tyrosine kinases. As expected, RIN1 expression directly correlates with RAB5- ... ...

    Abstract Stimulation of a receptor tyrosine kinase (RTK), such as EGFR, leads to RAS activation followed by RIN1 activation. RIN1, in turn, activates RAB5 family GTPases, as well as ABL tyrosine kinases. As expected, RIN1 expression directly correlates with RAB5-mediated EGFR endocytosis. We previously showed that normal receptor endocytosis and internalized EGFR fate also depend on the ability of RIN1 to concomitantly activate ABL tyrosine kinases, consistent with the established role of ABL kinases in cytoskeleton remodeling and the growing evidence that such remodeling plays a role in endocytic processes. Here we report that growth factor-directed cell migration, a physiological process that involves receptor endocytosis and actin remodeling, also requires the ability of RIN1 to coordinate RAB5 GTPase and ABL tyrosine kinase pathways.
    Language English
    Publishing date 2013-06-25
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2451097-X
    ISSN 1942-0889
    ISSN 1942-0889
    DOI 10.4161/cib.25421
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  5. Article ; Online: The RAB5-GEF Function of RIN1 Regulates Multiple Steps During Listeria monocytogenes Infection.

    Balaji, Kavitha / French, Christopher T / Miller, Jeff F / Colicelli, John

    Traffic (Copenhagen, Denmark)

    2015  Volume 16, Issue 7, Page(s) 796

    Language English
    Publishing date 2015-07
    Publishing country England
    Document type Published Erratum
    ZDB-ID 1483852-7
    ISSN 1600-0854 ; 1398-9219
    ISSN (online) 1600-0854
    ISSN 1398-9219
    DOI 10.1111/tra.12268
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 5634: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  6. Article ; Online: The RAB5-GEF function of RIN1 regulates multiple steps during Listeria monocytogenes infection.

    Balaji, Kavitha / French, Christopher T / Miller, Jeff F / Colicelli, John

    Traffic (Copenhagen, Denmark)

    2014  Volume 15, Issue 11, Page(s) 1206–1218

    Abstract: Listeria monocytogenes is a food-borne pathogenic bacterium that invades intestinal epithelial cells through a phagocytic pathway that relies on the activation of host cell RAB5 GTPases. Listeria monocytogenes must subsequently inhibit RAB5, however, in ... ...

    Abstract Listeria monocytogenes is a food-borne pathogenic bacterium that invades intestinal epithelial cells through a phagocytic pathway that relies on the activation of host cell RAB5 GTPases. Listeria monocytogenes must subsequently inhibit RAB5, however, in order to escape lysosome-mediated destruction. Relatively little is known about upstream RAB5 regulators during L. monocytogenes entry and phagosome escape processes in epithelial cells. Here we identify RIN1, a RAS effector and RAB5-directed guanine nucleotide exchange factor (GEF), as a host cell factor in L. monocytogenes infection. RIN1 is rapidly engaged following L. monocytogenes infection and is required for efficient invasion of intestinal epithelial cells. RIN1-mediated RAB5 activation later facilitates the fusion of phagosomes with lysosomes, promoting clearance of bacteria from the host cell. These results suggest that RIN1 is a host cell regulator that performs counterbalancing functions during early and late stages of L. monocytogenes infection, ultimately favoring pathogen clearance.
    MeSH term(s) Animals ; Cell Line ; Epithelial Cells/metabolism ; Epithelial Cells/microbiology ; HeLa Cells ; Humans ; Intracellular Signaling Peptides and Proteins/genetics ; Intracellular Signaling Peptides and Proteins/metabolism ; Listeria monocytogenes/pathogenicity ; Lysosomes ; Phagocytosis ; Phagosomes/metabolism ; Rats ; rab5 GTP-Binding Proteins/metabolism ; ras Guanine Nucleotide Exchange Factors/metabolism
    Chemical Substances Intracellular Signaling Peptides and Proteins ; RIN1 protein, human ; ras Guanine Nucleotide Exchange Factors ; rab5 GTP-Binding Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2014-09-04
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 1483852-7
    ISSN 1600-0854 ; 1398-9219
    ISSN (online) 1600-0854
    ISSN 1398-9219
    DOI 10.1111/tra.12204
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 5634: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  7. Article: Expression, purification, crystallization and X-ray data collection for RAS and its mutants.

    Johnson, Christian W / Buhrman, Greg / Ting, Pamela Y / Colicelli, John / Mattos, Carla

    Data in brief

    2015  Volume 6, Page(s) 423–427

    Abstract: This article expands on crystal structure data for human H-RAS with mutations at position Y137, briefly described in a paper on the effects of phosphorylation of Y137 by ABL kinases (Tyrosine phosphorylation of RAS by ABL allosterically enhances effector ...

    Abstract This article expands on crystal structure data for human H-RAS with mutations at position Y137, briefly described in a paper on the effects of phosphorylation of Y137 by ABL kinases (Tyrosine phosphorylation of RAS by ABL allosterically enhances effector binding, published in the FASEB Journal [1]). The crystal structures of the Y137E mutant (phosphorylation mimic) and of the Y137F mutant (without the hydroxyl group where phosphorylation occurs) were deposited in the Protein Data Bank with PDB codes 4XVQ (H-RAS(Y137E)) and 4XVR (H-RAS(Y137F)). This article includes details for expression and purification of RAS and its mutants with no affinity tags, in vitro exchange of guanine nucleotides, protein crystallization, X-ray data collection and structure refinement.
    Language English
    Publishing date 2015-12-17
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 2786545-9
    ISSN 2352-3409
    ISSN 2352-3409
    DOI 10.1016/j.dib.2015.12.007
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  8. Article ; Online: RIN3 is a negative regulator of mast cell responses to SCF.

    Janson, Christine / Kasahara, Noriyuki / Prendergast, George C / Colicelli, John

    PloS one

    2012  Volume 7, Issue 11, Page(s) e49615

    Abstract: Stimulation of the receptor tyrosine kinase KIT by Stem Cell Factor (SCF) triggers activation of RAS and its downstream effectors. Proper KIT activation is essential for the maturation, survival and proliferation of mast cells. In addition, SCF ... ...

    Abstract Stimulation of the receptor tyrosine kinase KIT by Stem Cell Factor (SCF) triggers activation of RAS and its downstream effectors. Proper KIT activation is essential for the maturation, survival and proliferation of mast cells. In addition, SCF activation of KIT is critical for recruiting mast cells to sites of infection or injury, where they release a mix of pro-inflammatory substances. RIN3, a RAS effector and RAB5-directed guanine nucleotide exchange factor (GEF), is highly expressed and enriched in human mast cells. SCF treatment of mast cells increased the amount of GTP-bound RAB5, and the degree of RAB5 activation correlated with the expression level of RIN3. At the same time, SCF caused the dissociation of a pre-formed complex of RIN3 with BIN2, a membrane bending protein implicated in endocytosis. Silencing of RIN3 increased the rate of SCF-induced KIT internalization, while persistent RIN3 over-expression led to KIT down regulation. These observations strongly support a role for RIN3 in coordinating the early steps of KIT endocytosis. Importantly, RIN3 also functioned as an inhibitor of mast cell migration toward SCF. Finally, we demonstrate that elevated RIN3 levels sensitize mastocytosis cells to treatment with a KIT tyrosine kinase inhibitor, suggesting the value of a two-pronged inhibitor approach for this difficult to treat malignancy. These findings directly connect KIT activation with a mast cell-specific RAS effector that regulates the cellular response to SCF and provide new insight for the development of more effective mastocytosis treatments.
    MeSH term(s) Benzamides/pharmacology ; Carrier Proteins/metabolism ; Cell Movement ; Cell Proliferation ; Endocytosis ; Gene Expression Regulation ; Gene Silencing ; Guanine Nucleotide Exchange Factors/metabolism ; Humans ; Imatinib Mesylate ; Immunohistochemistry/methods ; Inflammation ; Lipopolysaccharide Receptors/biosynthesis ; Mast Cells/cytology ; Mastocytosis/pathology ; Piperazines/pharmacology ; Protein Structure, Tertiary ; Proto-Oncogene Proteins c-kit/metabolism ; Pyrimidines/pharmacology ; Stem Cell Factor/metabolism ; rab5 GTP-Binding Proteins/metabolism
    Chemical Substances Benzamides ; Carrier Proteins ; Guanine Nucleotide Exchange Factors ; Lipopolysaccharide Receptors ; Piperazines ; Pyrimidines ; RIN3 protein, human ; Stem Cell Factor ; Imatinib Mesylate (8A1O1M485B) ; Proto-Oncogene Proteins c-kit (EC 2.7.10.1) ; rab5 GTP-Binding Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2012-11-20
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0049615
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  9. Article ; Online: Expression, purification, crystallization and X-ray data collection for RAS and its mutants

    Christian W. Johnson / Greg Buhrman / Pamela Y. Ting / John Colicelli / Carla Mattos

    Data in Brief, Vol 6, Iss , Pp 423-

    2016  Volume 427

    Abstract: This article expands on crystal structure data for human H-RAS with mutations at position Y137, briefly described in a paper on the effects of phosphorylation of Y137 by ABL kinases (Tyrosine phosphorylation of RAS by ABL allosterically enhances effector ...

    Abstract This article expands on crystal structure data for human H-RAS with mutations at position Y137, briefly described in a paper on the effects of phosphorylation of Y137 by ABL kinases (Tyrosine phosphorylation of RAS by ABL allosterically enhances effector binding, published in the FASEB Journal [1]). The crystal structures of the Y137E mutant (phosphorylation mimic) and of the Y137F mutant (without the hydroxyl group where phosphorylation occurs) were deposited in the Protein Data Bank with PDB codes 4XVQ (H-RASY137E) and 4XVR (H-RASY137F). This article includes details for expression and purification of RAS and its mutants with no affinity tags, in vitro exchange of guanine nucleotides, protein crystallization, X-ray data collection and structure refinement. Keywords: RAS GTPase, Protein purification, Nucleotide exchange, X-ray crystal structures
    Keywords Computer applications to medicine. Medical informatics ; R858-859.7 ; Science (General) ; Q1-390
    Subject code 500
    Language English
    Publishing date 2016-03-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

    More links

    Kategorien

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  10. Article: Expression, purification, crystallization and X-ray data collection for RAS and its mutants

    Johnson, Christian W. / Buhrman, Greg / Ting, Pamela Y. / Colicelli, John / Mattos, Carla

    Data in Brief. 2016 Mar., v. 6

    2016  

    Abstract: This article expands on crystal structure data for human H-RAS with mutations at position Y137, briefly described in a paper on the effects of phosphorylation of Y137 by ABL kinases (Tyrosine phosphorylation of RAS by ABL allosterically enhances effector ...

    Abstract This article expands on crystal structure data for human H-RAS with mutations at position Y137, briefly described in a paper on the effects of phosphorylation of Y137 by ABL kinases (Tyrosine phosphorylation of RAS by ABL allosterically enhances effector binding, published in the FASEB Journal [1]). The crystal structures of the Y137E mutant (phosphorylation mimic) and of the Y137F mutant (without the hydroxyl group where phosphorylation occurs) were deposited in the Protein Data Bank with PDB codes 4XVQ (H-RASY¹³⁷ᴱ) and 4XVR (H-RASY¹³⁷F). This article includes details for expression and purification of RAS and its mutants with no affinity tags, in vitro exchange of guanine nucleotides, protein crystallization, X-ray data collection and structure refinement.
    Keywords X-radiation ; crystal structure ; crystallization ; data collection ; databases ; guanine nucleotides ; humans ; mutants ; phosphorylation ; phosphotransferases (kinases) ; tyrosine
    Language English
    Dates of publication 2016-03
    Size p. 423-427.
    Publishing place Elsevier Inc.
    Document type Article
    ZDB-ID 2786545-9
    ISSN 2352-3409
    ISSN 2352-3409
    DOI 10.1016/j.dib.2015.12.007
    Database NAL-Catalogue (AGRICOLA)

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

To top