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  1. Article ; Online: Multiple lineage switches in KMT2A rearranged infant leukemia, responsive to combination therapy with CPX-351 and inotuzumab.

    Sperlazza, Justin / Galeotti, Jonathan / Hucks, George / Alexander, Thomas B

    Pediatric blood & cancer

    2023  Volume 70, Issue 11, Page(s) e30645

    MeSH term(s) Infant ; Humans ; Cytarabine ; Leukemia ; Daunorubicin
    Chemical Substances CPX-351 ; Cytarabine (04079A1RDZ) ; Daunorubicin (ZS7284E0ZP)
    Language English
    Publishing date 2023-08-28
    Publishing country United States
    Document type Letter
    ZDB-ID 2131448-2
    ISSN 1545-5017 ; 1545-5009
    ISSN (online) 1545-5017
    ISSN 1545-5009
    DOI 10.1002/pbc.30645
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1131: Show issues Location:
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  2. Article ; Online: Depletion of the chromatin remodeler CHD4 sensitizes AML blasts to genotoxic agents and reduces tumor formation.

    Sperlazza, Justin / Rahmani, Mohamed / Beckta, Jason / Aust, Mandy / Hawkins, Elisa / Wang, Shou Zhen / Zu Zhu, Sheng / Podder, Shreya / Dumur, Catherine / Archer, Kellie / Grant, Steven / Ginder, Gordon D

    Blood

    2015  Volume 126, Issue 12, Page(s) 1462–1472

    Abstract: Chromodomain helicase DNA-binding protein 4 (CHD4) is an ATPase that alters the phasing of nucleosomes on DNA and has recently been implicated in DNA double-stranded break (DSB) repair. Here, we show that depletion of CHD4 in acute myeloid leukemia (AML) ...

    Abstract Chromodomain helicase DNA-binding protein 4 (CHD4) is an ATPase that alters the phasing of nucleosomes on DNA and has recently been implicated in DNA double-stranded break (DSB) repair. Here, we show that depletion of CHD4 in acute myeloid leukemia (AML) blasts induces a global relaxation of chromatin that renders cells more susceptible to DSB formation, while concurrently impeding their repair. Furthermore, CHD4 depletion renders AML blasts more sensitive both in vitro and in vivo to genotoxic agents used in clinical therapy: daunorubicin (DNR) and cytarabine (ara-C). Sensitization to DNR and ara-C is mediated in part by activation of the ataxia-telangiectasia mutated pathway, which is preliminarily activated by a Tip60-dependent mechanism in response to chromatin relaxation and further activated by genotoxic agent-induced DSBs. This sensitization preferentially affects AML cells, as CHD4 depletion in normal CD34(+) hematopoietic progenitors does not increase their susceptibility to DNR or ara-C. Unexpectedly, we found that CHD4 is necessary for maintaining the tumor-forming behavior of AML cells, as CHD4 depletion severely restricted the ability of AML cells to form xenografts in mice and colonies in soft agar. Taken together, these results provide evidence for CHD4 as a novel therapeutic target whose inhibition has the potential to enhance the effectiveness of genotoxic agents used in AML therapy.
    MeSH term(s) Animals ; Antibiotics, Antineoplastic/therapeutic use ; Antimetabolites, Antineoplastic/therapeutic use ; Autoantigens/genetics ; Cell Line, Tumor ; Cytarabine/therapeutic use ; DNA Breaks, Double-Stranded/drug effects ; Daunorubicin/therapeutic use ; Female ; Humans ; Leukemia, Myeloid, Acute/drug therapy ; Leukemia, Myeloid, Acute/genetics ; Leukemia, Myeloid, Acute/pathology ; Mi-2 Nucleosome Remodeling and Deacetylase Complex/genetics ; Mice, Inbred NOD ; Mice, SCID ; RNA Interference ; Tumor Cells, Cultured
    Chemical Substances Antibiotics, Antineoplastic ; Antimetabolites, Antineoplastic ; Autoantigens ; CHD4 protein, human ; Cytarabine (04079A1RDZ) ; Mi-2 Nucleosome Remodeling and Deacetylase Complex (EC 3.5.1.98) ; Daunorubicin (ZS7284E0ZP)
    Language English
    Publishing date 2015-08-11
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 80069-7
    ISSN 1528-0020 ; 0006-4971
    ISSN (online) 1528-0020
    ISSN 0006-4971
    DOI 10.1182/blood-2015-03-631606
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.MO 364: Show issues

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  3. Article ; Online: Crystal structure analysis reveals Pseudomonas PilY1 as an essential calcium-dependent regulator of bacterial surface motility.

    Orans, Jillian / Johnson, Michael D L / Coggan, Kimberly A / Sperlazza, Justin R / Heiniger, Ryan W / Wolfgang, Matthew C / Redinbo, Matthew R

    Proceedings of the National Academy of Sciences of the United States of America

    2009  Volume 107, Issue 3, Page(s) 1065–1070

    Abstract: Several bacterial pathogens require the "twitching" motility produced by filamentous type IV pili (T4P) to establish and maintain human infections. Two cytoplasmic ATPases function as an oscillatory motor that powers twitching motility via cycles of ... ...

    Abstract Several bacterial pathogens require the "twitching" motility produced by filamentous type IV pili (T4P) to establish and maintain human infections. Two cytoplasmic ATPases function as an oscillatory motor that powers twitching motility via cycles of pilus extension and retraction. The regulation of this motor, however, has remained a mystery. We present the 2.1 A resolution crystal structure of the Pseudomonas aeruginosa pilus-biogenesis factor PilY1, and identify a single site on this protein required for bacterial translocation. The structure reveals a modified beta-propeller fold and a distinct EF-hand-like calcium-binding site conserved in pathogens with retractile T4P. We show that preventing calcium binding by PilY1 using either an exogenous calcium chelator or mutation of a single residue disrupts Pseudomonas twitching motility by eliminating surface pili. In contrast, placing a lysine in this site to mimic the charge of a bound calcium interferes with motility in the opposite manner--by producing an abundance of nonfunctional surface pili. Our data indicate that calcium binding and release by the unique loop identified in the PilY1 crystal structure controls the opposing forces of pilus extension and retraction. Thus, PilY1 is an essential, calcium-dependent regulator of bacterial twitching motility.
    MeSH term(s) Amino Acid Sequence ; Calcium/physiology ; Crystallography, X-Ray ; Fimbriae Proteins/chemistry ; Models, Molecular ; Protein Conformation ; Pseudomonas aeruginosa/chemistry ; Pseudomonas aeruginosa/physiology
    Chemical Substances PilY1 protein, Pseudomonas aeruginosa ; Fimbriae Proteins (147680-16-8) ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2009-12-28
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.0911616107
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 1148: Show issues Location:
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  4. Article: Tumor infiltrating Foxp3+ regulatory T-cells are associated with recurrence in pathologic stage I NSCLC patients.

    Petersen, Rebecca P / Campa, Michael J / Sperlazza, Justin / Conlon, Debbi / Joshi, Mary-Beth / Harpole, David H / Patz, Edward F

    Cancer

    2006  Volume 107, Issue 12, Page(s) 2866–2872

    Abstract: Background: Early stage lung cancer has a variable prognosis, and there are currently no markers that predict which patients will recur. This study examined the relation between tumor-regulatory T (Treg) cells and total tumor-infiltrating T-cell ... ...

    Abstract Background: Early stage lung cancer has a variable prognosis, and there are currently no markers that predict which patients will recur. This study examined the relation between tumor-regulatory T (Treg) cells and total tumor-infiltrating T-cell lymphocytes (TIL) to determine whether they correlated with recurrence.
    Methods: The authors reviewed all patients in our tissue databank from 1996 to 2001 and identified 64 consecutive pathologic stage I non-small cell lung cancer (NSCLC) patients who had surgical resection and at least a 2.5 years disease-free follow-up or documented recurrence within 2 years. Immunohistochemical analyses were performed on paraffin-embedded lung cancer tissue and the relation between Treg cells, TIL, and disease-specific survival was determined. A risk index was devised deductively for various possible combinations of Treg cells and TIL.
    Results: Treg cells and TIL were detected in 33 of 64 (51%) and 53 of 64 (83%) patients, respectively. When data were analyzed by using a Treg/TIL Combination Risk Index, patients with high-risk and intermediate-risk indices had hazard ratios of 8.2 (P = .007) and 3.3 (P = .109), respectively.
    Conclusions: Patients with stage I NSCLC who have a higher proportion of tumor Treg cells relative to TIL had a significantly higher risk of recurrence. These data may be useful, particularly if combined with a panel of tumor markers, to suggest at the time of diagnosis which patients with seemingly early-stage NSCLC will relapse.
    MeSH term(s) CD3 Complex/analysis ; Carcinoma, Non-Small-Cell Lung/diagnosis ; Carcinoma, Non-Small-Cell Lung/immunology ; Carcinoma, Non-Small-Cell Lung/pathology ; Forkhead Transcription Factors/analysis ; Humans ; Lung Neoplasms/diagnosis ; Lung Neoplasms/immunology ; Lung Neoplasms/pathology ; Lymphocytes, Tumor-Infiltrating/chemistry ; Lymphocytes, Tumor-Infiltrating/immunology ; Neoplasm Recurrence, Local/diagnosis ; Neoplasm Recurrence, Local/immunology ; Neoplasm Recurrence, Local/pathology ; Neoplasm Staging ; Prognosis ; T-Lymphocytes, Regulatory/chemistry ; T-Lymphocytes, Regulatory/immunology
    Chemical Substances CD3 Complex ; FOXP3 protein, human ; Forkhead Transcription Factors
    Language English
    Publishing date 2006-12-15
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 1429-1
    ISSN 1097-0142 ; 0008-543X ; 1934-662X
    ISSN (online) 1097-0142
    ISSN 0008-543X ; 1934-662X
    DOI 10.1002/cncr.22282
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Crystal structure analysis reveals Pseudomonas PilY1 as an essential calcium-dependent regulator of bacterial surface motility

    Orans, Jillian / Johnson, Michael D.L / Coggan, Kimberly A / Sperlazza, Justin R / Heiniger, Ryan W / Wolfgang, Matthew C / Redinbo, Matthew R

    Proceedings of the National Academy of Sciences of the United States of America. 2010 Jan. 19, v. 107, no. 3

    2010  

    Abstract: Several bacterial pathogens require the "twitching" motility produced by filamentous type IV pili (T4P) to establish and maintain human infections. Two cytoplasmic ATPases function as an oscillatory motor that powers twitching motility via cycles of ... ...

    Abstract Several bacterial pathogens require the "twitching" motility produced by filamentous type IV pili (T4P) to establish and maintain human infections. Two cytoplasmic ATPases function as an oscillatory motor that powers twitching motility via cycles of pilus extension and retraction. The regulation of this motor, however, has remained a mystery. We present the 2.1 Å resolution crystal structure of the Pseudomonas aeruginosa pilus-biogenesis factor PilY1, and identify a single site on this protein required for bacterial translocation. The structure reveals a modified β-propeller fold and a distinct EF-hand-like calcium-binding site conserved in pathogens with retractile T4P. We show that preventing calcium binding by PilY1 using either an exogenous calcium chelator or mutation of a single residue disrupts Pseudomonas twitching motility by eliminating surface pili. In contrast, placing a lysine in this site to mimic the charge of a bound calcium interferes with motility in the opposite manner--by producing an abundance of nonfunctional surface pili. Our data indicate that calcium binding and release by the unique loop identified in the PilY1 crystal structure controls the opposing forces of pilus extension and retraction. Thus, PilY1 is an essential, calcium-dependent regulator of bacterial twitching motility.
    Keywords Pseudomonas aeruginosa ; adenosinetriphosphatase ; calcium ; chelating agents ; crystal structure ; fimbriae ; human diseases ; lysine ; mutation ; pathogens
    Language English
    Dates of publication 2010-0119
    Size p. 1065-1070.
    Publishing place National Academy of Sciences
    Document type Article
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.0911616107
    Database NAL-Catalogue (AGRICOLA)

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