Pesquisa | BVS Integralidade em Saúde

1.

BCR::ABL1 Kinase N-lobe Mutants Confer Moderate to High Degrees of Resistance to Asciminib.

Leyte-Vidal, Ariel; Garrido Ruiz, Diego; DeFilippis, RosaAnna; Leske, Inga B; Rea, Delphine; Phan, Stacey; Miller, Kaeli B; Hu, Feifei; Mase, Anjeli; Shan, Yibing; Hantschel, Oliver; Jacobson, Matthew P; Shah, Neil P.

Blood ; 2024 04 21.

Artigo em Inglês | MEDLINE | ID: mdl-38643492

2.

Targeting the SH2-kinase interface in Bcr-Abl inhibits leukemogenesis.

Grebien, Florian; Hantschel, Oliver; Wojcik, John; Kaupe, Ines; Kovacic, Boris; Wyrzucki, Arkadiusz M; Gish, Gerald D; Cerny-Reiterer, Sabine; Koide, Akiko; Beug, Hartmut; Pawson, Tony; Valent, Peter; Koide, Shohei; Superti-Furga, Giulio.

Cell ; 147(2): 306-19, 2011 Oct 14.

Artigo em Inglês | MEDLINE | ID: mdl-22000011

3.

Structural coupling of SH2-kinase domains links Fes and Abl substrate recognition and kinase activation.

Filippakopoulos, Panagis; Kofler, Michael; Hantschel, Oliver; Gish, Gerald D; Grebien, Florian; Salah, Eidarus; Neudecker, Philipp; Kay, Lewis E; Turk, Benjamin E; Superti-Furga, Giulio; Pawson, Tony; Knapp, Stefan.

Cell ; 134(5): 793-803, 2008 Sep 05.

Artigo em Inglês | MEDLINE | ID: mdl-18775312

4.

The druggability of SH2 domains unmasked.

Hantschel, Oliver.

Nat Chem Biol ; 20(3): 271-272, 2024 Mar.

Artigo em Inglês | MEDLINE | ID: mdl-38361089

5.

Crizotinib acts as ABL1 inhibitor combining ATP-binding with allosteric inhibition and is active against native BCR-ABL1 and its resistance and compound mutants BCR-ABL1^T315I and BCR-ABL1^T315I-E255K.

Mian, Afsar Ali; Haberbosch, Isabella; Khamaisie, Hazem; Agbarya, Abed; Pietsch, Larissa; Eshel, Elizabeh; Najib, Dally; Chiriches, Claudia; Ottmann, Oliver Gerhard; Hantschel, Oliver; Biondi, Ricardo M; Ruthardt, Martin; Mahajna, Jamal.

Ann Hematol ; 100(8): 2023-2029, 2021 Aug.

Artigo em Inglês | MEDLINE | ID: mdl-34110462

6.

Single-molecule kinetic analysis of HP1-chromatin binding reveals a dynamic network of histone modification and DNA interactions.

Bryan, Louise C; Weilandt, Daniel R; Bachmann, Andreas L; Kilic, Sinan; Lechner, Carolin C; Odermatt, Pascal D; Fantner, Georg E; Georgeon, Sandrine; Hantschel, Oliver; Hatzimanikatis, Vassily; Fierz, Beat.

Nucleic Acids Res ; 45(18): 10504-10517, 2017 Oct 13.

Artigo em Inglês | MEDLINE | ID: mdl-28985346

7.

BioSITe: A Method for Direct Detection and Quantitation of Site-Specific Biotinylation.

Kim, Dae In; Cutler, Jevon A; Na, Chan Hyun; Reckel, Sina; Renuse, Santosh; Madugundu, Anil K; Tahir, Raiha; Goldschmidt, Hana L; Reddy, Karen L; Huganir, Richard L; Wu, Xinyan; Zachara, Natasha E; Hantschel, Oliver; Pandey, Akhilesh.

J Proteome Res ; 17(2): 759-769, 2018 02 02.

Artigo em Inglês | MEDLINE | ID: mdl-29249144

8.

ATP Site Ligands Determine the Assembly State of the Abelson Kinase Regulatory Core via the Activation Loop Conformation.

Sonti, Rajesh; Hertel-Hering, Ines; Lamontanara, Allan Joaquim; Hantschel, Oliver; Grzesiek, Stephan.

J Am Chem Soc ; 140(5): 1863-1869, 2018 02 07.

Artigo em Inglês | MEDLINE | ID: mdl-29319304

9.

Normal ABL1 is a tumor suppressor and therapeutic target in human and mouse leukemias expressing oncogenic ABL1 kinases.

Dasgupta, Yashodhara; Koptyra, Mateusz; Hoser, Grazyna; Kantekure, Kanchan; Roy, Darshan; Gornicka, Barbara; Nieborowska-Skorska, Margaret; Bolton-Gillespie, Elisabeth; Cerny-Reiterer, Sabine; Müschen, Markus; Valent, Peter; Wasik, Mariusz A; Richardson, Christine; Hantschel, Oliver; van der Kuip, Heiko; Stoklosa, Tomasz; Skorski, Tomasz.

Blood ; 127(17): 2131-43, 2016 04 28.

Artigo em Inglês | MEDLINE | ID: mdl-26864341

10.

Allosteric Inhibition of Bcr-Abl Kinase by High Affinity Monobody Inhibitors Directed to the Src Homology 2 (SH2)-Kinase Interface.

Wojcik, John; Lamontanara, Allan Joaquim; Grabe, Grzegorz; Koide, Akiko; Akin, Louesa; Gerig, Barbara; Hantschel, Oliver; Koide, Shohei.

J Biol Chem ; 291(16): 8836-47, 2016 Apr 15.

Artigo em Inglês | MEDLINE | ID: mdl-26912659

11.

CDK6 degradation hits Ph+ ALL hard.

Hantschel, Oliver.

Blood ; 135(18): 1512-1514, 2020 04 30.

Artigo em Inglês | MEDLINE | ID: mdl-32353124

12.

Targeting BCR-ABL and JAK2 in Ph+ ALL.

Hantschel, Oliver.

Blood ; 125(9): 1362-3, 2015 Feb 26.

Artigo em Inglês | MEDLINE | ID: mdl-25721043

13.

c-Abl phosphorylates α-synuclein and regulates its degradation: implication for α-synuclein clearance and contribution to the pathogenesis of Parkinson's disease.

Mahul-Mellier, Anne-Laure; Fauvet, Bruno; Gysbers, Amanda; Dikiy, Igor; Oueslati, Abid; Georgeon, Sandrine; Lamontanara, Allan J; Bisquertt, Alejandro; Eliezer, David; Masliah, Eliezer; Halliday, Glenda; Hantschel, Oliver; Lashuel, Hilal A.

Hum Mol Genet ; 23(11): 2858-79, 2014 Jun 01.

Artigo em Inglês | MEDLINE | ID: mdl-24412932

14.

Crystal structure of an SH2-kinase construct of c-Abl and effect of the SH2 domain on kinase activity.

Lorenz, Sonja; Deng, Patricia; Hantschel, Oliver; Superti-Furga, Giulio; Kuriyan, John.

Biochem J ; 468(2): 283-91, 2015 Jun 01.

Artigo em Inglês | MEDLINE | ID: mdl-25779001

15.

Dissection of the BCR-ABL signaling network using highly specific monobody inhibitors to the SHP2 SH2 domains.

Sha, Fern; Gencer, Emel Basak; Georgeon, Sandrine; Koide, Akiko; Yasui, Norihisa; Koide, Shohei; Hantschel, Oliver.

Proc Natl Acad Sci U S A ; 110(37): 14924-9, 2013 Sep 10.

Artigo em Inglês | MEDLINE | ID: mdl-23980151

16.

Mechanisms of resistance to BCR-ABL and other kinase inhibitors.

Lamontanara, Allan Joaquim; Gencer, Emel Basak; Kuzyk, Orest; Hantschel, Oliver.

Biochim Biophys Acta ; 1834(7): 1449-59, 2013 Jul.

Artigo em Inglês | MEDLINE | ID: mdl-23277196

17.

NUP214-ABL1-mediated cell proliferation in T-cell acute lymphoblastic leukemia is dependent on the LCK kinase and various interacting proteins.

De Keersmaecker, Kim; Porcu, Michaël; Cox, Luk; Girardi, Tiziana; Vandepoel, Roel; de Beeck, Joyce Op; Gielen, Olga; Mentens, Nicole; Bennett, Keiryn L; Hantschel, Oliver.

Haematologica ; 99(1): 85-93, 2014 Jan.

Artigo em Inglês | MEDLINE | ID: mdl-23872305

18.

BCR-ABL uncouples canonical JAK2-STAT5 signaling in chronic myeloid leukemia.

Hantschel, Oliver; Warsch, Wolfgang; Eckelhart, Eva; Kaupe, Ines; Grebien, Florian; Wagner, Kay-Uwe; Superti-Furga, Giulio; Sexl, Veronika.

Nat Chem Biol ; 8(3): 285-93, 2012 Jan 29.

Artigo em Inglês | MEDLINE | ID: mdl-22286129

19.

Improving the pharmacokinetics, biodistribution and plasma stability of monobodies.

Dinh-Fricke, Adrian Valentin; Hantschel, Oliver.

Front Pharmacol ; 152024 Apr 04.

Artigo em Inglês | MEDLINE | ID: mdl-38617793

20.

BCR-ABL1 compound mutants display differential and dose-dependent responses to ponatinib.

Byrgazov, Konstantin; Lucini, Chantal Blanche; Valent, Peter; Hantschel, Oliver; Lion, Thomas.

Haematologica ; 103(1): e10-e12, 2018 01.

Artigo em Inglês | MEDLINE | ID: mdl-28983061

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BCR::ABL1 Kinase N-lobe Mutants Confer Moderate to High Degrees of Resistance to Asciminib.

Targeting the SH2-kinase interface in Bcr-Abl inhibits leukemogenesis.

Structural coupling of SH2-kinase domains links Fes and Abl substrate recognition and kinase activation.

The druggability of SH2 domains unmasked.

Crizotinib acts as ABL1 inhibitor combining ATP-binding with allosteric inhibition and is active against native BCR-ABL1 and its resistance and compound mutants BCR-ABL1^T315I and BCR-ABL1^T315I-E255K.

Single-molecule kinetic analysis of HP1-chromatin binding reveals a dynamic network of histone modification and DNA interactions.

BioSITe: A Method for Direct Detection and Quantitation of Site-Specific Biotinylation.

ATP Site Ligands Determine the Assembly State of the Abelson Kinase Regulatory Core via the Activation Loop Conformation.

Normal ABL1 is a tumor suppressor and therapeutic target in human and mouse leukemias expressing oncogenic ABL1 kinases.

Allosteric Inhibition of Bcr-Abl Kinase by High Affinity Monobody Inhibitors Directed to the Src Homology 2 (SH2)-Kinase Interface.

CDK6 degradation hits Ph+ ALL hard.

Targeting BCR-ABL and JAK2 in Ph+ ALL.

c-Abl phosphorylates α-synuclein and regulates its degradation: implication for α-synuclein clearance and contribution to the pathogenesis of Parkinson's disease.

Crystal structure of an SH2-kinase construct of c-Abl and effect of the SH2 domain on kinase activity.

Dissection of the BCR-ABL signaling network using highly specific monobody inhibitors to the SHP2 SH2 domains.

Mechanisms of resistance to BCR-ABL and other kinase inhibitors.

NUP214-ABL1-mediated cell proliferation in T-cell acute lymphoblastic leukemia is dependent on the LCK kinase and various interacting proteins.

BCR-ABL uncouples canonical JAK2-STAT5 signaling in chronic myeloid leukemia.

Improving the pharmacokinetics, biodistribution and plasma stability of monobodies.

BCR-ABL1 compound mutants display differential and dose-dependent responses to ponatinib.