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Kinesins in the Arabidopsis genome: a comparative analysis among eukaryotes.

BMC genomics

Reddy AS, Day IS.
PMID: 11472632
BMC Genomics. 2001;2:2. doi: 10.1186/1471-2164-2-2. Epub 2001 Jun 25.

BACKGROUND: Kinesins constitute a superfamily of microtubule motor proteins that are found in eukaryotic organisms. Members of the kinesin superfamily perform many diverse cellular functions such as transport of vesicles and organelles, spindle formation and elongation, chromosome segregation, microtubule...

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Reddy AS, Day IS. Kinesins in the Arabidopsis genome: a comparative analysis among eukaryotes. BMC Genomics. 2001;2:2doi: 10.1186/1471-2164-2-2.
Reddy, A. S., & Day, I. S. (2001). Kinesins in the Arabidopsis genome: a comparative analysis among eukaryotes. BMC genomics, 22. https://doi.org/10.1186/1471-2164-2-2
Reddy, A S, and Day, I S. "Kinesins in the Arabidopsis genome: a comparative analysis among eukaryotes." BMC genomics vol. 2 (2001): 2. doi: https://doi.org/10.1186/1471-2164-2-2
Reddy AS, Day IS. Kinesins in the Arabidopsis genome: a comparative analysis among eukaryotes. BMC Genomics. 2001;2:2. doi: 10.1186/1471-2164-2-2. Epub 2001 Jun 25. PMID: 11472632; PMCID: PMC35278.
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[Clinical characteristics of primary cancer of the lung].

Voprosy kliniki i lecheniia zlokachestvennykh novoobrazovanii

KNESIS SG.
PMID: 14457217
Vopr Klin Lecheniia Zlokachestvennykh Novoobraz. 1961;7:179-86.

No abstract available.

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KNESIS SG. [Clinical characteristics of primary cancer of the lung]. Vopr Klin Lecheniia Zlokachestvennykh Novoobraz. 1961;7:179-86
KNESIS, S. G. (1961). [Clinical characteristics of primary cancer of the lung]. Voprosy kliniki i lecheniia zlokachestvennykh novoobrazovanii, 7179-86.
KNESIS, S G. "[Clinical characteristics of primary cancer of the lung]." Voprosy kliniki i lecheniia zlokachestvennykh novoobrazovanii vol. 7 (1961): 179-86.
KNESIS SG. [Clinical characteristics of primary cancer of the lung]. Vopr Klin Lecheniia Zlokachestvennykh Novoobraz. 1961;7:179-86. Russian. PMID: 14457217.
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Kinesins in the spindle: an update.

Trends in cell biology

Epstein H, Scholey JM.
PMID: 14731508
Trends Cell Biol. 1992 Nov;2(11):315-8. doi: 10.1016/0962-8924(92)90171-i.

Eukaryotes contain a superfamily of microtubule-based motor proteins comprising kinesin and a number of related proteins that are thought to participate in various forms of intracellular motility, including cell division and organelle transport. The role of various members of...

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Epstein H, Scholey JM. Kinesins in the spindle: an update. Trends Cell Biol. 1992;2(11):315-8doi: 10.1016/0962-8924(92)90171-i.
Epstein, H., & Scholey, J. M. (1992). Kinesins in the spindle: an update. Trends in cell biology, 2(11), 315-8. https://doi.org/10.1016/0962-8924(92)90171-i
Epstein, H, and Scholey, J M. "Kinesins in the spindle: an update." Trends in cell biology vol. 2,11 (1992): 315-8. doi: https://doi.org/10.1016/0962-8924(92)90171-i
Epstein H, Scholey JM. Kinesins in the spindle: an update. Trends Cell Biol. 1992 Nov;2(11):315-8. doi: 10.1016/0962-8924(92)90171-i. PMID: 14731508.
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Kinesin-like proteins in the flagella of Chlamydomonas.

Trends in cell biology

Bernstein M, Rosenbaum JL.
PMID: 14731662
Trends Cell Biol. 1994 Jul;4(7):236-40. doi: 10.1016/0962-8924(94)90115-5.

The flagella of the biflagellate unicellular alga Chlamydomonas have long been known to contain the microtubule-dependent motor protein dynein, but recent findings indicate they also contain multiple members of the kinesin superfamily. Two of these kinesin-like proteins are restricted...

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Bernstein M, Rosenbaum JL. Kinesin-like proteins in the flagella of Chlamydomonas. Trends Cell Biol. 1994;4(7):236-40doi: 10.1016/0962-8924(94)90115-5.
Bernstein, M., & Rosenbaum, J. L. (1994). Kinesin-like proteins in the flagella of Chlamydomonas. Trends in cell biology, 4(7), 236-40. https://doi.org/10.1016/0962-8924(94)90115-5
Bernstein, M, and Rosenbaum, J L. "Kinesin-like proteins in the flagella of Chlamydomonas." Trends in cell biology vol. 4,7 (1994): 236-40. doi: https://doi.org/10.1016/0962-8924(94)90115-5
Bernstein M, Rosenbaum JL. Kinesin-like proteins in the flagella of Chlamydomonas. Trends Cell Biol. 1994 Jul;4(7):236-40. doi: 10.1016/0962-8924(94)90115-5. PMID: 14731662.
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Motoring down the highways of the cell.

Trends in cell biology

Trayer IP, John Smith K.
PMID: 17708957
Trends Cell Biol. 1997 Jul;7(7):259-63. doi: 10.1016/S0962-8924(97)01083-0.

All eukaryotic cells contain large numbers of motor proteins (kinesins, dyneins and myosins), each of which appears to carry out a specialized force-generating function within the cell. They are known to have roles in muscle contraction, ciliary movement, organelle...

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Trayer IP, John Smith K. Motoring down the highways of the cell. Trends Cell Biol. 1997;7(7):259-63doi: 10.1016/S0962-8924(97)01083-0.
Trayer, I. P., & John Smith, K. (1997). Motoring down the highways of the cell. Trends in cell biology, 7(7), 259-63. https://doi.org/10.1016/S0962-8924(97)01083-0
Trayer, I P, and John Smith, K. "Motoring down the highways of the cell." Trends in cell biology vol. 7,7 (1997): 259-63. doi: https://doi.org/10.1016/S0962-8924(97)01083-0
Trayer IP, John Smith K. Motoring down the highways of the cell. Trends Cell Biol. 1997 Jul;7(7):259-63. doi: 10.1016/S0962-8924(97)01083-0. PMID: 17708957.
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Small-molecule and mutational analysis of allosteric Eg5 inhibition by monastrol.

BMC chemical biology

Maliga Z, Mitchison TJ.
PMID: 16504166
BMC Chem Biol. 2006 Feb 27;6:2. doi: 10.1186/1472-6769-6-2.

BACKGROUND: A recent crystal structure of monastrol in a ternary complex with the kinesin Eg5 motor domain highlights a novel, induced-fit drug binding site at atomic resolution. Mutational obliteration of the monastrol binding site results in a monastrol-resistant, but...

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Maliga Z, Mitchison TJ. Small-molecule and mutational analysis of allosteric Eg5 inhibition by monastrol. BMC Chem Biol. 2006;6:2doi: 10.1186/1472-6769-6-2.
Maliga, Z., & Mitchison, T. J. (2006). Small-molecule and mutational analysis of allosteric Eg5 inhibition by monastrol. BMC chemical biology, 62. https://doi.org/10.1186/1472-6769-6-2
Maliga, Zoltan, and Mitchison, Timothy J. "Small-molecule and mutational analysis of allosteric Eg5 inhibition by monastrol." BMC chemical biology vol. 6 (2006): 2. doi: https://doi.org/10.1186/1472-6769-6-2
Maliga Z, Mitchison TJ. Small-molecule and mutational analysis of allosteric Eg5 inhibition by monastrol. BMC Chem Biol. 2006 Feb 27;6:2. doi: 10.1186/1472-6769-6-2. PMID: 16504166; PMCID: PMC1448180.
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The Arabidopsis cytoskeletal genome.

The arabidopsis book

Meagher RB, Fechheimer M.
PMID: 22303225
Arabidopsis Book. 2003;2:e0096. doi: 10.1199/tab.0096. Epub 2003 Sep 30.

In the past decade the first Arabidopsis genes encoding cytoskeletal proteins were identified. A few dozen genes in the actin and tubulin cytoskeletal systems have been characterized thoroughly, including gene families encoding actins, profilins, actin depolymerizing factors, α-tubulins, and...

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Meagher RB, Fechheimer M. The Arabidopsis cytoskeletal genome. Arabidopsis Book. 2003;2:e0096doi: 10.1199/tab.0096.
Meagher, R. B., & Fechheimer, M. (2003). The Arabidopsis cytoskeletal genome. The arabidopsis book, 2e0096. https://doi.org/10.1199/tab.0096
Meagher, Richard B, and Fechheimer, Marcus. "The Arabidopsis cytoskeletal genome." The arabidopsis book vol. 2 (2003): e0096. doi: https://doi.org/10.1199/tab.0096
Meagher RB, Fechheimer M. The Arabidopsis cytoskeletal genome. Arabidopsis Book. 2003;2:e0096. doi: 10.1199/tab.0096. Epub 2003 Sep 30. PMID: 22303225; PMCID: PMC3243305.
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[Further investigations on the resistance ofMedicago species toPseudopeziza medicaginis (Lib.) Sacc].

TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik

Schmiedeknecht M, Lesins K.
PMID: 24442268
Theor Appl Genet. 1968 May;38(5):188-94. doi: 10.1007/BF00935265.

Experimental infections of 44 species and varieties ofMedicago with the f. sp.medicaginis sativae andmedicaginis lupulinae fromPseudopeziza medicaginis and withP. meliloti have broadened the knowledge on resistance behavior of the genusMedicago and confirmed earlier results.

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Schmiedeknecht M, Lesins K. Weitere Untersuchungen zur Resistenz vonMedicago-arten gegenPseudopeziza medicaginis (Lib.) Sacc. [Further investigations on the resistance ofMedicago species toPseudopeziza medicaginis (Lib.) Sacc]. Theor Appl Genet. 1968;38(5):188-94doi: 10.1007/BF00935265.
Schmiedeknecht, M., & Lesins, K. (1968). Weitere Untersuchungen zur Resistenz vonMedicago-arten gegenPseudopeziza medicaginis (Lib.) Sacc. [Further investigations on the resistance ofMedicago species toPseudopeziza medicaginis (Lib.) Sacc]. TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik, 38(5), 188-94. https://doi.org/10.1007/BF00935265
Schmiedeknecht, M, and Lesins, K. "Weitere Untersuchungen zur Resistenz vonMedicago-arten gegenPseudopeziza medicaginis (Lib.) Sacc." [Further investigations on the resistance ofMedicago species toPseudopeziza medicaginis (Lib.) Sacc]. TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik vol. 38,5 (1968): 188-94. doi: https://doi.org/10.1007/BF00935265
Schmiedeknecht M, Lesins K. Weitere Untersuchungen zur Resistenz vonMedicago-arten gegenPseudopeziza medicaginis (Lib.) Sacc. [Further investigations on the resistance ofMedicago species toPseudopeziza medicaginis (Lib.) Sacc]. Theor Appl Genet. 1968 May;38(5):188-94. doi: 10.1007/BF00935265. German. PMID: 24442268.
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Evaluation of activity and combination strategies with the microtubule-targeting drug sagopilone in breast cancer cell lines.

Frontiers in oncology

Eschenbrenner J, Winsel S, Hammer S, Sommer A, Mittelstaedt K, Drosch M, Klar U, Sachse C, Hannus M, Seidel M, Weiss B, Merz C, Siemeister G, Hoffmann J.
PMID: 22649765
Front Oncol. 2011 Nov 16;1:44. doi: 10.3389/fonc.2011.00044. eCollection 2011.

Sagopilone, a fully synthetic epothilone, is a microtubule-stabilizing agent optimized for high in vitro and in vivo activity against a broad range of tumor models, including those resistant to paclitaxel and other systemic treatments. Sagopilone development is accompanied by...

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Eschenbrenner J, Winsel S, Hammer S, et al. Evaluation of activity and combination strategies with the microtubule-targeting drug sagopilone in breast cancer cell lines. Front Oncol. 2011;1:44doi: 10.3389/fonc.2011.00044.
Eschenbrenner, J., Winsel, S., Hammer, S., Sommer, A., Mittelstaedt, K., Drosch, M., Klar, U., Sachse, C., Hannus, M., Seidel, M., Weiss, B., Merz, C., Siemeister, G., & Hoffmann, J. (2011). Evaluation of activity and combination strategies with the microtubule-targeting drug sagopilone in breast cancer cell lines. Frontiers in oncology, 144. https://doi.org/10.3389/fonc.2011.00044
Eschenbrenner, Julia, et al. "Evaluation of activity and combination strategies with the microtubule-targeting drug sagopilone in breast cancer cell lines." Frontiers in oncology vol. 1 (2011): 44. doi: https://doi.org/10.3389/fonc.2011.00044
Eschenbrenner J, Winsel S, Hammer S, Sommer A, Mittelstaedt K, Drosch M, Klar U, Sachse C, Hannus M, Seidel M, Weiss B, Merz C, Siemeister G, Hoffmann J. Evaluation of activity and combination strategies with the microtubule-targeting drug sagopilone in breast cancer cell lines. Front Oncol. 2011 Nov 16;1:44. doi: 10.3389/fonc.2011.00044. eCollection 2011. PMID: 22649765; PMCID: PMC3355879.
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Spherical network contraction forms microtubule asters in confinement.

Soft matter

Juniper MPN, Weiss M, Platzman I, Spatz JP, Surrey T.
PMID: 29364311
Soft Matter. 2018 Feb 14;14(6):901-909. doi: 10.1039/c7sm01718a. Epub 2018 Jan 24.

Microtubules and motor proteins form active filament networks that are critical for a variety of functions in living cells. Network topology and dynamics are the result of a self-organisation process that takes place within the boundaries of the cell....

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Juniper MPN, Weiss M, Platzman I, et al. Spherical network contraction forms microtubule asters in confinement. Soft Matter. 2018;14(6):901-909doi: 10.1039/c7sm01718a.
Juniper, M. P. N., Weiss, M., Platzman, I., Spatz, J. P., & Surrey, T. (2018). Spherical network contraction forms microtubule asters in confinement. Soft matter, 14(6), 901-909. https://doi.org/10.1039/c7sm01718a
Juniper, Michael P N, et al. "Spherical network contraction forms microtubule asters in confinement." Soft matter vol. 14,6 (2018): 901-909. doi: https://doi.org/10.1039/c7sm01718a
Juniper MPN, Weiss M, Platzman I, Spatz JP, Surrey T. Spherical network contraction forms microtubule asters in confinement. Soft Matter. 2018 Feb 14;14(6):901-909. doi: 10.1039/c7sm01718a. Epub 2018 Jan 24. PMID: 29364311.
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Preparative-Scale Synthesis of Vedejs Chiral DMAP Catalysts.

The Journal of organic chemistry

Kinens A, Balkaitis S, Suna E.
PMID: 30256638
J Org Chem. 2018 Oct 19;83(20):12449-12459. doi: 10.1021/acs.joc.8b01687. Epub 2018 Oct 10.

A scalable synthesis of chiral Vedejs-type DMAP catalysts is reported. The key step of the synthesis is amination of the enantiomerically pure 4-chloropyridine derivative using well-defined ZnCl

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Kinens A, Balkaitis S, Suna E. Preparative-Scale Synthesis of Vedejs Chiral DMAP Catalysts. J Org Chem. 2018;83(20):12449-12459doi: 10.1021/acs.joc.8b01687.
Kinens, A., Balkaitis, S., & Suna, E. (2018). Preparative-Scale Synthesis of Vedejs Chiral DMAP Catalysts. The Journal of organic chemistry, 83(20), 12449-12459. https://doi.org/10.1021/acs.joc.8b01687
Kinens, Artis, et al. "Preparative-Scale Synthesis of Vedejs Chiral DMAP Catalysts." The Journal of organic chemistry vol. 83,20 (2018): 12449-12459. doi: https://doi.org/10.1021/acs.joc.8b01687
Kinens A, Balkaitis S, Suna E. Preparative-Scale Synthesis of Vedejs Chiral DMAP Catalysts. J Org Chem. 2018 Oct 19;83(20):12449-12459. doi: 10.1021/acs.joc.8b01687. Epub 2018 Oct 10. PMID: 30256638.
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Development of a Chiral DMAP Catalyst for the Dynamic Kinetic Resolution of Azole Hemiaminals.

The Journal of organic chemistry

Kinens A, Sejejs M, Kamlet AS, Piotrowski DW, Vedejs E, Suna E.
PMID: 28060519
J Org Chem. 2017 Jan 20;82(2):869-886. doi: 10.1021/acs.joc.6b02955. Epub 2017 Jan 11.

A new catalyst for the dynamic kinetic resolution of azole hemiaminals has been developed using late-stage structural modifications of the tert-leucinol-derived chiral subunit of DMAP species.

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Kinens A, Sejejs M, Kamlet AS, et al. Development of a Chiral DMAP Catalyst for the Dynamic Kinetic Resolution of Azole Hemiaminals. J Org Chem. 2017;82(2):869-886doi: 10.1021/acs.joc.6b02955.
Kinens, A., Sejejs, M., Kamlet, A. S., Piotrowski, D. W., Vedejs, E., & Suna, E. (2017). Development of a Chiral DMAP Catalyst for the Dynamic Kinetic Resolution of Azole Hemiaminals. The Journal of organic chemistry, 82(2), 869-886. https://doi.org/10.1021/acs.joc.6b02955
Kinens, Artis, et al. "Development of a Chiral DMAP Catalyst for the Dynamic Kinetic Resolution of Azole Hemiaminals." The Journal of organic chemistry vol. 82,2 (2017): 869-886. doi: https://doi.org/10.1021/acs.joc.6b02955
Kinens A, Sejejs M, Kamlet AS, Piotrowski DW, Vedejs E, Suna E. Development of a Chiral DMAP Catalyst for the Dynamic Kinetic Resolution of Azole Hemiaminals. J Org Chem. 2017 Jan 20;82(2):869-886. doi: 10.1021/acs.joc.6b02955. Epub 2017 Jan 11. PMID: 28060519.
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Showing 1 to 12 of 122 entries