Holak TA - Search Results

1

Lifeact: a versatile marker to visualize F-actin.

Riedl J, Crevenna AH, Kessenbrock K, Yu JH, Neukirchen D, Bista M, Bradke F, Jenne D, Holak TA, Werb Z, Sixt M, Wedlich-Soldner R. Riedl J, et al. Among authors: holak ta. Nat Methods. 2008 Jul;5(7):605-7. doi: 10.1038/nmeth.1220. Epub 2008 Jun 8. Nat Methods. 2008. PMID: 18536722 Free PMC article.

2

Robust NMR screening for lead compounds using tryptophan-containing proteins.

Bista M, Kowalska K, Janczyk W, Dömling A, Holak TA. Bista M, et al. Among authors: holak ta. J Am Chem Soc. 2009 Jun 10;131(22):7500-1. doi: 10.1021/ja901863h. J Am Chem Soc. 2009. PMID: 19422216

3

Analysis tools for single-monomer measurements of self-assembly processes.

Hoyer M, Crevenna AH, Kitel R, Willems K, Czub M, Dubin G, Van Dorpe P, Holak TA, Lamb DC. Hoyer M, et al. Among authors: holak ta. Sci Rep. 2022 Mar 18;12(1):4682. doi: 10.1038/s41598-022-08245-6. Sci Rep. 2022. PMID: 35304498 Free PMC article.

4

Robust generation of lead compounds for protein-protein interactions by computational and MCR chemistry: p53/Hdm2 antagonists.

Czarna A, Beck B, Srivastava S, Popowicz GM, Wolf S, Huang Y, Bista M, Holak TA, Dömling A. Czarna A, et al. Among authors: holak ta. Angew Chem Int Ed Engl. 2010 Jul 19;49(31):5352-6. doi: 10.1002/anie.201001343. Angew Chem Int Ed Engl. 2010. PMID: 20575124 Free PMC article. No abstract available.

5

Transient protein states in designing inhibitors of the MDM2-p53 interaction.

Bista M, Wolf S, Khoury K, Kowalska K, Huang Y, Wrona E, Arciniega M, Popowicz GM, Holak TA, Dömling A. Bista M, et al. Among authors: holak ta. Structure. 2013 Dec 3;21(12):2143-51. doi: 10.1016/j.str.2013.09.006. Epub 2013 Oct 24. Structure. 2013. PMID: 24207125 Free PMC article.

6

Role of the ubiquitin-like protein Hub1 in splice-site usage and alternative splicing.

Mishra SK, Ammon T, Popowicz GM, Krajewski M, Nagel RJ, Ares M Jr, Holak TA, Jentsch S. Mishra SK, et al. Among authors: holak ta. Nature. 2011 May 25;474(7350):173-8. doi: 10.1038/nature10143. Nature. 2011. PMID: 21614000 Free PMC article.

7

The repeating segments of the F-actin cross-linking gelation factor (ABP-120) have an immunoglobulin-like fold.

Fucini P, Renner C, Herberhold C, Noegel AA, Holak TA. Fucini P, et al. Among authors: holak ta. Nat Struct Biol. 1997 Mar;4(3):223-30. doi: 10.1038/nsb0397-223. Nat Struct Biol. 1997. PMID: 9164464

8

Structure of hisactophilin is similar to interleukin-1 beta and fibroblast growth factor.

Habazettl J, Gondol D, Wiltscheck R, Otlewski J, Schleicher M, Holak TA. Habazettl J, et al. Among authors: holak ta. Nature. 1992 Oct 29;359(6398):855-8. doi: 10.1038/359855a0. Nature. 1992. PMID: 1436061

9

Structure in solution of the major cold-shock protein from Bacillus subtilis.

Schnuchel A, Wiltscheck R, Czisch M, Herrler M, Willimsky G, Graumann P, Marahiel MA, Holak TA. Schnuchel A, et al. Among authors: holak ta. Nature. 1993 Jul 8;364(6433):169-71. doi: 10.1038/364169a0. Nature. 1993. PMID: 8321289

10

Structure of interleukin 16 resembles a PDZ domain with an occluded peptide binding site.

Mühlhahn P, Zweckstetter M, Georgescu J, Ciosto C, Renner C, Lanzendörfer M, Lang K, Ambrosius D, Baier M, Kurth R, Holak TA. Mühlhahn P, et al. Among authors: holak ta. Nat Struct Biol. 1998 Aug;5(8):682-6. doi: 10.1038/1376. Nat Struct Biol. 1998. PMID: 9699630

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