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Determination of the three-dimensional structure of the bifunctional alpha-amylase/trypsin inhibitor from ragi seeds by NMR spectroscopy.
Biochemistry. 1995 Jul 4;34(26):8281-93. doi: 10.1021/bi00026a009.
Biochemistry. 1995.
PMID: 7599120
Structure of leech derived tryptase inhibitor (LDTI-C) in solution.
Mühlhahn P, Czisch M, Morenweiser R, Habermann B, Engh RA, Sommerhoff CP, Auerswald EA, Holak TA.
Mühlhahn P, et al.
FEBS Lett. 1994 Dec 5;355(3):290-6. doi: 10.1016/0014-5793(94)01225-3.
FEBS Lett. 1994.
PMID: 7988692
Free article.
Item in Clipboard
NMR characterization of structure, backbone dynamics, and glutathione binding of the human macrophage migration inhibitory factor (MIF).
Mühlhahn P, Bernhagen J, Czisch M, Georgescu J, Renner C, Ross A, Bucala R, Holak TA.
Mühlhahn P, et al.
Protein Sci. 1996 Oct;5(10):2095-103. doi: 10.1002/pro.5560051016.
Protein Sci. 1996.
PMID: 8897610
Free PMC article.
Item in Clipboard
Chalcone derivatives antagonize interactions between the human oncoprotein MDM2 and p53.
Stoll R, Renner C, Hansen S, Palme S, Klein C, Belling A, Zeslawski W, Kamionka M, Rehm T, Mühlhahn P, Schumacher R, Hesse F, Kaluza B, Voelter W, Engh RA, Holak TA.
Stoll R, et al. Among authors: muhlhahn p.
Biochemistry. 2001 Jan 16;40(2):336-44. doi: 10.1021/bi000930v.
Biochemistry. 2001.
PMID: 11148027
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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.
Nat Struct Biol. 1998 Aug;5(8):682-6. doi: 10.1038/1376.
Nat Struct Biol. 1998.
PMID: 9699630
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Sequence-specific 1H, 15N, and 13C assignment of the N-terminal domain of the human oncoprotein MDM2 that binds to p53.
Stoll R, Renner C, Mühlhahn P, Hansen S, Schumacher R, Hesse F, Kaluza B, Engh RA, Voelter W, Holak TA.
Stoll R, et al. Among authors: muhlhahn p.
J Biomol NMR. 2000 May;17(1):91-2. doi: 10.1023/a:1008365622798.
J Biomol NMR. 2000.
PMID: 10909873
No abstract available.
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