Vindigni A - Search Results

1

The core domain of hirudin from the leech Hirudinaria manillensis. Chemical modification of a tryptophan-containing synthetic peptide analog.

De Antoni F, De Filippis V, Altichieri L, Vindigni A, Polverino de Laureto P, Fontana A. De Antoni F, et al. Among authors: vindigni a. Adv Exp Med Biol. 1996;398:627-33. doi: 10.1007/978-1-4613-0381-7_103. Adv Exp Med Biol. 1996. PMID: 8906337 No abstract available.

2

Core domain of hirudin from the leech Hirudinaria manillensis: chemical synthesis, purification, and characterization of a Trp3 analog of fragment 1-47.

De Filippis V, Vindigni A, Altichieri L, Fontana A. De Filippis V, et al. Among authors: vindigni a. Biochemistry. 1995 Jul 25;34(29):9552-64. doi: 10.1021/bi00029a032. Biochemistry. 1995. PMID: 7626625

Hirudin is a small (approximately 7 kDa) disulfide-cross-linked polypeptide known as the most potent and specific thrombin inhibitor. We have previously shown that the N-terminal proteolytic fragment 1-47 of hirudin HM2 from Hirudinaria manillensis maintains inhibitory act …

Hirudin is a small (approximately 7 kDa) disulfide-cross-linked polypeptide known as the most potent and specific thrombin inhibitor. …

3

Probing the structure of hirudin from Hirudinaria manillensis by limited proteolysis. Isolation, characterization and thrombin-inhibitory properties of N-terminal fragments.

Vindigni A, De Filippis V, Zanotti G, Visco C, Orsini G, Fontana A. Vindigni A, et al. Eur J Biochem. 1994 Dec 1;226(2):323-33. doi: 10.1111/j.1432-1033.1994.tb20056.x. Eur J Biochem. 1994. PMID: 8001550 Free article.

4

Synthesis and characterization of more potent analogues of hirudin fragment 1-47 containing non-natural amino acids.

De Filippis V, Quarzago D, Vindigni A, Di Cera E, Fontana A. De Filippis V, et al. Among authors: vindigni a. Biochemistry. 1998 Sep 29;37(39):13507-15. doi: 10.1021/bi980717n. Biochemistry. 1998. PMID: 9753436

5

Incorporation of noncoded amino acids into the N-terminal domain 1-47 of hirudin yields a highly potent and selective thrombin inhibitor.

De Filippis V, Russo I, Vindigni A, Di Cera E, Salmaso S, Fontana A. De Filippis V, et al. Among authors: vindigni a. Protein Sci. 1999 Oct;8(10):2213-7. doi: 10.1110/ps.8.10.2213. Protein Sci. 1999. PMID: 10548068 Free PMC article.

Hirudin is composed of a compact N-terminal region (residues 1-47, cross-linked by three disulfide bridges) that binds to the active site of thrombin, and a flexible C-terminal tail (residues 48-64) that interacts with the exosite I of the enzyme. ...Thrombin inhibi …

Hirudin is composed of a compact N-terminal region (residues 1-47, cross-linked by three disulfide bridges) that binds to the active …

6

N(omega)-arginine dimethylation modulates the interaction between a Gly/Arg-rich peptide from human nucleolin and nucleic acids.

Raman B, Guarnaccia C, Nadassy K, Zakhariev S, Pintar A, Zanuttin F, Frigyes D, Acatrinei C, Vindigni A, Pongor G, Pongor S. Raman B, et al. Among authors: vindigni a. Nucleic Acids Res. 2001 Aug 15;29(16):3377-84. doi: 10.1093/nar/29.16.3377. Nucleic Acids Res. 2001. PMID: 11504875 Free PMC article.

7

Release of fibrinopeptides by the slow and fast forms of thrombin.

Vindigni A, Di Cera E. Vindigni A, et al. Biochemistry. 1996 Apr 9;35(14):4417-26. doi: 10.1021/bi952834d. Biochemistry. 1996. PMID: 8605191

8

Energetics of thrombin-thrombomodulin interaction.

Vindigni A, White CE, Komives EA, Di Cera E. Vindigni A, et al. Biochemistry. 1997 Jun 3;36(22):6674-81. doi: 10.1021/bi962766a. Biochemistry. 1997. PMID: 9184147

9

Thermodynamic investigation of hirudin binding to the slow and fast forms of thrombin: evidence for folding transitions in the inhibitor and protease coupled to binding.

Ayala YM, Vindigni A, Nayal M, Spolar RS, Record MT Jr, Di Cera E. Ayala YM, et al. Among authors: vindigni a. J Mol Biol. 1995 Nov 10;253(5):787-98. doi: 10.1006/jmbi.1995.0591. J Mol Biol. 1995. PMID: 7473752

10

Role of P225 and the C136-C201 disulfide bond in tissue plasminogen activator.

Vindigni A, Di Cera E. Vindigni A, et al. Protein Sci. 1998 Aug;7(8):1728-37. doi: 10.1002/pro.5560070807. Protein Sci. 1998. PMID: 10082369 Free PMC article.

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