Literature DB >> 7016120

The primary structure of crotalase, a thrombin-like venom enzyme, exhibits closer homology to kallikrein than to other serine proteases.

H Pirkle, F S Markland, I Theodor, R Baumgartner, S S Bajwa, H Kirakossian.   

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Year:  1981        PMID： 7016120     DOI： 10.1016/0006-291x(81)91802-7

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN： 0006-291X            Impact factor:   3.575


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  5 in total

1.  Evolutionary families of peptidases.

Authors:  N D Rawlings; A J Barrett
Journal:  Biochem J       Date:  1993-02-15       Impact factor: 3.857

2.  Kallikrein-like activity of crotalase, a snake venom enzyme that clots fibrinogen.

Authors:  F S Markland; C Kettner; S Schiffman; E Shaw; S S Bajwa; K N Reddy; H Kirakossian; G B Patkos; I Theodor; H Pirkle
Journal:  Proc Natl Acad Sci U S A       Date:  1982-03       Impact factor: 11.205

3.  Kn-Ba: a novel serine protease isolated from Bitis arietans snake venom with fibrinogenolytic and kinin-releasing activities.

Authors:  Ângela Alice Amadeu Megale; Fábio Carlos Magnoli; Alexandre Kazuo Kuniyoshi; Leo Kei Iwai; Denise V Tambourgi; Fernanda C V Portaro; Wilmar Dias da Silva
Journal:  J Venom Anim Toxins Incl Trop Dis       Date:  2018-12-13

Review 4.  Bioactive Molecules Derived from Snake Venoms with Therapeutic Potential for the Treatment of Thrombo-Cardiovascular Disorders Associated with COVID-19.

Authors:  Fatah Chérifi; Fatima Laraba-Djebari
Journal:  Protein J       Date:  2021-09-09       Impact factor: 2.371

5.  Helodermatine, a kallikrein-like, hypotensive enzyme from the venom of Heloderma horridum horridum (Mexican beaded lizard).

Authors:  A Alagon; L D Possani; J Smart; W D Schleuning
Journal:  J Exp Med       Date:  1986-12-01       Impact factor: 14.307
  5 in total

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