Literature for family M4
(Topics flags: S Structure, V Review. To select only the references relevant to a single topic, click the link above. See explanation.)
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Hasan,R., Rony,M.N.H. and Ahmed,R.
In silico characterization and structural modeling of bacterial metalloprotease of family M4
J Genet Eng Biotechnol19, 25-25. PubMed Europe PubMed DOI -
Ruf,A., Stihle,M., Benz,J., Schmidt,M. and Sobek,H.
Structure of gentlyase, the neutral metalloprotease of Paenibacillus polymyxa
Acta Crystallogr D Biol Crystallogr69, 24-31. PubMed Europe PubMed DOI S -
Auld,D.S.
Catalytic mechanisms for metallopeptidases
[ISSN:978-0-12-407744-7]3, 370-396. DOI -
Adekoya,O.A. and Sylte,I.
The thermolysin family (M4) of enzymes: therapeutic and biotechnological potential
Chem Biol Drug Des73, 7-16. PubMed Europe PubMed DOI V -
Khan,M.T. and Sylte,I.
Determinants for psychrophilic and thermophilic features of metallopeptidases of the M4 family
In Silico Biol9, 105-124. PubMed Europe PubMed DOI -
Demidyuk,I.V., Gasanov,E.V., Safina,D.R. and Kostrov,S.V.
Structural organization of precursors of thermolysin-like proteinases
Protein J27, 343-354. PubMed Europe PubMed DOI -
Auld,D.S.
Catalytic mechanisms of metallopeptidases
[ISSN:0-12-079610-4]2, 268-289. V -
Yeats,C., Rawlings,N.D. and Bateman,A.
The PepSY domain: a regulator of peptidase activity in the microbial environment?
Trends Biochem Sci29, 169-172. PubMed Europe PubMed DOI -
[YEAR:6-10-2000]de Kreij,A., Venema,G. and Van Den Burg,B.
Substrate specificity in the highly heterogeneous M4 peptidase family is determined by a small subset of amino acids
J Biol Chem275, 31115-31120. PubMed Europe PubMed DOI -
Vriend,G. and Eijsink,V.
Prediction and analysis of structure, stability and unfolding of thermolysin-like proteases
J Comput Aided Mol Des7, 367-396. PubMed Europe PubMed V
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