1.

Record Nr.

UNISA990000873020203316

Autore

SAGINJAN, Marietta Seergevna

Titolo

Monografii Etjudy o russkih klassikah : Marietta Seerggevna Saginjan ; redakcionnaja kollegija Vercenko Ju. N. ...[et al] (8)

Pubbl/distr/stampa

Moskva, : Hudožestvennaja literatura, 1989

ISBN

5-280-00791-9

Descrizione fisica

733 p. ; 21 cm

Disciplina

891.7844

Collocazione

VIII.1.A. 684/8(IIr A 311/8)

VIII.1.A. 684/8a(IIr A 311/8 BIS)

Lingua di pubblicazione

Russo

Formato

Materiale a stampa

Livello bibliografico

Monografia

Note generali

Titolo tradotto: Monografie; Articoli sui classici russi



2.

Record Nr.

UNISA996418949903316

Titolo

RBM : a journal of rare books, manuscripts, and cultural heritage

Pubbl/distr/stampa

Chicago, IL, : Association of College and Research Libraries

ISSN

2150-668X

Disciplina

026

Soggetti

Rare books

Manuscripts

Cultural property - Protection

Rare books - Collectors and collecting

Manuscripts - Collectors and collecting

Libraries - Special collections - Rare books

Libraries - Special collections - Manuscripts

Bibliothèques - Fonds spéciaux - Livres rares

Bibliothèques - Fonds spéciaux - Manuscrits

Livres rares - Collectionneurs et collections

Manuscrits - Collectionneurs et collections

Livres rares

Manuscrits

Libraries - Special collections

Zeldzame en kostbare boeken

Handschriften

Manuscripts.

Periodicals.

Lingua di pubblicazione

Inglese

Formato

Materiale a stampa

Livello bibliografico

Periodico



3.

Record Nr.

UNINA9910557717203321

Autore

Ågren Magnus S

Titolo

Matrix Metalloproteinase

Pubbl/distr/stampa

Basel, Switzerland, : MDPI - Multidisciplinary Digital Publishing Institute, 2020

Descrizione fisica

1 online resource (262 p.)

Soggetti

Biology, life sciences

Research & information: general

Lingua di pubblicazione

Inglese

Formato

Materiale a stampa

Livello bibliografico

Monografia

Sommario/riassunto

Zinc-dependent matrix metalloproteinases (MMPs) belong to metzincins that comprise not only 23 human MMPs but also other metalloproteinases, such as 21 human ADAMs (a disintegrin and metalloproteinase domain) and 19 secreted ADAMTSs (a disintegrin and metalloproteinase thrombospondin domain). The many setbacks from the clinical trials of broad-spectrum MMP inhibitors for cancer indications in the late 1990s emphasized the extreme complexity of the participation of these proteolytic enzymes in biology. This editorial mini-review summarizes the Special Issue, which includes four review articles and 10 original articles that highlight the versatile roles of MMPs, ADAMs, and ADAMTSs, in normal physiology as well as in neoplastic and destructive processes in tissue. In addition, we briefly discuss the unambiguous involvement of MMPs in wound healing.