Ob-Stopping obesity, metabolic and immune-mediated disorders

Giuseppe Matarese, Veronica De Rosa

Research output: Contribution to journalArticle

Abstract

Despite its physiological importance, no part of human leptin receptor (ObR) has been structurally characterized before. In this issue of Structure, Carpenter et al. report the crystal structure of the leptin-binding domain of human ObR in complex with the Fab fragment of an ObR-blocking monoclonal antibody (9F8 mAb).

Original languageEnglish
Pages (from-to)385-387
Number of pages3
JournalStructure
Volume20
Issue number3
DOIs
Publication statusPublished - Mar 7 2012

Fingerprint

Immunoglobulin Fab Fragments
Blocking Antibodies
Immune System Diseases
Leptin
Obesity
Monoclonal Antibodies
human leptin receptor

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology

Cite this

Ob-Stopping obesity, metabolic and immune-mediated disorders. / Matarese, Giuseppe; De Rosa, Veronica.

In: Structure, Vol. 20, No. 3, 07.03.2012, p. 385-387.

Research output: Contribution to journalArticle

Matarese, Giuseppe ; De Rosa, Veronica. / Ob-Stopping obesity, metabolic and immune-mediated disorders. In: Structure. 2012 ; Vol. 20, No. 3. pp. 385-387.
@article{3f99d2a07bec4603a23d4dbbb9f4d755,
title = "Ob-Stopping obesity, metabolic and immune-mediated disorders",
abstract = "Despite its physiological importance, no part of human leptin receptor (ObR) has been structurally characterized before. In this issue of Structure, Carpenter et al. report the crystal structure of the leptin-binding domain of human ObR in complex with the Fab fragment of an ObR-blocking monoclonal antibody (9F8 mAb).",
author = "Giuseppe Matarese and {De Rosa}, Veronica",
year = "2012",
month = "3",
day = "7",
doi = "10.1016/j.str.2012.02.005",
language = "English",
volume = "20",
pages = "385--387",
journal = "Structure with Folding & design",
issn = "0969-2126",
publisher = "Cell Press",
number = "3",

}

TY - JOUR

T1 - Ob-Stopping obesity, metabolic and immune-mediated disorders

AU - Matarese, Giuseppe

AU - De Rosa, Veronica

PY - 2012/3/7

Y1 - 2012/3/7

N2 - Despite its physiological importance, no part of human leptin receptor (ObR) has been structurally characterized before. In this issue of Structure, Carpenter et al. report the crystal structure of the leptin-binding domain of human ObR in complex with the Fab fragment of an ObR-blocking monoclonal antibody (9F8 mAb).

AB - Despite its physiological importance, no part of human leptin receptor (ObR) has been structurally characterized before. In this issue of Structure, Carpenter et al. report the crystal structure of the leptin-binding domain of human ObR in complex with the Fab fragment of an ObR-blocking monoclonal antibody (9F8 mAb).

UR - http://www.scopus.com/inward/record.url?scp=84857971959&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84857971959&partnerID=8YFLogxK

U2 - 10.1016/j.str.2012.02.005

DO - 10.1016/j.str.2012.02.005

M3 - Article

C2 - 22404995

AN - SCOPUS:84857971959

VL - 20

SP - 385

EP - 387

JO - Structure with Folding & design

JF - Structure with Folding & design

SN - 0969-2126

IS - 3

ER -