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  • Book
    Solange Peters, Benjamin Besse, editor.
    Summary: This book provides an up-to-date review of current management techniques for Non-Small Cell Lung Cancer. It addresses all of the latest issues that have been raised by the discovery of oncogenic drivers and the improvement of diagnosis and therapeutic methods, including new radiotherapy techniques and anticancer strategies like immunotherapy. New strategies for patients with molecular alterations and the management of particular types of cases are also highlighted. Written by recognized experts in their field, the book represents a unique and valuable resource in the field of lung cancer, both for those currently in training and for those already in clinical or research practice.

    Contents:
    Preface
    Foreword
    Screening
    New Diagnostic Approaches
    PET and Staging Minimally Invasive (EBUS)
    Innovative Approaches in Early NSCLC
    Minimally Invasive Surgery for Early NSCLC
    Stereotaxic Radiotherapy in Localized Cancer
    How to Personalize Perioperative Chemotherapy in Early Cancer?
    New Approaches in Locally Advanced NSCLC
    Advances in Radiotherapy for Locally Advanced NSCLC
    Advances in Systemic Treatment for Locally Advanced NSCLC
    Surgery of Advanced Tumors
    New Approaches in Stage IV NSCLC
    How to Personalize Chemotherapy in Stage IV NSCLC?
    Supportive Care
    Molecular Subgroups
    Strategies in EGFR Mutated NSCLC Patients
    Strategies in ALK Rearranged NSCLC patients
    Strategies in KRAS mutated NSCLC Patients
    Strategies in Patients with Other Molecular Alterations
    New Approaches in Immunotherapy
    Management of Particular Cases
    Oligometastasis
    Bone Metastasis
    Brain Metastasis.
    Digital Access Springer 2015
  • Article
    James HL, Cohen AB.
    J Clin Invest. 1978 Dec;62(6):1344-53.
    The interaction of the human plasma protein, alpha-1-antitrypsin, with porcine pancreatic elastase was studied by isolating and characterizing their reaction products. Native alpha-1-antitrypsin has a mass ratio (Mr) of 54,000, an amino-terminal glx, and a carboxy-terminal lys residue. The elastase used has an Mr of 26,400 and an amino-terminal val residue. When the two proteins are combined at inhibitor excess, two major products result. One of the products is a complex of the enzyme and inhibitor with amino-terminal ser and val residues, which indicates that a peptide has been removed from the amino-terminal end of the inhibitor. The second product is a modified form of alpha-1-antitrypsin with an Mr of 51,300, an aminoterminal glx residue and a carboxy-terminal thr-leu dipeptide. It has no inhibitory activity against elastase. The components of the isolated complex can be split at high pH in the presence of diisopropyl fluorophosphate, which results in a catalytically inactive enzyme with the same Mr and amino-terminal residue as the native enzyme, and a large fragment of alpha-1-antitrypsin (alpha-1-antitrypsin(*)). This fragment has an Mr of 50,100, an amino-terminal ser residue and a carboxy-terminal thr-leu dipeptide. Based on these data, the following hypothesis is proposed. Elastase can attack alpha-1-antitrypsin at either of two major sites. If it attacks first at the carboxy side of the thr-leu dipeptide, located in the carboxy-terminal portion of the inhibitor, the alpha-1-antitrypsin is cleaved into two fragments with loss of inhibitory activity and absence of complex formation. If, however, the elastase first attacks an x-ser bond near the amino-terminal end of the inhibitor, the elastase then reacts with alpha-1-antitrypsin at the same leu moiety to form a stable complex with complete inhibition of the enzyme.
    Digital Access Access Options