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  • Book
    editors, Sue Moorhead, Elizabeth Swanson, Marion Johnson, Meridean, L. Maas.
    Summary: "Promoting safe and effective nursing care, Nursing Outcomes Classification (NOC), 6th Edition standardizes the terminology and criteria needed to measure and evaluate outcomes that result from nursing interventions. Over 540 research-based nursing outcome labels -- including50 that are NEW to this edition -- help to standardize expected patient outcomes. Specific indicators make it easier to evaluate and rate the patient in relation to outcome achievement. Written by an expert author team led by Sue Moorhead, this book is ideal for practicing nurses, students, educators, researchers, and administrators seeking to improve cost containment and patient outcomes."

    Contents:
    Part I: Overview and Use of Nursing Outcomes Classification (NOC) in Education, Practice and Research
    1. The Current Classification of Outcomes
    2. Using NOC
    Part II: NOC Taxonomy Overview of the NOC Taxonomy
    Part III: The Outcomes
    Part IV: NOC Linkages
    NOC Knowledge Outcomes Linked to Related Behavior Outcomes
    NOC and NIC Linkage to Clinical Conditions
    Part V: Core NOC Outcomes
    Core Outcomes for Nursing Specialties
    Part VI: Appendixes
    Appendix A: Outcomes: New, Revised and Retired Since the Fifth Edition
    Appendix B: Previous Editions and Translations Appendix
    C: Selected Terms and Definitions Appendix
    D: Outcomes by Scale Appendix
    E: Guidelines for Submission of a New or Revised Outcome
    Appendix F: NANDA-I Diagnoses Definitions.
    Digital Access ClinicalKey Nursing 2018
  • Article
    Philips M, Roustan C, Fattoum A, Pradel LA.
    Biochim Biophys Acta. 1978 Apr 12;523(2):368-76.
    Yeast 3-phosphoglycerate kinase (ATP:3-phospho-D-glycerate 1-phospho-transferase, EC 2.7.2.3) is inactivated by phenylglyoxal. Loss of activity correlates with the modification of two arginyl residues, both of which are protected by all of the substrates. The modification is not accompanied by any significant conformational change as determined by optical rotatory dispersion. Ultraviolet difference spectrophotometry indicates that the inactivated enzyme retains its capacity for binding the nucleotide substrates whereas the spectral perturbation characteristic of 3-phosphoglycerate binding is abolished in the modified enzyme. The data suggest that at least one of the two essential arginyl residues is located at or near the 3-phosphoglycerate binding site. A likely role of this residue could be its interaction with the negatively charged phosphate or carboxylate groups of 3-phosphoglycerate.
    Digital Access Access Options