1985, ISBN 9780340370117, xi, 467
Book
1984, 1st ed. --, ISBN 0393018725, 121 p., [4] p. of plates
Book
2000, Ecological issues (British Ecological Society), ISBN 0632056088, Volume 9., v, 66
Book
JACC (Journal of the American College of Cardiology), ISSN 0735-1097, 2016, Volume 69, Issue 11, pp. 1427 - 1450
Abstract Cardiovascular disease (CVD) is a leading cause of death and disability in the United States. National quality programs such as the National...
Cardiovascular | Internal Medicine | congenital heart disease | percutaneous coronary intervention | implantable cardioverter-defibrillators | quality of care | acute coronary syndromes | APPROPRIATENESS | CARDIAC & CARDIOVASCULAR SYSTEMS | NCDR | RISK | IMPACT | OUTCOMES | PROGRAM | INSIGHTS | Defibrillators, Implantable - statistics & numerical data | Humans | Middle Aged | Aged, 80 and over | Acute Coronary Syndrome - therapy | Female | Male | Percutaneous Coronary Intervention - statistics & numerical data | Registries | Aged | Cardiology - trends | Transluminal angioplasty | Genetic disorders | Coronary artery bypass | Implants, Artificial | Prosthesis | Low density lipoproteins | Cardiac patients | Medical care | Congenital heart disease | Cardiology | Heart attack | Quality management | Intervention | Pediatrics | Angiography | Medical services | Cardiovascular disease | Data dictionaries | Datasets | Demographics | Defibrillators | Feedback | Quality | Electrocardiography | Heart diseases | Congenital diseases | Catheterization | Business metrics | Patients | Coronary artery disease | Validity | Hospitals | Accountability | Diagnostic systems | Diabetes | Clinical medicine | Quality assessment | Cardiovascular diseases | Ambulatory care
Cardiovascular | Internal Medicine | congenital heart disease | percutaneous coronary intervention | implantable cardioverter-defibrillators | quality of care | acute coronary syndromes | APPROPRIATENESS | CARDIAC & CARDIOVASCULAR SYSTEMS | NCDR | RISK | IMPACT | OUTCOMES | PROGRAM | INSIGHTS | Defibrillators, Implantable - statistics & numerical data | Humans | Middle Aged | Aged, 80 and over | Acute Coronary Syndrome - therapy | Female | Male | Percutaneous Coronary Intervention - statistics & numerical data | Registries | Aged | Cardiology - trends | Transluminal angioplasty | Genetic disorders | Coronary artery bypass | Implants, Artificial | Prosthesis | Low density lipoproteins | Cardiac patients | Medical care | Congenital heart disease | Cardiology | Heart attack | Quality management | Intervention | Pediatrics | Angiography | Medical services | Cardiovascular disease | Data dictionaries | Datasets | Demographics | Defibrillators | Feedback | Quality | Electrocardiography | Heart diseases | Congenital diseases | Catheterization | Business metrics | Patients | Coronary artery disease | Validity | Hospitals | Accountability | Diagnostic systems | Diabetes | Clinical medicine | Quality assessment | Cardiovascular diseases | Ambulatory care
Journal Article
1973, 164
Book
1986, ISBN 0231062745, xi, 467
Book
2014, First edition., ISBN 9780871404534, lxx, 852 pages
Book
Nature communications, ISSN 2041-1723, 2019, Volume 10, Issue 1, pp. 763 - 10
The N-terminal fusion peptide (FP) of the human immunodeficiency virus (HIV)-1 envelope glycoprotein (Env) gp41 subunit plays a critical role in cell entry....
INTERMOLECULAR DISULFIDE BOND | SITE | HEMAGGLUTININ | MULTIDISCIPLINARY SCIENCES | GP41 | ENV TRIMERS | ANTIBODY | INFLUENZA-VIRUS | CRYO-EM STRUCTURE | DEPENDENT EPITOPE | GP140 TRIMERS | Peptides | Glycoprotein gp41 | Human immunodeficiency virus--HIV | Crystallization | Glycoprotein | Antibodies | Tryptophan | Viruses | Glycoproteins | Trimers | Vaccines | Crystal structure
INTERMOLECULAR DISULFIDE BOND | SITE | HEMAGGLUTININ | MULTIDISCIPLINARY SCIENCES | GP41 | ENV TRIMERS | ANTIBODY | INFLUENZA-VIRUS | CRYO-EM STRUCTURE | DEPENDENT EPITOPE | GP140 TRIMERS | Peptides | Glycoprotein gp41 | Human immunodeficiency virus--HIV | Crystallization | Glycoprotein | Antibodies | Tryptophan | Viruses | Glycoproteins | Trimers | Vaccines | Crystal structure
Journal Article
1872, New ed.
eBook
MOLECULES, ISSN 1420-3049, 03/2019, Volume 24, Issue 7, p. 1240
The leaves and twigs of the desiccation-tolerant medicinal shrub Myrothamnus flabellifolia are harvested for use in traditional and commercial teas and...
OXIDATIVE STRESS | SOUTH-AFRICAN | anthocyanins | BIOCHEMISTRY & MOLECULAR BIOLOGY | LEAVES | desiccation tolerance | CANCER | CHEMISTRY, MULTIDISCIPLINARY | METHYL GALLATE | RESPONSES | LC-MS | O-GALLOYLQUINIC ACID | Myrothamnus flabellifolia | POLYPHENOL | flavonoids | resurrection plant | phenolics | LC-MS/MS
OXIDATIVE STRESS | SOUTH-AFRICAN | anthocyanins | BIOCHEMISTRY & MOLECULAR BIOLOGY | LEAVES | desiccation tolerance | CANCER | CHEMISTRY, MULTIDISCIPLINARY | METHYL GALLATE | RESPONSES | LC-MS | O-GALLOYLQUINIC ACID | Myrothamnus flabellifolia | POLYPHENOL | flavonoids | resurrection plant | phenolics | LC-MS/MS
Journal Article
Immunological Reviews, ISSN 0105-2896, 01/2017, Volume 275, Issue 1, pp. 161 - 182
Summary We describe the development and potential use of various designs of recombinant HIV‐1 envelope glycoprotein trimers that mimic the structure of the...
Env trimers | neutralizing antibodies | HIV‐1 vaccines | HIV-1 vaccines | B-CELL RECEPTORS | ENVELOPE GLYCOPROTEIN TRIMERS | AFFINITY MATURATION | CRYSTAL-STRUCTURE | RECOMBINANT GLYCOPROTEIN-120 | IMMUNOLOGY | GP140 TRIMERS | BROADLY NEUTRALIZING ANTIBODIES | PROTEOLYTICALLY MATURE | IMMUNODEFICIENCY-VIRUS TYPE-1 | CRYO-EM STRUCTURE | HIV Antibodies - metabolism | Humans | Protein Multimerization | AIDS Vaccines - immunology | Antibodies, Neutralizing - metabolism | Epitopes - immunology | HIV Infections - immunology | HIV-1 - immunology | Animals | HIV Antigens - immunology | Recombinant Proteins - immunology | Viral Envelope Proteins - chemistry | HIV Antigens - chemistry | Viral Envelope Proteins - immunology | HIV (Viruses) | Vaccines | Immunization | Immunoglobulins | Glycoprotein | Antibodies | Trimers | Immunology | Immunogenicity | Design improvements | Neutralizing | Human immunodeficiency virus--HIV | In vitro methods and tests | Recombinant | Invited Reviews | Invited Review
Env trimers | neutralizing antibodies | HIV‐1 vaccines | HIV-1 vaccines | B-CELL RECEPTORS | ENVELOPE GLYCOPROTEIN TRIMERS | AFFINITY MATURATION | CRYSTAL-STRUCTURE | RECOMBINANT GLYCOPROTEIN-120 | IMMUNOLOGY | GP140 TRIMERS | BROADLY NEUTRALIZING ANTIBODIES | PROTEOLYTICALLY MATURE | IMMUNODEFICIENCY-VIRUS TYPE-1 | CRYO-EM STRUCTURE | HIV Antibodies - metabolism | Humans | Protein Multimerization | AIDS Vaccines - immunology | Antibodies, Neutralizing - metabolism | Epitopes - immunology | HIV Infections - immunology | HIV-1 - immunology | Animals | HIV Antigens - immunology | Recombinant Proteins - immunology | Viral Envelope Proteins - chemistry | HIV Antigens - chemistry | Viral Envelope Proteins - immunology | HIV (Viruses) | Vaccines | Immunization | Immunoglobulins | Glycoprotein | Antibodies | Trimers | Immunology | Immunogenicity | Design improvements | Neutralizing | Human immunodeficiency virus--HIV | In vitro methods and tests | Recombinant | Invited Reviews | Invited Review
Journal Article
Bioconjugate Chemistry, ISSN 1043-1802, 06/2018, Volume 29, Issue 6, pp. 2074 - 2081
The high specificity and favorable pharmacological properties of monoclonal antibodies (mAbs) have prompted significant interest in re-engineering this class...
DRUG | PEPTIDE-BINDING-SITE | PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | HIGH-AFFINITY | CHEMISTRY, ORGANIC | DIFFRACTION | CHEMISTRY, MULTIDISCIPLINARY | Trastuzumab - chemistry | Fluorescent Dyes - chemistry | Optical Imaging | Click Chemistry | Humans | Amino Acids - chemistry | Models, Molecular | Immunoconjugates - chemistry | Animals | MCF-7 Cells | Disulfides - chemistry | Immunoglobulin Fab Fragments - chemistry | Female | Mice | Breast Neoplasms - diagnostic imaging | Catalysis | Antibodies, Monoclonal - chemistry
DRUG | PEPTIDE-BINDING-SITE | PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | HIGH-AFFINITY | CHEMISTRY, ORGANIC | DIFFRACTION | CHEMISTRY, MULTIDISCIPLINARY | Trastuzumab - chemistry | Fluorescent Dyes - chemistry | Optical Imaging | Click Chemistry | Humans | Amino Acids - chemistry | Models, Molecular | Immunoconjugates - chemistry | Animals | MCF-7 Cells | Disulfides - chemistry | Immunoglobulin Fab Fragments - chemistry | Female | Mice | Breast Neoplasms - diagnostic imaging | Catalysis | Antibodies, Monoclonal - chemistry
Journal Article
Journal of Physical Chemistry. C, ISSN 1932-7447, 01/2019, Volume 123, Issue 6
Films of (FA0.79MA0.16Cs0.05)0.97Pb(I0.84Br0.16)2.97 were grown over TiO2, SnO2, indium tin oxide (ITO), and NiO. Film conductivity was interrogated by...
perovskites | photoconductivity | conductivity | MATERIALS SCIENCE | SOLAR ENERGY | thin films
perovskites | photoconductivity | conductivity | MATERIALS SCIENCE | SOLAR ENERGY | thin films
Journal Article
Science, ISSN 0036-8075, 12/2013, Volume 342, Issue 6165, pp. 1477 - 1483
HIV-1 entry into CD4⁺ target cells is mediated by cleaved envelope glycoprotein (Env) trimers that have been challenging to characterize structurally. Here, we...
Polysaccharides | Electronic structure | RESEARCH ARTICLES | Viruses | Trimers | Epitopes | Grants | Electron density | Crystal structure | HIV 1 | Protein subunits | MEMBRANE-FUSION | NEUTRALIZING ANTIBODY PG9 | V3 LOOP | POTENT NEUTRALIZATION | GP120 CORE | MULTIDISCIPLINARY SCIENCES | MOLECULAR ARCHITECTURE | GLYCOPROTEIN TRIMER | HUMAN-IMMUNODEFICIENCY-VIRUS | N-GLYCAN RECOGNITION | VARIABLE LOOPS | env Gene Products, Human Immunodeficiency Virus - immunology | HIV Envelope Protein gp41 - immunology | Humans | Protein Multimerization | Solubility | Recombinant Proteins - chemistry | Crystallography, X-Ray | HIV Envelope Protein gp41 - chemistry | HIV Envelope Protein gp120 - immunology | Recombinant Proteins - immunology | Antibodies, Neutralizing - chemistry | Antibodies, Viral - chemistry | Protein Structure, Quaternary | HIV Envelope Protein gp120 - chemistry | env Gene Products, Human Immunodeficiency Virus - chemistry | Physiological aspects | Host-parasite relationships | Research | HIV (Viruses) | Structure | Crystals | Glycoproteins | Vaccines | Human immunodeficiency virus--HIV | Envelopes | Mutations | Neutralizing | Antibodies | Flexibility
Polysaccharides | Electronic structure | RESEARCH ARTICLES | Viruses | Trimers | Epitopes | Grants | Electron density | Crystal structure | HIV 1 | Protein subunits | MEMBRANE-FUSION | NEUTRALIZING ANTIBODY PG9 | V3 LOOP | POTENT NEUTRALIZATION | GP120 CORE | MULTIDISCIPLINARY SCIENCES | MOLECULAR ARCHITECTURE | GLYCOPROTEIN TRIMER | HUMAN-IMMUNODEFICIENCY-VIRUS | N-GLYCAN RECOGNITION | VARIABLE LOOPS | env Gene Products, Human Immunodeficiency Virus - immunology | HIV Envelope Protein gp41 - immunology | Humans | Protein Multimerization | Solubility | Recombinant Proteins - chemistry | Crystallography, X-Ray | HIV Envelope Protein gp41 - chemistry | HIV Envelope Protein gp120 - immunology | Recombinant Proteins - immunology | Antibodies, Neutralizing - chemistry | Antibodies, Viral - chemistry | Protein Structure, Quaternary | HIV Envelope Protein gp120 - chemistry | env Gene Products, Human Immunodeficiency Virus - chemistry | Physiological aspects | Host-parasite relationships | Research | HIV (Viruses) | Structure | Crystals | Glycoproteins | Vaccines | Human immunodeficiency virus--HIV | Envelopes | Mutations | Neutralizing | Antibodies | Flexibility
Journal Article