| 词条 | Nancy Hogg |
| 释义 |
| name = Nancy Hogg | image = Nancy Hogg.png | image_size = | alt = | caption = | birth_name = | birth_date = | birth_place = | death_date = | death_place = | resting_place = | resting_place_coordinates = | residence = | nationality = | fields = Immunology | workplaces = | patrons = | alma_mater = | thesis_title = | thesis_url = | thesis_year = | doctoral_advisor = | academic_advisors = | doctoral_students = | notable_students = | known_for = Study of Leukocyte Integrins | influences = | influenced = | awards = | spouse = | children = | death_cause = | education = }} Nancy Hogg FMedSci is an immunologist who has made major contributions in the field of adhesion molecules, focusing on the integrins expressed by leukocytes. [1] Hogg was elected to the Academy of Medical Sciences in 2002 and currently holds an Emeritus position at The Francis Crick Institute, London. Education and academic careerNancy Hogg studied for a BSc at the University of Toronto. She was awarded a PhD working with Rodney Porter firstly at the University of London and then at Department of Biochemistry, University of Oxford. This was followed by a post–doctoral period at National Institute for Medical Research (NIMR) and finally a position at Imperial Cancer Research Fund (ICRF) (which became Cancer Research UK London Research Institute and is now part of the Francis Crick Institute). Hogg was located initially at University College London followed by a move to the main laboratories in Lincoln’s Inn Fields where she set up her laboratory focusing initially on the function of macrophages, but then increasingly on the adhesion molecules termed integrins expressed by all leukocytes. Research interestsNancy Hogg’s PhD project involved the protein sequencing of immunoglobulin heavy chains identifying for the first time the heterogeneity that accounts for immunoglobulin specificity.[2] During a postdoctoral period at ICRF she co-discovered the protein that is now known as fibronectin. [3] Through study of leukocyte integrin LFA-1 and particularly special mAb 24, Hogg was the first to document that the state of integrin activity could be controlled by bound divalent cations. [4] [5] The active forms are linked to different cytoskeletal proteins, namely talin for high affinity and a-actinin for clustered intermediate affinity LFA-1 . [6][7] The lab showed that the LFA-1 ligand ICAM-1 was a target for pathogen binding, for example the malaria parasite Plasmodium falciparum.[8] The generation of LFA-1 null mice revealed the central role of LFA-1 in leukocyte migration within lymph nodes in vivo. [9][10] Hogg also first identified and characterised unique Leukocyte Adhesion Deficiency-III (LAD-III) patients that expressed inactive leukocyte integrins. [11] This integrin malfunction was due to mutation in protein kindlin-3. [12] Hogg has also studied the S100A8/S100A9 proteins that constitute 45% of neutrophil cytosolic protein.[13][14] S100a9 null mice demonstrated that myeloid cells could function relatively normally without these proteins but they had a major role in responding to infections such as S. pneumonia in terms of cytokine generation.[15] Professional associations and awards
References1. ^1 {{Cite web|url=https://acmedsci.ac.uk/fellows/fellows-directory/ordinary-fellows/professor-nancy-hogg|title=Professor Nancy Hogg {{!}} The Academy of Medical Sciences|website=acmedsci.ac.uk|access-date=2019-02-16}} {{authority control}}{{DEFAULTSORT:Hogg, Nancy}}2. ^{{Cite journal|last=Press|first=E. M.|last2=Hogg|first2=N. M.|date=1969-08-23|title=Comparative study of two immunoglobulin G Fd-fragments|journal=Nature|volume=223|issue=5208|pages=808–810|issn=0028-0836|pmid=5799021}} 3. ^{{Cite journal|last=Hogg|first=Nancy M.|date=February 1974|title=A Comparison of Membrane Proteins of Normal and Transformed Cells by Lactoperoxidase Labeling|journal=Proceedings of the National Academy of Sciences of the United States of America|volume=71|issue=2|pages=489–492|issn=0027-8424|pmid=4360946|pmc=388032|doi=10.1073/pnas.71.2.489}} 4. ^{{Cite journal|last=Dransfield|first=I|last2=Hogg|first2=N|date=1989-12-01|title=Regulated expression of Mg2+ binding epitope on leukocyte integrin alpha subunits.|journal=The EMBO Journal|volume=8|issue=12|pages=3759–3765|issn=0261-4189|pmid=2479549|pmc=402061|doi=10.1002/j.1460-2075.1989.tb08552.x}} 5. ^{{Cite journal|date=1992-01-01|title=Divalent cation regulation of the function of the leukocyte integrin LFA-1|journal=The Journal of Cell Biology|volume=116|issue=1|pages=219–226|issn=0021-9525|pmc=2289255|pmid=1346139|last1=Dransfield|first1=I.|last2=Cabañas|first2=C.|last3=Craig|first3=A.|last4=Hogg|first4=N.|doi=10.1083/jcb.116.1.219}} 6. ^{{Cite journal|last=Stanley|first=Paula|last2=Smith|first2=Andrew|last3=McDowall|first3=Alison|last4=Nicol|first4=Alastair|last5=Zicha|first5=Daniel|last6=Hogg|first6=Nancy|date=2008-01-09|title=Intermediate-affinity LFA-1 binds α-actinin-1 to control migration at the leading edge of the T cell|journal=The EMBO Journal|volume=27|issue=1|pages=62–75|doi=10.1038/sj.emboj.7601959|issn=0261-4189|pmc=2147999|pmid=18079697}} 7. ^{{Cite journal|last=Smith|first=Andrew|last2=Carrasco|first2=Yolanda R.|last3=Stanley|first3=Paula|last4=Kieffer|first4=Nelly|last5=Batista|first5=Facundo D.|last6=Hogg|first6=Nancy|date=2005-07-04|title=A talin-dependent LFA-1 focal zone is formed by rapidly migrating T lymphocytes|journal=The Journal of Cell Biology|volume=170|issue=1|pages=141–151|doi=10.1083/jcb.200412032|issn=0021-9525|pmc=2171377|pmid=15983060}} 8. ^{{Cite journal|last=Hogg|first=Nancy|last2=Newbold|first2=Christopher I.|last3=Marsh|first3=Kevin|last4=Sternberg|first4=Michael J. E.|last5=Bates|first5=Paul A.|last6=Craig|first6=Alister G.|last7=McDowall|first7=Alison|last8=Berendt|first8=Anthony R.|date=1992-01-10|title=The binding site on ICAM-1 for plasmodium falciparum-infected erythrocytes overlaps, but is distinct from, the LFA-1-binding site|url=https://www.cell.com/cell/abstract/0092-8674(92)90207-S|journal=Cell|language=English|volume=68|issue=1|pages=71–81|doi=10.1016/0092-8674(92)90207-S|issn=0092-8674|pmid=1370656}} 9. ^{{Cite journal|last=Berlin-Rufenach|first=Cornelia|last2=Otto|first2=Florian|last3=Mathies|first3=Meg|last4=Westermann|first4=Juergen|last5=Owen|first5=Michael J.|last6=Hamann|first6=Alf|last7=Hogg|first7=Nancy|date=1999-05-03|title=Lymphocyte Migration in Lymphocyte Function-associated Antigen (LFA)-1–deficient Mice|journal=The Journal of Experimental Medicine|volume=189|issue=9|pages=1467–1478|issn=0022-1007|pmc=2193056|pmid=10224287|doi=10.1084/jem.189.9.1467}} 10. ^{{Cite journal|last=Reichardt|first=Peter|last2=Patzak|first2=Irene|last3=Jones|first3=Kristian|last4=Etemire|first4=Eloho|last5=Gunzer|first5=Matthias|last6=Hogg|first6=Nancy|date=2013-03-20|title=A role for LFA-1 in delaying T-lymphocyte egress from lymph nodes|journal=The EMBO Journal|volume=32|issue=6|pages=829–843|doi=10.1038/emboj.2013.33|issn=0261-4189|pmc=3604724|pmid=23443048}} 11. ^{{Cite journal|last=Hogg|first=Nancy|last2=Stewart|first2=Mairi P.|last3=Scarth|first3=Sarah L.|last4=Newton|first4=Rebecca|last5=Shaw|first5=Jacqueline M.|last6=Law|first6=S.K. Alex|last7=Klein|first7=Nigel|date=1999-01-01|title=A novel leukocyte adhesion deficiency caused by expressed but nonfunctional β2 integrins Mac-1 and LFA-1|journal=Journal of Clinical Investigation|volume=103|issue=1|pages=97–106|issn=0021-9738|pmid=9884339|pmc=407855|doi=10.1172/JCI3312}} 12. ^{{Cite journal|last=Svensson|first=Lena|last2=Howarth|first2=Kimberley|last3=McDowall|first3=Alison|last4=Patzak|first4=Irene|last5=Evans|first5=Rachel|last6=Ussar|first6=Siegfried|last7=Moser|first7=Markus|last8=Metin|first8=Ayse|last9=Fried|first9=Mike|date=March 2009|title=Leukocyte adhesion deficiency-III is caused by mutations in KINDLIN3 affecting integrin activation|journal=Nature Medicine|volume=15|issue=3|pages=306–312|doi=10.1038/nm.1931|issn=1078-8956|pmc=2680140|pmid=19234463}} 13. ^{{Cite journal|last=Hogg|first=N.|last2=Freemont|first2=P.|last3=Bennett|first3=R.|last4=Gorman|first4=M.|last5=Edgeworth|first5=J.|date=1991-04-25|title=Identification of p8,14 as a highly abundant heterodimeric calcium binding protein complex of myeloid cells.|url=http://www.jbc.org/content/266/12/7706|journal=Journal of Biological Chemistry|volume=266|issue=12|pages=7706–7713|issn=0021-9258|pmid=2019594}} 14. ^{{Cite journal|last=Hobbs|first=Josie A. R.|last2=May|first2=Richard|last3=Tanousis|first3=Kiki|last4=McNeill|first4=Eileen|last5=Mathies|first5=Margaret|last6=Gebhardt|first6=Christoffer|last7=Henderson|first7=Robert|last8=Robinson|first8=Matthew J.|last9=Hogg|first9=Nancy|date=April 2003|title=Myeloid Cell Function in MRP-14 (S100A9) Null Mice|journal=Molecular and Cellular Biology|volume=23|issue=7|pages=2564–2576|doi=10.1128/MCB.23.7.2564-2576.2003|issn=0270-7306|pmid=12640137|pmc=150714}} 15. ^{{Cite journal|last=De Filippo|first=Katia|last2=Neill|first2=Daniel R.|last3=Mathies|first3=Meg|last4=Bangert|first4=Mathieu|last5=McNeill|first5=Eileen|last6=Kadioglu|first6=Aras|last7=Hogg|first7=Nancy|date=2014-04-28|title=A new protective role for S100A9 in regulation of neutrophil recruitment during invasive pneumococcal pneumonia|journal=The FASEB Journal|volume=28|issue=8|pages=3600–3608|doi=10.1096/fj.13-247460|pmid=24776746|issn=0892-6638}} 16. ^{{Cite web|url=https://www.immunology.org/|title=British Society for Immunology {{!}}|website=www.immunology.org|access-date=2019-02-16}} 17. ^{{Cite web|url=http://ukcelladhesion.org/|title=ukcelladhesion|access-date=2019-02-16}} 10 : Fellows of the Academy of Medical Sciences|British immunologists|British women scientists|21st-century British scientists|Year of birth missing (living people)|Living people|Women immunologists|21st-century women scientists|Alumni of the University of London|University of Toronto alumni |
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