L.R. Wright | AMiner学者主页

全面呈现 [L.R. Wright] 的学术影响力

深度挖掘高质量成果与权威引用，让优秀看得见

研究兴趣

暂无数据

论文（6）

专利

基金项目

按年份排序按引用量排序主题筛选期刊级别筛选合作者筛选合作机构筛选

1Stress and Nursing in the Pig: Role of HPA Axis and Endogenous Opioid Peptides

J RUSHEN,TS NAY,LR WRIGHT,DC PAYNE,GR FOXCROFT

To determine the effect of stress on nursing, and the roles of HPA activity and opioid peptides, nine sows had their piglets removed for 2 h and were treated as follows: (a) control; (b) nose-snare restraint for 20 min; (c) naloxone injections (IV 2 mg/kg); and (d) snare + naloxone. After the treatment, the piglets were returned, milk ejections were timed, and the sows' blood sampled every 10 min for cortisol, growth hormone (GH), and prolactin assays. Piglet removal increased cortisol and decreased prolactin and GH. This was reversed when the piglets were returned. Restraint increased cortisol and decreased GH, but did not affect prolactin. Naloxone alone increased cortisol and decreased GH but did not increase the effect of restraint. The rise in GH following the piglets' return was abolished by the combination of restraint and naloxone. Neither restraint nor naloxone delayed the latency to first milk ejection or reduced the frequency. No unsuccessful nursings were observed. First milk ejections occurred when cortisol levels were elevated. Stress-induced activity of the hypothalamo-pituitary-adrenocortical (HPA) axis does not inhibit milk ejection in the pig, but this is not due to a protective opioid action. Endogenous opioids protect lactogenic hormones against inhibition by stress.

1995PHYSIOLOGY & BEHAVIOR（1995）引用：22

引用

AI阅读

2Ab Initio SCF Studies of the Peptides Gly-Gly, Gly-Ala, Ala-Gly, and Gly-Gly-Gly

LR WRIGHT,RF BORKMAN

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTAb initio SCF studies of the peptides Gly-Gly, Gly-Ala, Ala-Gly, and Gly-Gly-GlyLance R. Wright and Raymond F. BorkmanCite this: J. Phys. Chem. 1982, 86, 20, 3956–3962Publication Date (Print):September 1, 1982Publication History Published online1 May 2002Published inissue 1 September 1982https://pubs.acs.org/doi/10.1021/j100217a015https://doi.org/10.1021/j100217a015research-articleACS PublicationsRequest reuse permissionsArticle Views122Altmetric-Citations32LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access options Get e-Alerts

1982JOURNAL OF PHYSICAL CHEMISTRY（1982）引用：54

引用

AI阅读

3A B I N I T I O Studies on the Stabilities of Even- and Odd-Membered Hn+ Clusters

LR WRIGHT,RF BORKMAN

A b initio SCF and SD–CI calculations have been performed for the hydrogen positive ion clusters Hn+ with n = 3–9. The optimum structures of the clusters were all determined to consist of a nearly equilateral H3+ core surrounded by neutral H and/or H2 ligands at the apices. The most interesting new finding is that the even-membered clusters with n = 4, 6, 8 have binding energies comparable to the odd-membered clusters with n = 5, 7, 9. This result is striking since the odd-membered clusters have been observed in a number of previous experiments; whereas no even-membered H+n clusters have ever been observed experimentally. The conclusion appears to be that kinetic (but not thermodynamic) factors preclude formation of H+4, and other even-membered hydrogen ion clusters, in experiments performed to date. Our best calculations indicate that H4+ is stable by at least 5 kcal/mol relative to H3++H. The other Hn+ species studied have probable binding energies in the range 3–7 kcal/mol.

1982JOURNAL OF CHEMICAL PHYSICS（1982）引用：81

引用

AI阅读

4Energetics and Possible Mechanisms of Ion-Beam Protein Tritiation Based on AB Initio Potential Surfaces.

RF BORKMAN,LR WRIGHT,TF MORAN

Ab initio self-consistent field potential energy surfaces for the approach of T, T2, T+, T3+ and HeT+ to glycine in the gas phase have been determined and this data used to obtain insight into mechanisms of experimental ion-beam protein tritiation processes. Results of these calculations show that the ionic species T+, T3+ and HeT+ can form stable adducts with glycine (Gly) and that each functions as a tritiation agent forming the complex GlyT+. Neutral T and T2 experience a purely repulsive interaction with Gly and do not form an intermediate complex. These neutral species are expected to be less effective tritiation agents than the respective ions, in agreement with experimental observations. The fate of the stable GlyT+ complex is discussed and it is proposed that this species is neutralized by electron capture to give GlyT which spontaneously dissociates to either Gly+T or tritiated glycine (Gly*)+H, with the latter reaction product channel favored statistically. The most likely site of exchange is predicted to be at the amine nitrogen although significance exchange is expected to occur at the alpha-carbon site by a somewhat more complex reaction mechanism.

1982Biophysical Chemistry（1982）引用：8

引用

AI阅读

5Abinitio Scf Calculations On Small Amino-Acids And Dipeptides

Lr Wright,Rf Borkman

1981ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY（1981）

引用

AI阅读

6Abinitio Self-Consistent Field Calculations on Some Small Amino-Acids

LR WRIGHT,RF BORKMAN

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTAb initio self-consistent field calculations on some small amino acidsLance R. Wright and Raymond R. BorkmanCite this: J. Am. Chem. Soc. 1980, 102, 20, 6207–6210Publication Date (Print):September 1, 1980Publication History Published online1 May 2002Published inissue 1 September 1980https://doi.org/10.1021/ja00540a006RIGHTS & PERMISSIONSArticle Views192Altmetric-Citations56LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InReddit PDF (534 KB) Get e-Alerts Get e-Alerts

1980JOURNAL OF THE AMERICAN CHEMICAL SOCIETY（1980）引用：87

引用

AI阅读