Datasets:
princeton-nlp
/
datasets-for-simcse

Dataset card Data Studio Files Community
text
stringlengths
1
2.56k
"Pioneer"s wreck sits below sea level, at , approximately east of Vaucluse.
The wreck lies with the bow towards the south-east, and is intact in places, with structures rising up to from the sea floor.
Following a reorganisation of the RAN battle honours system, completed in March 2010, "Pioneer" was retroactively awarded the honour "German East Africa 1915–16" in recognition of her wartime service.
Council of Science Editors
The Council of Science Editors ("CSE", former Council of Biology Editors, "CBE") is a United States–based nonprofit organization that supports editorial practice among scientific writers.
In 2008, the CSE adopted the slogan "CSE: Education, Ethics, and Evidence for Editors (E4)".
A volunteer Board of Directors leads the Council, with the assistance of several committees.
CSE is managed by Kellen Company, located in Wheat Ridge, Colorado.
The organization was established in 1957 by the National Science Foundation and the American Institute of Biological Sciences as the Council of Biology Editors (CBE), being renamed the Council of Science Editors, with a broader mission, on January 1, 2000.
The membership of CSE comprises editorial professionals, mainly in the United States.
As well as providing services and advice online, CSE holds an annual meeting that includes short courses on topics such as journal editorship, publication management, manuscript editing, and journal metrics.
The CSE offers guidance on ethics and practice in scientific publishing.
The CSE publishes a style guide for scientific papers, "Scientific Style and Format: The CSE Manual for Authors, Editors, and Publishers", although CSE style is not as widely used as some other scientific styles such as AMA style and APA style.
In 2014, CSE partnered with the University of Chicago Press to use the successful online platform of the "Chicago Manual of Style" (CMOS) (which provides users with search and personal annotation of the manual) to publish "Scientific Style and Format" online.
As of 2014, it is in the 8th edition.
The 7th edition was published in 2006 and the 6th in 1994.
"Science Editor" is the quarterly publication of the CSE; after one year, articles are available as open access (delayed open access).
Robert L. Stewart
Robert Lee Stewart (born August 13, 1942) is a retired brigadier general of the United States Army and a former NASA astronaut.
Stewart was born May 10, 1942, in Washington, D.C.
He graduated from Hattiesburg High School in Hattiesburg, Mississippi in 1960.
He also received a Bachelor of Science degree in Mathematics from the University of Southern Mississippi in 1964, and a Master of Science degree in Aerospace Engineering from the University of Texas at Arlington in 1972.
Stewart is married and has two children.
His interests include woodworking, photography, and skiing.
Stewart entered on active duty with the United States Army in May 1964 and was assigned as an air defense artillery director at the 32nd NORAD Region Headquarters (SAGE), Gunter Air Force Base, Alabama.
In July 1966, after completing rotary wing training at Fort Wolters, Texas, and Fort Rucker, Alabama, he was designated an Army Aviator.
He flew 1,035 hours of combat time from August 1966 to 1967, primarily as a fire team leader in the armed helicopter platoon of "A" Company, 101st Aviation Battalion (redesignated 336th Assault Helicopter Company).
He was an instructor pilot at the U.S. Army Primary Helicopter School — serving one year in the pre-solo/primary-1 phase of instruction and about 6 months as commander of methods of instruction flight III, training rated aviators to become instructor pilots.
He is a graduate of the U.S. Army's Air Defense Artillery School's Air Defense Officers Advanced Course and Guided Missile Systems Officers Course.
Stewart served in Seoul, Korea, from 1972 to 1973, with the 309th Aviation Battalion (Combat) as a battalion operations officer and battalion executive officer.
He next attended the U.S.
Naval Test Pilot School at NAS Patuxent River, Maryland, completing the Rotary Wing Test Pilot Course in 1974, and was then assigned as an experimental test pilot to the U.S. Army Aviation Engineering Flight Activity at Edwards Air Force Base, California.
His duties there included chief of the integrated systems test division, as well as participating in engineering flight tests of UH-1 and AH-1 helicopters and U-21 and OV-1 fixed wing aircraft, serving as project officer and senior test pilot on the Hughes YAH-64 advanced attack helicopter during government competitive testing; and participation with Sikorsky Aircraft Corporation test pilots in developing an electronic automatic flight control system for the new Army transport helicopter — the UH-60A Black Hawk.
He has military and civilian experience in 38 types of airplanes and helicopters and logged approximately 6,000 hours total flight time.
Stewart became a NASA astronaut in August 1979.
His technical duties in the Astronaut Office included: testing and evaluation of the entry flight control systems for STS-1 (the first Space Shuttle orbital mission), ascent abort procedures development, and payload coordination.
He also served as support crewman for STS-4, and Ascent/Orbit CAPCOM for STS-5.
He served as a mission specialist on STS-41-B in 1984 and STS-51-J in 1985, and logged a total of 289 hours in space, including approximately 12 hours of EVA operations.
Although astronauts who had served in the United States Army Air Forces during World War II (including Gus Grissom and Deke Slayton) had previously flown, Stewart was the first active-duty Army officer to make a spaceflight.
While in training for his scheduled third flight (STS-61-K, ultimately cancelled as a result of the "Challenger" disaster) in 1986, Stewart was selected by the Army for promotion to Brigadier General.
Upon accepting this promotion, Stewart was reassigned from NASA to be the Deputy Commanding General, U.S. Army Strategic Defense Command, in Huntsville, Alabama.
In this capacity, Stewart managed research efforts in developing ballistic missile defense technology.
He was reassigned as Director of Plans, United States Space Command, Colorado Springs, Colorado, in 1989.
STS-41-B "Challenger" (February 3–11, 1984) was launched from Kennedy Space Center, Florida, and returned to land there 8 days later.
During the mission, Stewart and fellow astronaut Bruce McCandless participated in two extravehicular activities (EVAs) to conduct first flight evaluations of the Manned Maneuvering Units (MMUs).
These EVAs represented man's first untethered operations from a spacecraft in flight.
Upon completion of this mission Stewart became the first Army officer awarded the Army Astronaut Badge.
Stewart first EVA, together with Bruce McCandless lasted 6 hours and 17 minutes.
During second EVA, Stewart used the MMU for an untethered spacewalk, lasted 5 hours and 55 minutes.
STS-51-J "Atlantis" (October 3–7, 1985) was launched from Kennedy Space Center, Florida, and after 98 hours of orbital operations returned to land at Edwards Air Force Base, California.
It was the second Space Shuttle Department of Defense mission, and the maiden voyage of "Atlantis".
During the mission he was responsible for a number of on-orbit activities.
Stewart retired from the Army in 1992 and made his home in Woodland Park, Colorado for many years.
He was employed as Director of Advanced Programs at the Nichols Research Corporation in Colorado Springs, Colorado, before retiring.
He later moved to Huntsville, Alabama, where he currently resides.
He makes daily appearances at the U.S. Space & Rocket Center, greeting visitors and signing autographs.
He has been a member of the Society of Experimental Test Pilots, Association of Space Explorers, Phi Eta Sigma, and the Scabbard and Blade (a military honor society).
Phosphatase
A phosphatase is an enzyme that uses water to cleave a phosphoric acid monoester into a phosphate ion and an alcohol.
Because a phosphatase enzyme catalyzes the hydrolysis of its substrate, it is a subcategory of hydrolases.
Phosphatase enzymes are essential to many biological functions, because phosphorylation (e.g.
by protein kinases) and dephosphorylation (by phosphatases) serve diverse roles in cellular regulation and signaling.
Whereas phosphatases remove phosphate groups from molecules, kinases catalyze the transfer of phosphate groups to molecules from ATP.
Together, kinases and phosphatases direct a form of post-translational modification that is essential to the cell's regulatory network.
Phosphatase enzymes are not to be confused with phosphorylase enzymes, which catalyze the transfer of a phosphate group from hydrogen phosphate to an acceptor.
Due to their prevalence in cellular regulation, phosphatases are an area of interest for pharmaceutical research.
Phosphatases catalyze the hydrolysis of a phosphomonoester, removing a phosphate moiety from the substrate.
Water is split in the reaction, with the -OH group attaching to the phosphate ion, and the H+ protonating the hydroxyl group of the other product.
The net result of the reaction is the destruction of a phosphomonoester and the creation of both a phosphate ion and a molecule with a free hydroxyl group.
Phosphatases are able to dephosphorylate seemingly different sites on their substrates with great specificity.
Identifying the "phosphatase code," that is, the mechanisms and rules that govern substrate recognition for phosphatases, is still a work in progress, but the first comparative analysis of all the protein phosphatases encoded across nine eukaryotic 'phosphatome' genomes is now available.
Studies reveal that so called "docking interactions" play a significant role in substrate binding.
A phosphatase recognizes and interacts with various motifs (elements of secondary structure) on its substrate; these motifs bind with low affinity to docking sites on the phosphatase, which are not contained within its active site.
Although each individual docking interaction is weak, many interactions occur simultaneously, conferring a cumulative effect on binding specificity.
Docking interactions can also allosterically regulate phosphatases and thus influence their catalytic activity.
In contrast to kinases, phosphatase enzymes recognize and catalyze a wider array of substrates and reactions.
For example, in humans, Ser/Thr kinases outnumber Ser/Thr phosphatases by a factor of ten.
To some extent, this disparity results from incomplete knowledge of the human phosphatome, that is, the complete set of phosphatases expressed in a cell, tissue, or organism.
Many phosphatases have yet to be discovered, and for numerous known phosphatases, a substrate has yet to be identified.
However, among well-studied phosphatase/kinase pairs, phosphatases exhibit greater variety than their kinase counterparts in both form and function; this may result from the lesser degree of conservation among phosphatases.
A protein phosphatase is an enzyme that dephosphorylates an amino acid residue of its protein substrate.
Whereas protein kinases act as signaling molecules by phosphorylating proteins, phosphatases remove the phosphate group, which is essential if the system of intracellular signaling is to be able to reset for future use.
The tandem work of kinases and phosphatases constitute a significant element of the cell’s regulatory network.
Phosphorylation (and dephosphorylation) is among the most common modes of posttranslational modification in proteins, and it is estimated that, at any given time, up to 30% of all proteins are phosphorylated.
Two notable protein phosphatases are PP2A and PP2B.
PP2A is involved in multiple regulatory processes, such as DNA replication, metabolism, transcription, and development.
PP2B, also called calcineurin, is involved in the proliferation of T cells; because of this, it is the target of some drugs that seek to suppress the immune system.
A nucleotidase is an enzyme that catalyzes the hydrolysis of a nucleotide, forming a nucleoside and a phosphate ion.
Nucleotidases are essential for cellular homeostasis, because they are partially responsible for maintaining a balanced ratio of nucleotides to nucleosides.
Some nucleotidases function outside the cell, creating nucleosides that can be transported into the cell and used to regenerate nucleotides via salvage pathways.
Inside the cell, nucleotidases may help to maintain energy levels under stress conditions.
A cell deprived of oxygen and nutrients may catabolize more nucleotides to boost levels of nucleoside triphosphates such as ATP, the primary energy currency of the cell.
Phosphatases can also act on carbohydrates, such as intermediates in gluconeogenesis.
Gluconeogenesis is a biosynthetic pathway wherein glucose is created from noncarbohydrate precursors; the pathway is essential because many tissues can only derive energy from glucose.
Two phosphatases, glucose-6-phosphatase and fructose-1,6-bisphosphatase, catalyze irreversible steps in gluconeogenesis.
Each cleaves a phosphate group from a six-carbon sugar phosphate intermediate.
Within the larger class of phosphatase, the Enzyme Commission recognizes 104 distinct enzyme families.
Phosphatases are classified by substrate specificity and sequence homology in catalytic domains.
Despite their classification into over one hundred families, all phosphatases still catalyze the same general hydrolysis reaction.
In in-vitro experiments, phosphatase enzymes seem to recognize many different substrates, and one substrate may be recognized by many different phosphatases.